3.A.1 The ATP-binding Cassette (ABC) Superfamily

The ABC superfamily contains both uptake and efflux transport systems, and the members of these two porter groups generally cluster loosely together with just a few exceptions (Saurin et al., 1999). ATP hydrolysis without protein phosphorylation energizes transport. There are dozens of families within the ABC superfamily, and family generally correlates with substrate specificity. However there are exceptions. The high resolution X-ray structures of several ABC transporters, both uptake and efflux systems, have been determined, and specific details of the transport mechanisms have been proposed (Davidson and Maloney, 2007; Lee et al., 2007).

The porters of the ABC superfamily consist of two integral membrane domains/proteins and two cytoplasmic domains/proteins. The uptake systems (but not the efflux systems) additionally possess extracytoplasmic solute-binding receptors (one or more per system) which in Gram-negative bacteria is found in the periplasm, and in Gram-positive bacteria is present either as a lipoprotein, tethered to the external surface of the cytoplasmic membrane, or as a cell surface-associated protein, bound to the external membrane surface via electrostatic interactions. For those systems with two or more extracytoplasmic solute binding receptors, the receptors may interact in a cooperative fashion (Biemans-Oldehinkel and Poolman, 2003). Both the integral membrane channel constituent(s) and the cytoplasmic ATP-hydrolyzing constituent(s) may be present as homodimers or heterodimers. Two families of ABC transporters have members in which one or two receptors are fused to either the N- or C-terminus of the translocating membrane protein. This suggests that two or even four substrate-binding sites may function in the complex. Possibly multiple receptors in proximity to the translocator enhances the transport rate. Multiple receptors may also broaden the substrate specificity of the system (van der Heide and Poolman, 2002). These systems with covalent receptor domains linked to the transmembrane translocators are found in the PAAT family (TC #3.A.1.3) and the QAT family (TC #3.A.1.12) (van der Heide and Poolman, 2002).

The homodimeric LmrA drug efflux pump (TC #3.A.1.117.1) of Lactococcus lactis appears to function by an alternating site (half of sites) type mechanism. In many of these porters, the various domains are fused in a variety of combinations. Uptake porters generally have their constituents as distinct polypeptide chains, while efflux systems usually have them fused. ABC-type uptake systems have not been identified in eukaryotes, but ABC-type efflux systems abound in both prokaryotes and eukaryotes. The eukaryotic efflux systems often have the four domains (two cytoplasmic domains and two integral membrane domains) fused into either one or two polypeptide chains. The integral membrane porter domains each usually possesses 5 (uptake) or 6 (efflux) transmembrane spanners, but exceptions exist. For example, the MntB protein (TC #3.A.1.15.1) exhibits 9 established TMSs. The 3-dimensional structure of the E. coli MsbA protein (TC #3.A.1.106.1) has been solved to a resolution of 3.7 Å (Ward et al., 2007), that of the Staphylococcus aureus Sav1866 protein (TC #3.A.1.106.2) has been solved to a resolution of 3.0 Å (Dawson and Locher, 2006), that of the Archaeoglobus fulgidus ModABC complex has been solved at 3.1 Å resolution (Hollenstein et al., 2007), that of the E. coli BtuCDF Vitamin B12 transporter was solved at 2.6 Å resolution (Hvorup et al., 2007), and the maltose transporter has been solved at 2.8 Å resolution (Oldham et al., 2007). These structures are very different, but the two transmembrane domains form a single barrel 5-6 nm in diameter and about 5 nm deep with an entral pore open either to the external or internal surface spanning much of the membrane (Rosenberg et al., 2003). A model has been proposed allowing the channel to open up to the lipid bilayer. A half of sites model in which the two nucleotide binding domains interact in a fashion controlled by substrate binding has also been proposed (Hou et al., 2003; Loo et al., 2003).

Hollenstein et al. (2007) presented the 3.1 Å crystal structure of a putative molybdate transporter (ModB2C2) from Archaeoglobus fulgidus in complex with its binding protein (ModA). Twelve transmembrane helices of the ModB subunits provide an inward-facing conformation, with a closed gate near the external membrane boundary. The ATP-hydrolyzing ModC subunits reveal a nucleotide-free, open conformation, whereas the attached binding protein aligns the substrate-binding cleft with the entrance to the presumed translocation pathway. Structural comparison of ModB2C2A with Sav1866 suggests a common alternating access and release mechanism, with binding of ATP promoting an outward-facing conformation and dissociation of the hydrolysis products promoting an inward-facing conformation.

Smriti et al., 2009 mapped residues proximal to the daunorubicin (DNR)-binding site in MsbA (TC#3.A.1.106.1) using site-specific, ATP-dependent quenching of DNR intrinsic fluorescence by spin labels. In the nucleotide-free MsbA intermediate, DNR-binding residues cluster at the cytoplasmic end of helices 3 and 6 at a site accessible from the membrane/water interface and extending into an aqueous chamber formed at the interface between the two transmembrane domains. Binding of a nonhydrolyzable ATP analog inverts the transporter to an outward-facing conformation. DNR may thus enter near an elbow helix parallel to the water/membrane interface, partitioning into the open chamber, and then translocating toward the periplasm upon ATP binding.

The turnover rates of some transporters are inhibited by their substrates in a process termed trans-inhibition. Gerber et al. (2008) presented the crystal structure of a molybdate/tungstate ABC transporter (ModBC) from Methanosarcina acetivorans in a trans-inhibited state. The regulatory domains of the nucleotide-binding subunits proved to be in close contact, providing two oxyanion binding pockets at the shared interface. By specifically binding to these pockets, molybdate or tungstate prevent adenosine triphosphatase activity and lock the transporter in an inward-facing conformation, with the catalytic motifs of the nucleotide-binding domains separated. This allosteric effect prevents the transporter from switching between the inward-facing and the outward-facing states, thus interfering with the alternating access and release mechanism.

The cystic fibrosis transmembrane conductance regulator (CFTR; 3.A.1.202.1) is an ATP-dependent chloride channel. Jordan et al., 2008 compared CFTR protein sequences to those of ABCC4 proteins (the closest mammalian paralogs) to identify the evolutionary transition from transporter to channel activity. R352 in the sixth transmembrane helix interacts with D993 in TM9 to stabilize the open-channel state; D993 is absolutely conserved between CFTRs and ABCC4s. Thus CFTR channel activity evolved, at least in part, by converting the conformational changes associated with binding and hydrolysis of ATP, as are found in true ABC transporters, into an open permeation pathway by means of intraprotein interactions that stabilize the open state.

The LolCDE complex of Escherichia coli (TC# 3.A.1.125.1) initiates the lipoprotein sorting to the outer membrane by catalysing their release from the inner membrane. LolC and/or LolE, membrane subunits, recognize lipoproteins anchored to the outer surface of the inner membrane, while LolD hydrolyses ATP on its inner surface. The ligand-bound LolCDE has been purified from the inner membrane in the absence of ATP (Ito et al., 2006). Liganded LolCDE represents an intermediate of the release reaction and exhibits higher affinity for ATP than the unliganded form. ATP binding to LolD weakens the interaction between LolCDE and lipoproteins and causes their dissociation in a detergent solution, while lipoprotein release from membranes requires ATP hydrolysis. A single molecule of lipoprotein is found to bind per molecule of the LolCDE complex.

The three structurally dissimilar constituents of the ABC uptake porters have generally arisen from a common ancestral porter system with minimal shuffling of constituents between/domain constituents is almost always the same. However the rates of sequence divergences differ drastically with the extracytoplasmic solute-binding receptors diverging most rapidly, the integral-membrane, channel-forming constituents diverging at an intermediate rate, and the cytoplasmic ATP-hydrolyzing constituents diverging most slowly. Thus, all ATP-hydrolyzing constituents are demonstrably homologous, but this is not true for the integral membrane constituents or the receptors. Nevertheless, clustering patterns are generally the same for all three types of proteins, and 3-dimensional structural data suggest that, in spite of their extensive sequence divergence, the extracytoplasmic solute-binding receptors are homologous to each other.

Unlike most of the known ABC transporters, ABCC1 (TC #3.A.1.208.8) has an additional membrane-spanning domain (MSD) at its amino terminus with a domain arrangement of MSD0-MSD1-NBD1-MSD2-NBD2. The additional MSD0 domain consists of five putative transmembrane segments with a predicted extracellular amino terminus. It has a U-shaped folding with the bottom of the U-structure facing cytoplasm and both ends in extracellular space. This U-shaped amino terminus probably functions as a gate to regulate the drug transport activity of human ABCC1 (Chen et al., 2006).

Polar lipid trafficking is essential in eukaryotic cells as membranes of lipid assembly are often distinct from final destination membranes. A striking example is the biogenesis of the photosynthetic membranes (thylakoids) in plastids of plants. Lipid biosynthetic enzymes at the endoplasmic reticulum and the inner and outer plastid envelope membranes are involved. This compartmentalization requires extensive lipid trafficking. Mutants of Arabidopsis disrupt the incorporation of endoplasmic reticulum-derived lipid precursors into thylakoid lipids. Two proteins affected in two of these mutants, trigalactosyldiacylglycerol 1 (TGD1) and TGD2, encode the permease and substrate binding component, respectively, of a proposed lipid translocator at the inner chloroplast envelope membrane. A third protein, TGD3, a small ABC-type ATPase, energizer transport. As in the tgd1 and tgd2 mutants, triacylglycerols and trigalactolipids accumulate in a tgd3 mutant. The TGD3 protein shows basal ATPase activity and is localized inside the chloroplast beyond the inner chloroplast envelope membrane. Proteins orthologous to TGD1, -2, and -3 are predicted to be present in Gram-negative bacteria, and the respective genes are organized in operons suggesting a common biochemical role for the gene products. The Tgd1,2,3 system (TC#3.A.1.27.2) probably transfers ER-derived lipids to the thylakoid membrane (Lu et al., 2007). It is one of the few known eukaryotic uptake systems.

Some transporters have a conserved transmembrane protein and two nucleotide binding proteins similar to those of ABC transporters. However, unlike typical ABC transporters (E.I. Sun & M.H. Saier, unpublished results), they use small integral membrane proteins that are postulated to capture specific substrates. Our studies have shown that both of these integral membrane protein constituents of these systems are distantly related but homologous, and in this respect they resemble typical ABC porters. We postulate that these two transmembrane proteins comprise the pathway for transmembrane transport.

Rodionov et al., 2009 identified 21 families of these substrate capture proteins, each with a different specificity predicted by genome context analyses. Roughly half of the substrate capture proteins (335 cases) examined by Rodionov et al., 2009 have a dedicated energizing module, but in 459 cases distributed among almost 100 gram-positive bacteria, different and unrelated substrate capture proteins share the same energy-coupling module. The shared use of energy-coupling modules was experimentally confirmed for folate, thiamine, and riboflavin transporters. Rodionov et al., 2009 proposed the name energy-coupling factor transporters for the new class of putative ABC membrane transporters. These membrane proteins are homologues to ABC-2 exporters. When evidence is minimal for association with an ABC-type ATP-hydrolyzing subunit, these porters are placed in category 2.A (secondary carriers; e.g., 2.A.88).

The uptake porters of the ABC superfamily and of the vitamin/small molecule transporters described by Rodionov et al., 2009 are homologous to the porters in the VUT family (2.A.88). In fact, our studies indicated that all uptake porters of the ABC superfamily are of the ABC2 type. When evidence suggests that homologous membrane transport proteins of the ABC2 type couple transport to ATP hydrolysis using a homologue of the ABC-type ATPases, we list these proteins in the ABC superfamily. If there is no such evidence, (e.g., experimental evidence and the occurrence of the gene for the membrane transporter protein is in an operon that lacks the ATPase and auxillary subunit) then the porter is placed into family 2.A.88.

Dassa and Bouige (2001) have devised a phylogenetic/functional classification system for ABC transporters that overlaps the TC system. In their system, several of the TC families are included in single families. These reveal the closer phylogenetic relationship of TC families as follows:

Table 1
D&B Family TC Families
Uptake
MOI SulT, + PhoT + MolT + FeT + POPT + ThiT
OTCN QAT + NitT + TauT
ISVH VB12 + FeCT
Export
DPL Lipid E + Glucan E + Prot1E + Prot2E + Pep1E + Pep2E + Pep3E + DrugE2 + DrugE3 + MDR + CFTR + Ste + TAP + HMT + MPE
OAD CT1 + CT2
EPD EPP + PDR
DRA DrugE1 + CPR
DRI NatE
CLS CPSE + LPSE + TAE

Dassa and Bouige (2001) also provide the protein and domain organization of each of the various family-type proteins (see Table 1).

The generalized transport reaction for ABC-type uptake systems is:

Solute (out) + ATP → Solute (in) + ADP + Pi.

The generalized transport reaction for ABC-type efflux systems is:

Substrate (in) + ATP → Substrate (out) + ADP + Pi.

Macromolecular structures of proteins in this family:

3.A.1.1.1 - 1ANF
3.A.1.1.1 - 4MBP
3.A.1.1.1 - 3MBP
3.A.1.106.1 - 1JSQ
3.A.1.106.1 - 1PF4
3.A.1.13.1 - 1L7V
3.A.1.13.1 - 1N2Z

 

References:

Abele, R. and R. Tampé. (1999). Function of the transport complex TAP in cellular immune recognition. Biochim. Biophys. Acta. 1461: 405-419.
Agarwal, S., D.W. Hunnicutt, and M.J. McBride. (1997). Cloning and characterization of the Flavobacterium johnsoniae (Cytophaga johnsonae) gliding motility gene, gldA. Proc. Natl. Acad. Sci. USA 94: 12139-12144.
Aguilar-Bryan, L. and J. Bryan. (1999). Molecular biology of adenosine triphosphate-sensitive potassium channels. Endocr Rev 20: 101-135.
Agustiandari, H., J. Lubelski, H.B. van den Berg van Saparoea, O.P. Kuipers, and A.J. Driessen. (2008). LmrR is a transcriptional repressor of expression of the multidrug ABC transporter LmrCD in Lactococcus lactis. J. Bacteriol. 190: 759-763.
Akabas, M.H. (2000). Cystic fibrosis transmembrane conductance regulator. Structure and function of an epithelial chloride channel. J. Biol. Chem. 275: 3729-3732.
Akatsuka, H., E. Kawai, K. Omori, and T. Shibatani. (1995). The three genes lipB, lipC, and lipD involved in the extracellular secretion of the Serratia marcescens lipase which lacks an N-terminal signal peptide. J. Bacteriol. 177: 6381-6389.
Alloing, G., I. Travers, B. Sagot, D. Le Rudulier, and L. Dupont. (2006). Proline betaine uptake in Sinorhizobium meliloti: Characterization of Prb, an opp-like ABC transporter regulated by both proline betaine and salinity stress. J. Bacteriol. 188: 6308-6317.
Ammendola, S., P. Pasquali, C. Pistoia, P. Petrucci, P. Petrarca, G. Rotilio, and A. Battistoni. (2007). High-affinity Zn2+ uptake system ZnuABC is required for bacterial zinc homeostasis in intracellular environments and contributes to the virulence of Salmonella enterica. Infect. Immun. 75: 5867-5876.
Anderson, D.S., P. Adhikari, A.J. Nowalk, C.Y. Chen, and T.A. Mietzner. (2004). The hFbpABC transporter from Haemophilus influenzae functions as a binding-protein-dependent ABC transporter with high specificity and affinity for ferric iron. J. Bacteriol. 186: 6220-6229.
Andrade, A.C., G. Del Sorbo, J.G. Van Nistelrooy, and M.A. Waard. (2000). The ABC transporter AtrB from Aspergillus nidulans mediates resistance to all major classes of fungicides and some natural toxic compounds. Microbiology 146(Pt8): 1987-1997.
Andreesen, J.R. and K. Makdessi. (2008). Tungsten, the surprisingly positively acting heavy metal element for prokaryotes. Ann. N.Y. Acad. Sci. 1125: 215-229.
Anjard, C., W.F. Loomis, and. (2002). Evolutionary analyses of ABC transporters of Dictyostelium discoideum. Eukaryot. Cell. 1: 643-652.
Aranda, R., 4th, C.E. Worley, M. Liu, E. Bitto, M.S. Cates, J.S. Olson, B. Lei, and G.N. Phillips, Jr. (2007). Bis-methionyl coordination in the crystal structure of the heme-binding domain of the streptococcal cell surface protein Shp. J. Mol. Biol. 374: 374-383.
Arends, S.J., R.J. Kustusch, and D.S. Weiss. (2009). ATP-binding site lesions in FtsE impair cell division. J. Bacteriol. 191: 3772-3784.
Assaraf, Y.G. The role of multidrug resistance efflux transporters in antifolate resistance and folate homeostasis. Drug Resist Updat 9: 227-246.
Assaraf, Y.G., I. Ifergan, W.N. Kadry, and R.Y. Pinter. (2006). Computer modelling of antifolate inhibition of folate metabolism using hybrid functional petri nets. J Theor Biol 240: 637-647.
Awram, P. and J. Smit. (1998). The Caulobacter crescentus paracrystalline S-layer protein is secreted by an ABC transporter (type I) secretion apparatus. J. Bacteriol. 180: 3062-3069.
Börnke, F., M. Hajirezaei, and U. Sonnewald. (2001). Cloning and characterization of the gene cluster for palatinose metabolism from the phytopathogenic bacterium Erwinia rhapontici. J. Bacteriol. 183: 2425-2430.
Balzi, E., M. Wang, S. Leterme, L. Van Dyck, and A. Goffeau. (1994). PDR5, a novel yeast multidrug resistance conferring transporter controlled by the transcription regulator PDR1. J. Biol. Chem. 269: 2206-2214.
Ban, N., Y. Matsumura, H. Sakai, Y. Takanezawa, M. Sasaki, H. Arai, and N. Inagaki. (2007). ABCA3 as a lipid transporter in pulmonary surfactant biogenesis. J. Biol. Chem. 282: 9628-9634.
Barona-Gómez, F., S. Lautru, F.X. Francou, P. Leblond, J.L. Pernodet, and G.L. Challis. (2006). Multiple biosynthetic and uptake systems mediate siderophore-dependent iron acquisition in Streptomyces coelicolor A3(2) and Streptomyces ambofaciens ATCC 23877. Microbiology 152: 3355-3366.
Barrangou, R., E. Altermann, R. Hutkins, R. Cano, and T.R. Klaenhammer. (2003). Functional and comparative genomic analyses of an operon involved in fructooligosaccharide utilization by Lactobacillus acidophilus. Proc. Natl. Acad. Sci. USA 100: 8957-8962.
Bartsevich, V.V. and H.B. Pakrasi. (1999). Membrane topology of MntB, the transmembrane protein component of an ABC transporter system for manganese in the cyanobacterium Synechocystis sp. strain PCC 6803. J. Bacteriol. 181: 3591-3593.
Bauer, B.E., H. Wolfger, and K. Kuchler. (1999). Inventory and function of yeast ABC proteins: about sex, stress, pleiotropic drug and heavy metal resistance. Biochim. Biophys. Acta. 1461: 217-236.
Bearden, S.W. and R.D. Perry. (1999). The Yfe system of Yersinia pestis transports iron and manganese and is required for full virulence of plague. Mol. Microbiol. 32: 403-414.
Beasley, F.C., E.D. Vinés, J.C. Grigg, Q. Zheng, S. Liu, G.A. Lajoie, M.E. Murphy, and D.E. Heinrichs. (2009). Characterization of staphyloferrin A biosynthetic and transport mutants in Staphylococcus aureus. Mol. Microbiol. 72: 947-963.
Becker, P., R. Hakenbeck, and B. Henrich. (2009). An ABC transporter of Streptococcus pneumoniae involved in susceptibility to vancoresmycin and bacitracin. Antimicrob. Agents Chemother. 53: 2034-2041.
Beckers, G., A.K. Bendt, R. Krämer, and A. Burkovski. (2004). Molecular identification of the urea uptake system and transcriptional analysis of urea transporter- and urease-encoding genes in Corynebacterium glutamicum. J. Bacteriol. 186: 7645-7652.
Bellamy, W.T. (1996). P-glycoproteins and multidrug resistance. Annu Rev Pharmacol Toxicol 36: 161-183.
Bernard, R., A. Guiseppi, M. Chippaux, M. Foglino, and F. Denizot. (2007). Resistance to bacitracin in Bacillus subtilis: unexpected requirement of the BceAB ABC transporter in the control of expression of its own structural genes. J. Bacteriol. 189: 8636-8642.
Berntsson, R.P., M.K. Doeven, F. Fusetti, R.H. Duurkens, D. Sengupta, S.J. Marrink, A.M. Thunnissen, B. Poolman, and D.J. Slotboom. (2009). The structural basis for peptide selection by the transport receptor OppA. EMBO. J. 28: 1332-1340.
Bevers, L.E., P.L. Hagedoorn, G.C. Krijger, and W.R. Hagen. (2006). Tungsten transport protein A (WtpA) in Pyrococcus furiosus: the first member of a new class of tungstate and molybdate transporters. J. Bacteriol. 188: 6498-6505.
Bieler, S., F. Silva, C. Soto, and D. Belin. (2006). Bactericidal activity of both secreted and nonsecreted microcin E492 requires the mannose permease. J. Bacteriol. 188: 7049-7061.
Biemans-Oldehinkel, E. and B. Poolman. (2003). On the role of the two extracytoplasmic substrate-binding domains in the ABC transporter OpuA. EMBO. J. 22: 5983-5993.
Biemans-Oldehinkel, E., N.A. Mahmood, and B. Poolman. (2006). A sensor for intracellular ionic strength. Proc. Natl. Acad. Sci. USA 103: 10624-10629.
Binet, R., S. Létoffé, J.M. Ghigo, P. Delepelaire, and C. Wandersman. (1997). Protein secretion by Gram-negative bacterial ABC exporters--a review. Gene 192: 7-11.
Bird, D., F. Beisson, A. Brigham, J. Shin, S. Greer, R. Jetter, L. Kunst, X. Wu, A. Yephremov, and L. Samuels. (2007). Characterization of Arabidopsis ABCG11/WBC11, an ATP binding cassette (ABC) transporter that is required for cuticular lipid secretion. Plant J. 52: 485-498.
Borst, P. and R.O. Elferink. (2002). Mammalian ABC transporters in health and disease. Annu. Rev. Biochem. 71: 537-592.
Borst, P., R. Evers, M. Kool, and J. Wijnholds. (1999). The multidrug resistance protein family. Biochim. Biophys. Acta. 1461: 347-357.
BoseDasgupta, S., A. Ganguly, A. Roy, T. Mukherjee, and H.K. Majumder. (2008). A novel ATP-binding cassette transporter, ABCG6 is involved in chemoresistance of Leishmania. Mol Biochem Parasitol 158: 176-188.
Bossé, J.T., H.D. Gilmour, and J.I. MacInnes. (2001). Novel genes affecting urease acivity in Actinobacillus pleuropneumoniae. J. Bacteriol. 183: 1242-1247.
Bouchard, R., A. Bailly, J.J. Blakeslee, S.C. Oehring, V. Vincenzetti, O.R. Lee, I. Paponov, K. Palme, S. Mancuso, A.S. Murphy, B. Schulz, and M. Geisler. (2006). Immunophilin-like TWISTED DWARF1 modulates auxin efflux activities of Arabidopsis P-glycoproteins. J. Biol. Chem. 281: 30603-30612.
Braibant, M., P. Gilot, and J. Content. (2000). The ATP binding cassette (ABC) transport systems of Mycobacterium tuberculosis. FEMS Microbiol. Rev. 24: 449-467.
Braun, V. and C. Herrmann. (2007). Docking of the periplasmic FecB binding protein to the FecCD transmembrane proteins in the ferric citrate transport system of Escherichia coli. J. Bacteriol. 189: 6913-6918.
Breedveld, P., D. Pluim, G. Cipriani, F. Dahlhaus, M.A. van Eijndhoven, C.J. de Wolf, A. Kuil, J.H. Beijnen, G.L. Scheffer, G. Jansen, P. Borst, and J.H. Schellens. (2007). The effect of low pH on breast cancer resistance protein (ABCG2)-mediated transport of methotrexate, 7-hydroxymethotrexate, methotrexate diglutamate, folic acid, mitoxantrone, topotecan, and resveratrol in in vitro drug transport models. Mol Pharmacol 71: 240-249.
Brem, D., C. Pelludat, A. Rakin, C.A. Jacobi, and J. Heesemann. (2001). Functional analysis of yersiniabactin transport genes of Yersinia enterocolitica. Microbiology 147: 1115-1127.
Bryan, J. and L. Aguilar-Bryan. (1999). Sulfonylurea receptors: ABC transporters that regulate ATP-sensitive K+ channels. Biochim. Biophys. Acta. 1461: 285-303.
Burguière, P., J. Fert, I. Guillouard, S. Auger, A. Danchin, and I. Martin-Verstraete. (2005). Regulation of the Bacillus subtilis ytmI operon, involved in sulfur metabolism. J. Bacteriol. 187: 6019-6030.
Burguière, P., S. Auger, M.F. Hullo, A. Danchin, and I. Martin-Verstraete. (2004). Three different systems participate in L-cystine uptake in Bacillus subtilis. J. Bacteriol. 186: 4875-4884.
Burkhard, K.A. and A. Wilks. (2008). Functional characterization of the Shigella dysenteriae heme ABC transporter. Biochemistry 47: 7977-7979.
Butcher, B.G. and J.D. Helmann. (2006). Identification of Bacillus subtilis sigma-dependent genes that provide intrinsic resistance to antimicrobial compounds produced by Bacilli. Mol. Microbiol. 60: 765-782.
Butcher, B.G., Y.P. Lin, and J.D. Helmann. (2007). The yydFGHIJ operon of Bacillus subtilis encodes a peptide that induces the LiaRS two-component system. J. Bacteriol. 189: 8616-8625.
Cai, S.Y., L. Wang, N. Ballatori, and J.L. Boyer. (2001). Bile salt export pump is highly conserved during vertebrate evolution and its expression is inhibited by PFIC type II mutations. Am. J. Physiol. Gastrointest Liver Physiol 281: G316-322.
Castanys-Muñoz, E., N. Alder-Baerens, T. Pomorski, F. Gamarro, and S. Castanys. (2007). A novel ATP-binding cassette transporter from Leishmania is involved in transport of phosphatidylcholine analogues and resistance to alkyl-phospholipids. Mol. Microbiol. 64: 1141-1153.
Chan, Y.K., W.A. McCormick, and R.J. Watson. (1997). A new nos gene downstream from nosDFY is essential for dissimilatory reduction of nitrous oxide by Rhizobium (Sinorhizobium) meliloti. Microbiology 143(Pt8): 2817-2824.
Chang, G. (2003). Structure of MsbA from Vibrio cholera: a multidrug resistance ABC transporter homolog in a closed conformation. J. Mol. Biol. 330: 419-430.
Chang, G. and C.B. Roth. (2001). Structure of MsbA from E. coli: a homolog of the multidrug resistance ATP binding cassette (ABC) transporters. Science 293: 1793-1800.
Chang, G., C.B. Roth, C.L. Reyes, O. Pornillos, Y.J. Chen, and A.P. Chen. (2006). Retraction. Science 314: 1875.
Chang, H.K., J.J. Dennis, and G.J. Zylstra. (2009). Involvement of Two Transport Systems and a Specific Porin in the Uptake of Phthalate by Burkholderia spp. J. Bacteriol. [Epub: Ahead of Print]
Chater, K.F. and S. Horinouchi. (2003). Signalling early developmental events in two highly diverged Streptomyces species. Mol. Microbiol. 48: 9-15.
Chen, C. and G.A. Beattie. (2007). Characterization of the osmoprotectant transporter OpuC from Pseudomonas syringae and demonstration that cystathionine-β-synthase domains are required for its osmoregulatory function. J. Bacteriol. 189: 6901-6912.
Chen, Q., Y. Yang, L. Li, and J.T. Zhang. (2006). The amino terminus of the human multidrug resistance transporter ABCC1 has a U-shaped folding with a gating function. J. Biol. Chem. 281: 31152-31163.
Chen, S., R. Sánchez-Fernández, E.R. Lyver, A. Dancis, and P.A. Rea. (2007). Functional characterization of AtATM1, AtATM2, and AtATM3, a subfamily of Arabidopsis half-molecule ATP-binding cassette transporters implicated in iron homeostasis. J. Biol. Chem. 282: 21561-21571.
Chen, Y.Y. and R.A. Burne. (2003). Identification and characterization of the nickel uptake system for urease biogenesis in Streptococcus salivarius 57.I. J. Bacteriol. 185: 6773-6779.
Cheng, J., A.A. Guffanti, and T.A. Krulwich. (1997). A two-gene ABC-type transport system that extrudes Na+ in Bacillus subtilis is induced by ethanol or protonophore. Mol. Microbiol. 23: 1107-1120.
Cheong, N., H. Zhang, M. Madesh, M. Zhao, K. Yu, C. Dodia, A.B. Fisher, R.C. Savani, and H. Shuman. (2007). ABCA3 is critical for lamellar body biogenesis in vivo. J. Biol. Chem. 282: 23811-23817.
Chevance, F.F., M. Erhardt, C. Lengsfeld, S.J. Lee, and W. Boos. (2006). Mlc of Thermus thermophilus: a glucose-specific regulator for a glucose/mannose ABC transporter in the absence of the phosphotransferase system. J. Bacteriol. 188: 6561-6571.
Chow, V., G. Nong, and J.F. Preston. (2007). Structure, function, and regulation of the aldouronate utilization gene cluster from Paenibacillus sp. strain JDR-2. J. Bacteriol. 189: 8863-8870.
Christensen, O., E.M. Harvat, L. Thöny-Meyer, S.J. Ferguson, and J.M. Stevens. (2007). Loss of ATP hydrolysis activity by CcmAB results in loss of c-type cytochrome synthesis and incomplete processing of CcmE. FEBS J. 274: 2322-2332.
Conners, S.B., C.I. Montero, D.A. Comfort, K.R. Shockley, M.R. Johnson, S.R. Chhabra, and R.M. Kelly. (2005). An expression-driven approach to the prediction of carbohydrate transport and utilization regulons in the hyperthermophilic bacterium Thermotoga maritima. J. Bacteriol. 187: 7267-7282.
Crouch, M.L., M. Castor, J.E. Karlinsey, T. Kalhorn, and F.C. Fang. (2008). Biosynthesis and IroC-dependent export of the siderophore salmochelin are essential for virulence of Salmonella enterica serovar Typhimurium. Mol. Microbiol. 67: 971-983.
Cruz-Ramos, H., G.M. Cook, G. Wu, M.W. Cleeter, and R.K. Poole. (2004). Membrane topology and mutational analysis of Escherichia coli CydDC, an ABC-type cysteine exporter required for cytochrome assembly. Microbiology 150: 3415-3427.
Cuthbertson, L., M.S. Kimber, and C. Whitfield. (2007). Substrate binding by a bacterial ABC transporter involved in polysaccharide export. Proc. Natl. Acad. Sci. USA 104: 19529-19534.
Dalton, T.L., J.T. Collins, T.C. Barnett, and J.R. Scott. (2006). RscA, a member of the MDR1 family of transporters, is repressed by CovR and required for growth of Streptococcus pyogenes under heat stress. J. Bacteriol. 188: 77-85.
Danilchanka, O., C. Mailaender, and M. Niederweis. (2008). Identification of a novel multidrug efflux pump of Mycobacterium tuberculosis. Antimicrob. Agents Chemother. 52: 2503-2511.
Dassa, E. and P. Bouige. The ABC of ABCS: a phylogenetic and functional classification of ABC systems in living organisms. Res. Microbiol. 152: 211-229.
Davidson, A.L. and P.C. Maloney. (2007). ABC transporters: how small machines do a big job. Trends Microbiol. 15: 448-455.
Davies, B.W. and G.C. Walker. (2007). Disruption of sitA compromises Sinorhizobium meliloti for manganese uptake required for protection against oxidative stress. J. Bacteriol. 189: 2101-2109.
Dawson, R.J. and K.P. Locher. (2006). Structure of a bacterial multidrug ABC transporter. Nature 443: 180-185.
De Costa, D.M., K. Suzuki, and K. Yoshida. (2003). Structural and functional analysis of a putative gene cluster for palatinose transport on the linear chromosome of Agrobacterium tumefaciens MAFF301001. J. Bacteriol. 185: 2369-2373.
de Wet, H., M.G. Rees, K. Shimomura, J. Aittoniemi, A.M. Patch, S.E. Flanagan, S. Ellard, A.T. Hattersley, M.S. Sansom, and F.M. Ashcroft. (2007). Increased ATPase activity produced by mutations at arginine-1380 in nucleotide-binding domain 2 of ABCC8 causes neonatal diabetes. Proc. Natl. Acad. Sci. USA 104: 18988-18992.
Dean, M. and R. Allikmets. (2001). Complete characterization of the human ABC gene family. J. Bioenerg. Biomembr. 33: 475-479.
Decottignies, A. and A. Goffeau. (1997). Complete inventory of the yeast ABC proteins. Nat. Genet. 15: 137-145.
Deeley, R.G., C. Westlake, and S.P. Cole. (2006). Transmembrane transport of endo- and xenobiotics by mammalian ATP-binding cassette multidrug resistance proteins. Physiol. Rev. 86: 849-899.
Deka, R.K., C.A. Brautigam, X.F. Yang, J.S. Blevins, M. Machius, D.R. Tomchick, and M.V. Norgard. (2006). The PnrA (Tp0319; TmpC) lipoprotein represents a new family of bacterial purine nucleoside receptor encoded within an ATP-binding cassette (ABC)-like operon in Treponema pallidum. J. Biol. Chem. 281: 8072-8081.
del Castillo, T., E. Duque, and J.L. Ramos. (2008). A set of activators and repressors control peripheral glucose pathways in Pseudomonas putida to yield a common central intermediate. J. Bacteriol. 190: 2331-2339.
Delgado, M.A., P.A. Vincent, R.N. Farías, and R.A. Salomón. (2005). YojI of Escherichia coli functions as a microcin J25 efflux pump. J. Bacteriol. 187: 3465-3470.
Demirel, O., Z. Waibler, U. Kalinke, F. Grünebach, S. Appel, P. Brossart, A. Hasilik, R. Tampé, and R. Abele. (2007). Identification of a lysosomal peptide transport system induced during dendritic cell development. J. Biol. Chem. 282: 37836-37843.
Diederichs, K., J. Diez, G. Greller, C. Müller, J. Breed, C. Schnell, C. Vonrhein, W. Boos, and W. Welte. (2000). Crystal structure of MalK, the ATPase subunit of the trehalose/maltose ABC transporter of the archaeon Thermococcus litoralis. EMBO. J. 19: 5951-5961.
Dietrich, D., H. Schmuths, C.d.e.M. Lousa, J.M. Baldwin, S.A. Baldwin, A. Baker, F.L. Theodoulou, and M.J. Holdsworth. (2009). Mutations in the Arabidopsis peroxisomal ABC transporter COMATOSE allow differentiation between multiple functions in planta: insights from an allelic series. Mol. Biol. Cell 20: 530-543.
Dintilhac, A., G. Alloing, C. Granadel, and J.P. Claverys. (1997). Competence and virulence of Streptococcus pneumoniae: Adc and PsaA mutants exhibit a requirement for Zn and Mn resulting from inactivation of putative ABC metal permeases. Mol. Microbiol. 25: 727-739.
Doerrler, W.T., M.C. Reedy, and C.R. Raetz. (2001). An Escherichia coli mutant defective in lipid export. J. Biol. Chem. 276: 11461-11464.
Doeven, M.K., G. van den Bogaart, V. Krasnikov, and B. Poolman. (2008). Probing receptor-translocator interactions in the oligopeptide ABC transporter by fluorescence correlation spectroscopy. Biophys. J. 94: 3956-3965.
Doeven, M.K., R. Abele, R. Tampé, and B. Poolman. (2004). The binding specificity of OppA determines the selectivity of the oligopeptide ATP-binding cassette transporter. J. Biol. Chem. 279: 32301-32307.
Domenech, P., H. Kobayashi, K. LeVier, G.C. Walker, and C.E. Barry, 3rd. (2009). BacA, an ABC transporter involved in maintenance of chronic murine infections with Mycobacterium tuberculosis. J. Bacteriol. 191: 477-485.
Duanmu, D., A.R. Miller, K.M. Horken, D.P. Weeks, and M.H. Spalding. (2009). Knockdown of limiting-CO2-induced gene HLA3 decreases HCO3- transport and photosynthetic Ci affinity in Chlamydomonas reinhardtii. Proc. Natl. Acad. Sci. USA 106: 5990-5995.
Dugourd, D., C. Martin, C.R. Rioux, M. Jacques, and J. Harel. (1999). Characterization of a periplasmic ATP-binding cassette iron import system of Brachyspira (Serpulina) hyodysenteriae. J. Bacteriol. 181: 6948-6957.
Dupont, L., I. Garcia, M.C. Poggi, G. Alloing, K. Mandon, and D. Le Rudulier. (2004). The Sinorhizobium meliloti ABC transporter Cho is highly specific for choline and expressed in bacteroids from Medicago sativa nodules. J. Bacteriol. 186: 5988-5996.
Elferink, M.G., S.V. Albers, W.N. Konings, and A.J. Driessen. (2001). Sugar transport in Sulfolobus solfataricus is mediated by two families of binding protein-dependent ABC transporters. Mol. Microbiol. 39: 1494-1503.
Endo, R., Y. Ohtsubo, M. Tsuda, and Y. Nagata. (2007). Identification and characterization of genes encoding a putative ABC-type transporter essential for utilization of γ-hexachlorocyclohexane in Sphingobium japonicum UT26. J. Bacteriol. 189: 3712-3720.
Engelen, M., R. Ofman, P.A. Mooijer, B.T. Poll-The, R.J. Wanders, and S. Kemp. (2008). Cholesterol-deprivation increases mono-unsaturated very long-chain fatty acids in skin fibroblasts from patients with X-linked adrenoleukodystrophy. Biochim. Biophys. Acta. 1781: 105-111.
Espinasse, S., M. Gohar, D. Lereclus, and V. Sanchis. (2002). An ABC transporter from Bacillus thuringiensis is essential for β-exotoxin I production. J. Bacteriol. 184: 5848-5854.
Eswarappa, S.M., K.K. Panguluri, M. Hensel, and D. Chakravortty. (2008). The yejABEF operon of Salmonella confers resistance to antimicrobial peptides and contributes to its virulence. Microbiology 154: 666-678.
Falcón-Pérez, J.M., M.J. Mazón, J. Molano, and P. Eraso. (1999). Functional domain analysis of the yeast ABC transporter Ycf1p by site-directed mutagenesis. J. Biol. Chem. 274: 23584-23590.
Fath, M.J. and R. Kolter. (1993). ABC transporters: bacterial exporters. Microbiol Rev 57: 995-1017.
Feissner, R.E., C.L. Richard-Fogal, E.R. Frawley, and R.G. Kranz. (2006). ABC transporter-mediated release of a haem chaperone allows cytochrome c biogenesis. Mol. Microbiol. 61: 219-231.
Feng, L., S.N. Senchenkova, J. Yang, A.S. Shashkov, J. Tao, H. Guo, J. Cheng, Y. Ren, Y.A. Knirel, P.R. Reeves, and L. Wang. (2004). Synthesis of the heteropolysaccharide O antigen of Escherichia coli O52 requires an ABC transporter: structural and genetic evidence. J. Bacteriol. 186: 4510-4519.
Fetherston, J.D., V.J. Bertolino, and R.D. Perry. (1999). YbtP and YbtQ: two ABC transporters required for iron uptake in Yersinia pestis. Mol. Microbiol. 32: 289-299.
Fiedler, G., M. Arnold, S. Hannus, and I. Maldener. (1998). The DevBCA exporter is essential for envelope formation in heterocysts of the cyanobacterium Anabaena sp. strain PCC 7120. Mol. Microbiol. 27: 1193-1202.
Fiedler, G., M. Pajatsch, and A. Böck. (1996). Genetics of a novel starch utilisation pathway present in Klebsiella oxytoca. J. Mol. Biol. 256: 279-291.
Francis, G.A., M. Tsujita, and T.L. Terry. (1999). Apolipoprotein AI efficiently binds to and mediates cholesterol and phospholipid efflux from human but not rat aortic smooth muscle cells. Biochemistry 38: 16315-16322.
Frelet-Barrand, A., H.U. Kolukisaoglu, S. Plaza, M. Rüffer, L. Azevedo, S. Hörtensteiner, K. Marinova, B. Weder, B. Schulz, and M. Klein. (2008). Comparative mutant analysis of Arabidopsis ABCC-type ABC transporters: AtMRP2 contributes to detoxification, vacuolar organic anion transport and chlorophyll degradation. Plant Cell Physiol. 49: 557-569.
Gaballa, A. and J.D. Helmann. (2007). Substrate induction of siderophore transport in Bacillus subtilis mediated by a novel one-component regulator. Mol. Microbiol. 66: 164-173.
Gaballa, A., T. Wang, R.W. Ye, and J.D. Helmann. (2002). Functional analysis of the Bacillus subtilis Zur regulon. J. Bacteriol. 184: 6508-6514.
Gadsby, D.C., P. Vergani, and L. Csanády. (2006). The ABC protein turned chloride channel whose failure causes cystic fibrosis. Nature 440: 477-483.
Garault, P., D. Le Bars, C. Besset, and V. Monnet. (2002). Three oligopeptide-binding proteins are involved in the oligopeptide transport of Streptococcus thermophilus. J. Biol. Chem. 277: 32-39.
Garrigues, A., A.E. Escargueil, and S. Orlowski. (2002). The multidrug transporter, P-glycoprotein, actively mediates cholesterol redistribution in the cell membrane. Proc. Natl. Acad. Sci. USA 99: 10347-10352.
Gebhard, S. and G.M. Cook. (2008). Differential regulation of high-affinity phosphate transport systems of Mycobacterium smegmatis: identification of PhnF, a repressor of the phnDCE operon. J. Bacteriol. 190: 1335-1343.
Gerber, S., M. Comellas-Bigler, B.A. Goetz, and K.P. Locher. (2008). Structural basis of trans-inhibition in a molybdate/tungstate ABC transporter. Science 321: 246-250.
Gimmestad, M., M. Steigedal, H. Ertesvåg, S. Moreno, B.E. Christensen, G. Espín, and S. Valla. (2006). Identification and characterization of an Azotobacter vinelandii type I secretion system responsible for export of the AlgE-type mannuronan C-5-epimerases. J. Bacteriol. 188: 5551-5560.
Glaser, P., H. Sakamoto, J. Bellalou, A. Ullmann, and A. Danchin. (1988). Secretion of cyclolysin, the calmodulin-sensitive adenylate cyclase-haemolysin bifunctional protein of Bordetella pertussis. EMBO. J. 7: 3997-4004.
Golin, J., Z.N. Kon, C.P. Wu, J. Martello, L. Hanson, S. Supernavage, S.V. Ambudkar, and Z.E. Sauna. (2007). Complete inhibition of the Pdr5p multidrug efflux pump ATPase activity by its transport substrate clotrimazole suggests that GTP as well as ATP may be used as an energy source. Biochemistry 46: 13109-13119.
Gompf, S., A. Zutz, M. Hofacker, W. Haase, C. van der Does, and R. Tampé. (2007). Switching of the homooligomeric ATP-binding cassette transport complex MDL1 from post-translational mitochondrial import to endoplasmic reticulum insertion. FEBS J. 274: 5298-5310.
González-Pastor, J.E., E.C. Hobbs, and R. Losick. (2003). Cannibalism by sporulating bacteria. Science 301: 510-513.
Goodman, C.D., P. Casati, and V. Walbot. (2004). A multidrug resistance-associated protein involved in anthocyanin transport in Zea mays. Plant Cell 16: 1812-1826.
Gottesman, M.M., C.A. Hrycyna, P.V. Schoenlein, U.A. Germann, and I. Pastan. (1995). Genetic analysis of the multidrug transporter. Annu Rev Genet 29: 607-649.
Gottschalk, B., G. Bröker, M. Kuhn, S. Aymanns, U. Gleich-Theurer, and B. Spellerberg. (2006). Transport of multidrug resistance substrates by the Streptococcus agalactiae hemolysin transporter. J. Bacteriol. 188: 5984-5992.
Green, R.M., F. Hoda, and K.L. Ward. (2000). Molecular cloning and characterization of the murine bile salt export pump. Gene 241: 117-123.
Grigoras, I., M. Lazard, P. Plateau, and S. Blanquet. (2008). Functional characterization of the Saccharomyces cerevisiae ABC-transporter Yor1p overexpressed in plasma membranes. Biochim. Biophys. Acta. 1778: 68-78.
Haimeur, A., R.G. Deeley, and S.P. Cole. (2002). Charged amino acids in the sixth transmembrane helix of multidrug resistance protein 1 (MRP1/ABCC1) are critical determinants of transport activity. J. Biol. Chem. 277: 41326-41333.
Hammond, C.L., R. Marchan, S.M. Krance, and N. Ballatori. (2007). Glutathione export during apoptosis requires functional multidrug resistance-associated proteins. J. Biol. Chem. 282: 14337-14347.
Hanekop, N., M. Höing, L. Sohn-Bösser, M. Jebbar, L. Schmitt, and E. Bremer. (2007). Crystal structure of the ligand-binding protein EhuB from Sinorhizobium meliloti reveals substrate recognition of the compatible solutes ectoine and hydroxyectoine. J. Mol. Biol. 374: 1237-1250.
Haney, D.Q. (1999). New class of antibiotics may help doctors overcome resistant germs. Assoc. Press.
Hashimoto, Y., N. Li, H. Yokoyama, and T. Ezaki. (1993). Complete nucleotide sequence and molecular characterization of ViaB region encoding Vi antigen in Salmonella typhi. J. Bacteriol. 175: 4456-4465.
Hazlett, K.R., F. Rusnak, D.G. Kehres, S.W. Bearden, C.J. La Vake, M.E. La Vake, M.E. Maguire, R.D. Perry, and J.D. Radolf. (2003). The Treponema pallidum tro operon encodes a multiple metal transporter, a zinc-dependent transcriptional repressor, and a semi-autonomously expressed phosphoglycerate mutase. J. Biol. Chem. 278: 20687-20694.
Hebbeln, P., D.A. Rodionov, A. Alfandega, and T. Eitinger. (2007). Biotin uptake in prokaryotes by solute transporters with an optional ATP-binding cassette-containing module. Proc. Natl. Acad. Sci. USA 104: 2909-2914.
Hettema, E.H., C.W. van Roermund, B. Distel, M. van den Berg, C. Vilela, C. Rodrigues-Pousada, R.J. Wanders, and H.F. Tabak. (1996). The ABC transporter proteins Pat1 and Pat2 are required for import of long-chain fatty acids into peroxisomes of Saccharomyces cerevisiae. EMBO. J. 15: 3813-3822.
Higgins, C.F. (1995). The ABC of channel regulation. Cell 82: 693-696.
Hinsa, S.M., M. Espinosa-Urgel, J.L. Ramos, and G.A. O'Toole. (2003). Transition from reversible to irreversible attachment during biofilm formation by Pseudomonas fluorescens WCS365 requires an ABC transporter and a large secreted protein. Mol. Microbiol. 49: 905-918.
Hiron, A., E. Borezée-Durant, J.C. Piard, and V. Juillard. (2007). Only one of four oligopeptide transport systems mediates nitrogen nutrition in Staphylococcus aureus. J. Bacteriol. 189: 5119-5129.
Holland, I.B. and M.A. Blight. (1999). ABC-ATPases, adaptable energy generators fuelling transmembrane movement of a variety of molecules in organisms from bacteria to humans. J. Mol. Biol. 293: 381-399.
Holland, I.B., S.P.C. Cole, K. Kuchler, and C.F. Higgins (Eds.). (2003). ABC Proteins: From Bacteria to Man. London: Academic Press/Elsevier Science.
Hollenstein, K., D.C. Frei, and K.P. Locher. (2007). Structure of an ABC transporter in complex with its binding protein. Nature 446: 213-216.
Holmes, A.R., S. Tsao, S.W. Ong, E. Lamping, K. Niimi, B.C. Monk, M. Niimi, A. Kaneko, B.R. Holland, J. Schmid, and R.D. Cannon. (2006). Heterozygosity and functional allelic variation in the Candida albicans efflux pump genes CDR1 and CDR2. Mol. Microbiol. 62: 170-186.
Holmes, A.R., Y.H. Lin, K. Niimi, E. Lamping, M. Keniya, M. Niimi, K. Tanabe, B.C. Monk, and R.D. Cannon. (2008). ABC transporter Cdr1p contributes more than Cdr2p does to fluconazole efflux in fluconazole-resistant Candida albicans clinical isolates. Antimicrob. Agents Chemother. 52: 3851-3862.
Horlacher, R., K.B. Xavier, H. Santos, J. DiRuggiero, M. Kossmann, and W. Boos. (1998). Archaeal binding protein-dependent ABC transporter: molecular and biochemical analysis of the trehalose/maltose transport system of the hyperthermophilic archaeon Thermococcus litoralis. J. Bacteriol. 180: 680-689.
Hosie, A.H., D. Allaway, C.S. Galloway, H.A. Dunsby, and P.S. Poole. (2002). Rhizobium leguminosarum has a second general amino acid permease with unusually broad substrate specificity and high similarity to branched-chain amino acid transporters (Bra/LIV) of the ABC family. J. Bacteriol. 184: 4071-4080.
Hou, Y.X., J.R. Riordan, and X.B. Chang. (2003). ATP binding, not hydrolysis, at the first nucleotide-binding domain of multidrug resistance-associated protein MRP1 enhances ADP.Vi trapping at the second domain. J. Biol. Chem. 278: 3599-3605.
Hugouvieux-Cotte-Pattat, N. and S. Reverchon. (2001). Two transporters, TogT and TogMNAB, are responsible for oligogalacturonide uptake in Erwinia chrysanthemi 3937. Mol. Microbiol. 41: 1125-1132.
Hullo, M.F., S. Auger, E. Dassa, A. Danchin, and I. Martin-Verstraete. (2004). The metNPQ operon of Bacillus subtilis encodes an ABC permease transporting methionine sulfoxide, D- and L-methionine. Res. Microbiol. 155: 80-86.
Hunnicutt, D.W., M.J. Kempf, and M.J. McBride. (2002). Mutations in Flavobacterium johnsoniae gldF and gldG disrupt gliding motility and interfere with membrane localization of GldA. J. Bacteriol. 184: 2370-2378.
Hvorup, R.N., B.A. Goetz, M. Niederer, K. Hollenstein, E. Perozo, and K.P. Locher. (2007). Asymmetry in the structure of the ABC transporter-binding protein complex BtuCD-BtuF. Science 317: 1387-1390.
Hyink, O., P.A. Wescombe, M. Upton, N. Ragland, J.P. Burton, and J.R. Tagg. (2007). Salivaricin A2 and the novel lantibiotic salivaricin B are encoded at adjacent loci on a 190-kilobase transmissible megaplasmid in the oral probiotic strain Streptococcus salivarius K12. Appl. Environ. Microbiol. 73: 1107-1113.
Igarashi, Y., K.F. Aoki, H. Mamitsuka, K. Kuma, and M. Kanehisa. (2004). The evolutionary repertoires of the eukaryotic-type ABC transporters in terms of the phylogeny of ATP-binding domains in eukaryotes and prokaryotes. Mol Biol Evol 21: 2149-2160.
Iliás, A., Z. Urbán, T.L. Seidl, O. Le Saux, E. Sinkó, C.D. Boyd, B. Sarkadi, and A. Váradi. (2002). Loss of ATP-dependent transport activity in pseudoxanthoma elasticum-associated mutants of human ABCC6 (MRP6). J. Biol. Chem. 277: 16860-16867.
Ito, Y., K. Kanamaru, N. Taniguchi, S. Miyamoto, and H. Tokuda. (2006). A novel ligand bound ABC transporter, LolCDE, provides insights into the molecular mechanisms underlying membrane detachment of bacterial lipoproteins. Mol. Microbiol. 62: 1064-1075.
Iwaki, T., Y. Giga-Hama, and K. Takegawa. (2006). A survey of all 11 ABC transporters in fission yeast: two novel ABC transporters are required for red pigment accumulation in a Schizosaccharomyces pombe adenine biosynthetic mutant. Microbiology 152: 2309-2321.
Janas, E., M. Hofacker, M. Chen, S. Gompf, C. van der Does, and R. Tampé. (2003). The ATP hydrolysis cycle of the nucleotide-binding domain of the mitochondrial ATP-binding cassette transporter Mdl1p. J. Biol. Chem. 278: 26862-26869.
Janvilisri, T., H. Venter, S. Shahi, G. Reuter, L. Balakrishnan, and H.W. van Veen. (2003). Sterol transport by the human breast cancer resistance protein (ABCG2) expressed in Lactococcus lactis. J. Biol. Chem. 278: 20645-20651.
Jedlitschky, G., B. Burchell, and D. Keppler. (2000). The multidrug resistance protein 5 functions as an ATP-dependent export pump for cyclic nucleotides. J. Biol. Chem. 275: 30069-30074.
Jensen, J.B., N.K. Peters, and T.V. Bhuvaneswari. (2002). Redundancy in periplasmic binding protein-dependent transport systems for trehalose, sucrose, and maltose in Sinorhizobium meliloti. J. Bacteriol. 184: 2978-2986.
Jordan, I.K., K.C. Kota, G. Cui, C.H. Thompson, and N.A. McCarty. (2008). Evolutionary and functional divergence between the cystic fibrosis transmembrane conductance regulator and related ATP-binding cassette transporters. Proc. Natl. Acad. Sci. USA 105: 18865-18870.
Kadaba, N.S., J.T. Kaiser, E. Johnson, A. Lee, and D.C. Rees. (2008). The high-affinity E. coli methionine ABC transporter: structure and allosteric regulation. Science 321: 250-253.
Kagawa, T., N. Watanabe, K. Mochizuki, A. Numari, Y. Ikeno, J. Itoh, H. Tanaka, I.M. Arias, and T. Mine. (2008). Phenotypic differences in PFIC2 and BRIC2 correlate with protein stability of mutant Bsep and impaired taurocholate secretion in MDCK II cells. Am. J. Physiol. Gastrointest Liver Physiol 294: G58-67.
Kahnert, A., P. Vermeij, C. Wietek, P. James, T. Leisinger, and M.A. Kertesz. (2000). The ssu locus plays a key role in organosulfur metabolism in Pseudomonas putida S-313. J. Bacteriol. 182: 2869-2878.
Kala, S.V., M.W. Neely, G. Kala, C.I. Prater, D.W. Atwood, J.S. Rice, and M.W. Lieberman. (2000). The MRP2/cMOAT transporter and arsenic-glutathione complex formation are required for biliary excretion of arsenic. J. Biol. Chem. 275: 33404-33408.
Kamakura, A., Y. Fujimoto, Y. Motohashi, K. Ohashi, A. Ohashi-Kobayashi, and M. Maeda. (2008). Functional dissection of transmembrane domains of human TAP-like (ABCB9). Biochem. Biophys. Res. Commun. 377: 847-851.
Kanamaru, K., N. Taniguchi, S. Miyamoto, S. Narita, and H. Tokuda. (2007). Complete reconstitution of an ATP-binding cassette transporter LolCDE complex from separately isolated subunits. FEBS J. 274: 3034-3043.
Kappes, R.M. and E. Bremer. (1998). Response of Bacillus subtilis to high osmolarity: uptake of carnitine, crotonobetaine and ?-butyrobetaine via the ABC transport system OpuC. Microbiology 144: 83-90.
Kashiwagi, K., M.H. Tsuhako, K. Sakata, T. Saisho, A. Igarashi, S.O. da Costa, and K. Igarashi. (1998). Relationship between spontaneous aminoglycoside resistance in Escherichia coli and a decrease in oligopeptide binding protein. J. Bacteriol. 180: 5484-5488.
Kawai, E., H. Akatsuka, A. Idei, T. Shibatani, and K. Omori. (1998). Serratia marcescens S-layer protein is secreted extracellularly via an ATP-binding cassette exporter, the Lip system. Mol. Microbiol. 27: 941-952.
Kehres, D.G., A. Janakiraman, J.M. Slauch, and M.E. Maguire. (2002). SitABCD is the alkaline Mn2+ transporter of Salmonella enterica serovar Typhimurium. J. Bacteriol. 184: 3159-3166.
Kempf, B. and E. Bremer. (1998). Uptake and synthesis of compatible solutes as microbial stress responses to high-osmolality environments. Arch. Microbiol. 170: 319-330.
Keppler, D. (1999). Export pumps for glutathione S-conjugates. Free Radic Biol Med 27: 985-991.
Keppler, D. and J. Konig. (1997). Hepatic canalicular membrane 5: Expression and localization of the conjugate export pump encoded by the MRP2 (cMRP/cMOAT) gene in liver. FASEB J. 11: 509-516.
Kim, C., S. Song, and C. Park. (1997). The D-allose operon of Escherichia coli K-12. J. Bacteriol. 179: 7631-7637.
Kim, D.Y., L. Bovet, M. Maeshima, E. Martinoia, and Y. Lee. (2007). The ABC transporter AtPDR8 is a cadmium extrusion pump conferring heavy metal resistance. Plant J. 50: 207-218.
Kim, H. and S.K. Farrand. (1997). Characterization of the acc operon from the nopaline-type Ti plasmid pTiC58, which encodes utilization of agrocinopines A and B and susceptibility to agrocin 84. J. Bacteriol. 179: 7559-7572.
Klein, I., B. Sarkadi, and A. Váradi. (1999). An inventory of the human ABC proteins. Biochim. Biophys. Acta. 1461: 237-262.
Kobayashi, N., K. Nishino, and A. Yamaguchi. (2001). Novel macrolide-specific ABC-type efflux transporter in Escherichia coli. J. Bacteriol. 183: 5639-5644.
Kobayashi, N., N. Kobayashi, A. Yamaguchi, and T. Nishi. (2009). Characterization of the ATP-dependent sphingosine-1-phosphate transporter in rat erythrocytes. J. Biol. Chem. [Epub: Ahead of Print]
Kogan, I., M. Ramjeesingh, C. Li, J.F. Kidd, Y. Wang, E.M. Leslie, S.P. Cole, and C.E. Bear. (2003). CFTR directly mediates nucleotide-regulated glutathione flux. EMBO. J. 22: 1981-1989.
Koide, A. and J.A. Hoch. (1994). Identification of a second oligopeptide transport system in Bacillus subtilis and determination of its role in sporulation. Mol. Microbiol. 13: 417-426.
Kolenbrander, P.E., R.N. Andersen, R.A. Baker, and H.F. Jenkinson. (1998). The adhesion-associated sca operon in Streptococcus gordonii encodes an inducible high-affinity ABC transporter for Mn2+ uptake. J. Bacteriol. 180: 290-295.
Koyanagi, T., T. Katayama, H. Suzuki, and H. Kumagai. (2004). Identification of the LIV-I/LS system as the third phenylalanine transporter in Escherichia coli K-12. J. Bacteriol. 186: 343-350.
Krehenbrink, M. and J.A. Downie. (2008). Identification of protein secretion systems and novel secreted proteins in Rhizobium leguminosarum bv. viciae. BMC Genomics 9: 55.
Krejcík, Z., K. Denger, S. Weinitschke, K. Hollemeyer, V. Paces, A.M. Cook, and T.H. Smits. (2008). Sulfoacetate released during the assimilation of taurine-nitrogen by Neptuniibacter caesariensis: purification of sulfoacetaldehyde dehydrogenase. Arch. Microbiol. 190: 159-168.
Krishnamurthy, P.C., G. Du, Y. Fukuda, D. Sun, J. Sampath, K.E. Mercer, J. Wang, B. Sosa-Pineda, K.G. Murti, and J.D. Schuetz. (2006). Identification of a mammalian mitochondrial porphyrin transporter. Nature 443: 586-589.
Kuan, G., E. Dassa, W. Saurin, M. Hofnung, and M.H. Saier, Jr. (1995). Phylogenetic analyses of the ATP-binding constituents of bacterial extracytoplasmic receptor-dependent ABC-type nutrient uptake permeases. Res. Microbiol. 146: 271-278.
Légaré, D., D. Richard, R. Mukhopadhyay, Y.D. Stierhof, B.P. Rosen, A. Haimeur, B. Papadopoulou, and M. Ouellette. (2001). The Leishmania ATP-binding cassette protein PGPA is an intracellular metal-thiol transporter ATPase. J. Biol. Chem. 276: 26301-26307.
Létoffé, S., P. Delepelaire, and C. Wandersman. (2008). Functional differences between heme permeases: Serratia marcescens HemTUV permease exhibits a narrower substrate specificity (restricted to heme) than the Escherichia coli DppABCDF peptide-heme permease. J. Bacteriol. 190: 1866-1870.
Lagos, R., J.E. Villanueva, and O. Monasterio. (1999). Identification and properties of the genes encoding microcin E492 and its immunity protein. J. Bacteriol. 181: 212-217.
Lagos, R., M. Baeza, G. Corsini, C. Hetz, E. Strahsburger, J.A. Castillo, C. Vergara, and O. Monasterio. (2001). Structure, organization and characterization of the gene cluster involved in the production of microcin E492, a channel-forming bacteriocin. Mol. Microbiol. 42: 229-243.
Lambert, A., M. Østerås, K. Mandon, M.C. Poggi, and D. Le Rudulier. (2001). Fructose uptake in Sinorhizobium meliloti is mediated by a high-affinity ATP-binding cassette transport system. J. Bacteriol. 183: 4709-4717.
Lange, H., G. Kispal, and R. Lill. (1999). Mechanism of iron transport to the site of heme synthesis inside yeast mitochondria. J. Biol. Chem. 274: 18989-18996.
Larsen, P.B., J. Cancel, M. Rounds, and V. Ochoa. (2007). Arabidopsis ALS1 encodes a root tip and stele localized half type ABC transporter required for root growth in an aluminum toxic environment. Planta 225: 1447-1458.
Latunde-Dada, G.O., R.J. Simpson, and A.T. McKie. (2006). Recent advances in mammalian haem transport. Trends. Biochem. Sci. 31: 182-188.
Lee, E.M., S.H. Ahn, J.H. Park, J.H. Lee, S.C. Ahn, and I.S. Kong. (2004). Identification of oligopeptide permease (opp) gene cluster in Vibrio fluvialis and characterization of biofilm production by oppA knockout mutation. FEMS Microbiol. Lett. 240: 21-30.
Lee, M., K. Lee, J. Lee, E.W. Noh, and Y. Lee. (2005). AtPDR12 contributes to lead resistance in Arabidopsis. Plant Physiol. 138: 827-836.
Lee, S.J., A. Böhm, M. Krug, and W. Boos. (2007). The ABC of binding-protein-dependent transport in Archaea. Trends Microbiol. 15: 389-397.
Leon-Kempis, M.d.e.l.R., E. Guccione, F. Mulholland, M.P. Williamson, and D.J. Kelly. (2006). The Campylobacter jejuni PEB1a adhesin is an aspartate/glutamate-binding protein of an ABC transporter essential for microaerobic growth on dicarboxylic amino acids. Mol. Microbiol. 60: 1262-1275.
Leslie, E.M., A. Haimeur, and M.P. Waalkes. (2004). Arsenic transport by the human multidrug resistance protein 1 (MRP1/ABCC1). Evidence that a tri-glutathione conjugate is required. J. Biol. Chem. 279: 32700-32708.
Li, C., P.C. Krishnamurthy, H. Penmatsa, K.L. Marrs, X.Q. Wang, M. Zaccolo, K. Jalink, M. Li, D.J. Nelson, J.D. Schuetz, and A.P. Naren. (2007). Spatiotemporal coupling of cAMP transporter to CFTR chloride channel function in the gut epithelia. Cell 131: 940-951.
Li, Y. and W.A. Prinz. (2004). ATP-binding cassette (ABC) transporters mediate nonvesicular, raft-modulated sterol movement from the plasma membrane to the endoplasmic reticulum. J. Biol. Chem. 279: 45226-45234.
Lim, K.H., C.E. Jones, R.N. vanden Hoven, J.L. Edwards, M.L. Falsetta, M.A. Apicella, M.P. Jennings, and A.G. McEwan. (2008). Metal binding specificity of the MntABC permease of Neisseria gonorrhoeae and its influence on bacterial growth and interaction with cervical epithelial cells. Infect. Immun. 76: 3569-3576.
Lin, H.T., V.N. Bavro, N.P. Barrera, H.M. Frankish, S. Velamakanni, H.W. van Veen, C.V. Robinson, M.I. Borges-Walmsley, and A.R. Walmsley. (2009). MacB ABC transporter is a dimer whose ATPase activity and macrolide-binding capacity are regulated by the membrane fusion protein MacA. J. Biol. Chem. 284: 1145-1154.
Linton, K.J. and C.F. Higgins. (1998). The Escherichia coli ATP-binding cassette (ABC) proteins. Mol. Microbiol. 28: 5-13.
Liu, G., R. Sánchez-Fernández, Z.S. Li, and P.A. Rea. (2001). Enhanced multispecificity of arabidopsis vacuolar multidrug resistance-associated protein-type ATP-binding cassette transporter, AtMRP2. J. Biol. Chem. 276: 8648-8656.
Liu, M., W.N. Tanaka, H. Zhu, G. Xie, D.M. Dooley, and B. Lei. (2008). Direct hemin transfer from IsdA to IsdC in the iron-regulated surface determinant (Isd) heme acquisition system of Staphylococcus aureus. J. Biol. Chem. 283: 6668-6676.
Locher, K.P., A.T. Lee, and D.C. Rees. (2002). The E. coli BtuCD structure: a framework for ABC transporter architecture and mechanism. Science 296: 1091-1098.
Loo, T.W., M.C. Bartlett, and D.M. Clarke. (2003). Drug binding in human P-glycoprotein causes conformational changes in both nucleotide-binding domains. J. Biol. Chem. 278: 1575-1578.
Lu, B., C. Xu, K. Awai, A.D. Jones, and C. Benning. (2007). A small ATPase protein of Arabidopsis, TGD3, involved in chloroplast lipid import. J. Biol. Chem. 282: 35945-35953.
Lubelski, J., A. de Jong, R. van Merkerk, H. Agustiandari, O.P. Kuipers, J. Kok, and A.J. Driessen. (2006). LmrCD is a major multidrug resistance transporter in Lactococcus lactis. Mol. Microbiol. 61: 771-781.
Lubelski, J., P. Mazurkiewicz, R. van Merkerk, W.N. Konings, and A.J. Driessen. (2004). ydaG and ydbA of Lactococcus lactis encode a heterodimeric ATP-binding cassette-type multidrug transporter. J. Biol. Chem. 279: 34449-34455.
Luckenbach, T. and D. Epel. (2008). ABCB- and ABCC-type transporters confer multixenobiotic resistance and form an environment-tissue barrier in bivalve gills. Am. J. Physiol. Regul Integr Comp Physiol 294: R1919-1929.
Méndez, C. and J.A. Salas. (1998). ABC transporters in antibiotic-producing actinomycetes. FEMS Microbiol. Lett. 158: 1-8.
Mühlenhoff, U. and R. Lill. (2000). Biogenesis of iron-sulfur proteins in eukaryotes: a novel task of mitochondria that is inherited from bacteria. Biochim. Biophys. Acta. 1459: 370-382.
Maeda, S. and T. Omata. (1997). Substrate-binding lipoprotein of the cyanobacterium Synechococcus sp. strain PCC 7942 involved in the transport of nitrate and nitrite. J. Biol. Chem. 272: 3036-3041.
Maeda, S. and T. Omata. (2009). Nitrite transport activity of the ABC-type cyanate transporter of the cyanobacterium Synechococcus elongatus. J. Bacteriol. 191: 3265-3272.
Mahé, Y., Y. Lemoine, and K. Kuchler. (1996). The ATP binding cassette transporters Pdr5 and Snq2 of Saccharomyces cerevisiae can mediate transport of steroids in vivo. J. Biol. Chem. 271: 25167-25172.
Mahmood, N.A., E. Biemans-Oldehinkel, J.S. Patzlaff, G.K. Schuurman-Wolters, and B. Poolman. (2006). Ion specificity and ionic strength dependence of the osmoregulatory ABC transporter OpuA. J. Biol. Chem. 281: 29830-29839.
Makdessi, K., J.R. Andreesen, and A. Pich. (2001). Tungstate Uptake by a highly specific ABC transporter in Eubacterium acidaminophilum. J. Biol. Chem. 276: 24557-24564.
Mao, Q., R.G. Deeley, and S.P. Cole. (2000). Functional reconstitution of substrate transport by purified multidrug resistance protein MRP1 (ABCC1) in phospholipid vesicles. J. Biol. Chem. 275: 34166-34172.
Margolles, A., A.B. Flórez, J.A. Moreno, D. van Sinderen, and C.G. de los Reyes-Gavilán. (2006). Two membrane proteins from Bifidobacterium breve UCC2003 constitute an ABC-type multidrug transporter. Microbiology 152: 3497-3505.
Mason, K.M., M.E. Bruggeman, R.S. Munson, and L.O. Bakaletz. (2006). The non-typeable Haemophilus influenzae Sap transporter provides a mechanism of antimicrobial peptide resistance and SapD-dependent potassium acquisition. Mol. Microbiol. 62: 1357-1372.
Matsumoto-Nakano, M. and H.K. Kuramitsu. (2006). Role of bacteriocin immunity proteins in the antimicrobial sensitivity of Streptococcus mutans. J. Bacteriol. 188: 8095-8102.
Matsumura, Y., N. Ban, K. Ueda, and N. Inagaki. (2006). Characterization and classification of ATP-binding cassette transporter ABCA3 mutants in fatal surfactant deficiency. J. Biol. Chem. 281: 34503-34514.
Matsuo, T., J. Chen, Y. Minato, W. Ogawa, T. Mizushima, T. Kuroda, and T. Tsuchiya. (2008). SmdAB, a heterodimeric ABC-Type multidrug efflux pump, in Serratia marcescens. J. Bacteriol. 190: 648-654.
McAuliffe, O., R.P. Ross, and C. Hill. (2001). Lantibiotics: structure, biosynthesis and mode of action. FEMS Microbiol. Rev. 25: 285-308.
Medrano, M.S., Y. Ding, X.G. Wang, P. Lu, J. Coburn, and L.T. Hu. (2007). Regulators of expression of the oligopeptide permease A proteins of Borrelia burgdorferi. J. Bacteriol. 189: 2653-2659.
Menéndez, N., A.F. Braña, J.A. Salas, and C. Méndez. (2007). Involvement of a chromomycin ABC transporter system in secretion of a deacetylated precursor during chromomycin biosynthesis. Microbiology 153: 3061-3070.
Miethke, M., O. Klotz, U. Linne, J.J. May, C.L. Beckering, and M.A. Marahiel. (2006). Ferri-bacillibactin uptake and hydrolysis in Bacillus subtilis. Mol. Microbiol. 61: 1413-1427.
Mikkat, S. and M. Hagemann. (2000). Molecular analysis of the ggtBCD gene cluster of Synechocystis sp. strain PCC6803 encoding subunits of an ABC transporter for osmoprotective compounds. Arch. Microbiol. 174: 273-282.
Mikolay, A. and D.H. Nies. (2009). The ABC-transporter AtmA is involved in nickel and cobalt resistance of Cupriavidus metallidurans strain CH34. Antonie Van Leeuwenhoek 96: 183-191.
Mishima, Y., K. Momma, W. Hashimoto, B. Mikami, and K. Murata. (2001). Super-channel in bacteria: function and structure of the macromolecule import system mediated by a pit-dependent ABC transporter. FEMS Microbiol. Lett. 204: 215-221.
Mitsuhashi, N., T. Miki, H. Senbongi, N. Yokoi, H. Yano, M. Miyazaki, N. Nakajima, T. Iwanaga, Y. Yokoyama, T. Shibata, and S. Seino. (2000). MTABC3, a novel mitochondrial ATP-binding cassette protein involved in iron homeostasis. J. Biol. Chem. 275: 17536-17540.
Molday, R.S. (2007). ATP-binding cassette transporter ABCA4: molecular properties and role in vision and macular degeneration. J. Bioenerg. Biomembr. 39: 507-517.
Molday, R.S., M. Zhong, and F. Quazi. (2009). The role of the photoreceptor ABC transporter ABCA4 in lipid transport and Stargardt macular degeneration. Biochim. Biophys. Acta. [Epub: Ahead of Print]
Mollapour, M., A. Shepherd, and P.W. Piper. (2008). Novel stress responses facilitate Saccharomyces cerevisiae growth in the presence of the monocarboxylate preservatives. Yeast 25: 169-177.
Momma, K., M. Okamoto, Y. Mishima, S. Mori, W. Hashimoto, and K. Murata. (2000). A novel bacterial ATP-binding cassette transporter system that allows uptake of macromolecules. J. Bacteriol. 182: 3998-4004.
Montañez, G.E., M.N. Neely, and Z. Eichenbaum. (2005). The streptococcal iron uptake (Siu) transporter is required for iron uptake and virulence in a zebrafish infection model. Microbiology 151: 3749-3757.
Moslavac, S., K. Nicolaisen, O. Mirus, F. Al Dehni, R. Pernil, E. Flores, I. Maldener, and E. Schleiff. (2007). A TolC-like protein is required for heterocyst development in Anabaena sp. strain PCC 7120. J. Bacteriol. 189: 7887-7895.
Murat, D., L. Goncalves, and E. Dassa. (2008). Deletion of the Escherichia coli uup gene encoding a protein of the ATP binding cassette superfamily affects bacterial competitiveness. Res. Microbiol. 159: 671-677.
Nagao, K., Y. Taguchi, M. Arioka, H. Kadokura, A. Takatsuki, K. Yoda, and M. Yamasaki. (1995). bfr1+, a novel gene of Schizosaccharomyces pombe which confers brefeldin A resistance, is structurally related to the ATP-binding cassette superfamily. J. Bacteriol. 177: 1536-1543.
Nagy, R., H. Grob, B. Weder, P. Green, M. Klein, A. Frelet, J.K. Schjoerring, C.A. Brearley, and E. Martinoia. (2009). The Arabidopsis ATP-binding cassette protein ATMRP5/ATABCC5 is a high-affinity inositol hexakisphosphate transporter involved in guard cell signaling and phytate storage. J. Biol. Chem. [Epub: Ahead of Print]
Nakano, S., M. Fukaya, and S. Horinouchi. (2006). Putative ABC transporter responsible for acetic acid resistance in Acetobacter aceti. Appl. Environ. Microbiol. 72: 497-505.
Nanavati, D.M., T.N. Nguyen, and K.M. Noll. (2005). Substrate specificities and expression patterns reflect the evolutionary divergence of maltose ABC transporters in Thermotoga maritima. J. Bacteriol. 187: 2002-2009.
Narita, S., K. Kanamaru, S. Matsuyama, and H. Tokuda. (2003). A mutation in the membrane subunit of an ABC transporter LolCDE complex causing outer membrane localization of lipoproteins against their inner membrane-specific signals. Mol. Microbiol. 49: 167-177.
Narita, S., K. Tanaka, S. Matsuyama, and H. Tokuda. (2002). Disruption of lolCDE, encoding an ATP-binding cassette transporter, is lethal for Escherichia coli and prevents release of lipoproteins from the inner membrane. J. Bacteriol. 184: 1417-1422.
Netz, D.J., H.G. Sahl, R. Marcelino, J. dos Santos Nascimento, S.S. de Oliveira, M.B. Soares, M. do Carmo de Freire Bastos, and R. Marcolino. (2001). Molecular characterisation of aureocin A70, a multi-peptide bacteriocin isolated from Staphylococcus aureus. J. Mol. Biol. 311: 939-949.
Neubauer, O., A. Alfandega, J. Schoknecht, U. Sternberg, A. Pohlmann, and T. Eitinger. (2009). Two essential arginine residues in the T components of energy-coupling factor transporters. J. Bacteriol. 191: 6482-6488.
Neumann, L. and R. Tampé. (1999). Kinetic analysis of peptide binding to the TAP transport complex: evidence for structural rearrangements induced by substrate binding. J. Mol. Biol. 294: 1203-1213.
Nishimura, T., Y. Takahashi, O. Yamaguchi, H. Suzuki, S. Maeda, and T. Omata. (2008). Mechanism of low CO2-induced activation of the cmp bicarbonate transporter operon by a LysR family protein in the cyanobacterium Synechococcus elongatus strain PCC 7942. Mol. Microbiol. 68: 98-109.
Novikova, M., A. Metlitskaya, K. Datsenko, T. Kazakov, A. Kazakov, B. Wanner, and K. Severinov. (2007). The Escherichia coli Yej transporter is required for the uptake of translation inhibitor microcin C. J. Bacteriol. 189: 8361-8365.
Nygaard, T.K., G.C. Blouin, M. Liu, M. Fukumura, J.S. Olson, M. Fabian, D.M. Dooley, and B. Lei. (2006). The mechanism of direct heme transfer from the streptococcal cell surface protein Shp to HtsA of the HtsABC transporter. J. Biol. Chem. 281: 20761-20771.
Obis, D., A. Guillot, J.C. Gripon, P. Renault, A. Bolotin, and M.Y. Mistou. (1999). Genetic and biochemical characterization of a high-affinity betaine uptake system (BusA) in Lactococcus lactis reveals a new functional organization within bacterial ABC transporters. J. Bacteriol. 181: 6238-6246.
Ohki, R., Giyanto, K. Tateno, W. Masuyama, S. Moriya, K. Kobayashi, and N. Ogasawara. (2003). The BceRS two-component regulatory system induces expression of the bacitracin transporter, BceAB, in Bacillus subtilis. Mol. Microbiol. 49: 1135-1144.
Ohki, R., K. Tateno, T. Takizawa, T. Aiso, and M. Murata. (2005). Transcriptional termination control of a novel ABC transporter gene involved in antibiotic resistance in Bacillus subtilis. J. Bacteriol. 187: 5946-5954.
Okuda, K., Y. Aso, J. Nakayama, and K. Sonomoto. (2008). Cooperative transport between NukFEG and NukH in immunity against the lantibiotic nukacin ISK-1 produced by Staphylococcus warneri ISK-1. J. Bacteriol. 190: 356-362.
Oldham, M.L., D. Khare, F.A. Quiocho, A.L. Davidson, and J. Chen. (2007). Crystal structure of a catalytic intermediate of the maltose transporter. Nature 450: 515-521.
Oram, J.F., G. Wolfbauer, C. Tang, W.S. Davidson, and J.J. Albers. (2008). An amphipathic helical region of the N-terminal barrel of phospholipid transfer protein is critical for ABCA1-dependent cholesterol efflux. J. Biol. Chem. 283: 11541-11549.
Ortiz, D.F., L. Kreppel, D.M. Speiser, G. Scheel, G. McDonald, and D.W. Ow. (1992). Heavy metal tolerance in the fission yeast requires an ATP-binding cassette-type vacuolar membrane transporter. EMBO. J. 11: 3491-3499.
Ozvegy-Laczka, C., G. Köblös, B. Sarkadi, and A. Váradi. (2005). Single amino acid (482) variants of the ABCG2 multidrug transporter: major differences in transport capacity and substrate recognition. Biochim. Biophys. Acta. 1668: 53-63.
Papadelli, M., A. Karsioti, R. Anastasiou, M. Georgalaki, and E. Tsakalidou. (2007). Characterization of the gene cluster involved in the biosynthesis of macedocin, the lantibiotic produced by Streptococcus macedonicus. FEMS Microbiol. Lett. 272: 75-82.
Park, J.T., D. Raychaudhuri, H. Li, S. Normark, and D. Mengin-Lecreulx. (1998). MppA, a periplasmic binding protein essential for import of the bacterial cell wall peptide L-alanyl-γ-D-glutamyl-meso-diaminopimelate. J. Bacteriol. 180: 1215-1223.
Patzer, S.I. and K. Hantke. (1998). The ZnuABC high-affinity zinc uptake system and its regulator Zur in Escherichia coli. Mol. Microbiol. 28: 1199-1210.
Paulsen, I.T., A.M. Beness, and M.H. Saier, Jr. (1997). Computer-based analyses of the protein constituents of transport systems catalysing export of complex carbohydrates in bacteria. Microbiology 143(Pt8): 2685-2699.
Pernil, R., S. Picossi, V. Mariscal, A. Herrero, and E. Flores. (2008). ABC-type amino acid uptake transporters Bgt and N-II of Anabaena sp. strain PCC 7120 share an ATPase subunit and are expressed in vegetative cells and heterocysts. Mol. Microbiol. 67: 1067-1080.
Perria, C.L., V. Rajamanickam, P.E. Lapinski, and M. Raghavan. (2006). Catalytic site modifications of TAP1 and TAP2 and their functional consequences. J. Biol. Chem. 281: 39839-39851.
Picossi, S., M.L. Montesinos, R. Pernil, C. Lichtlé, A. Herrero, and E. Flores. (2005). ABC-type neutral amino acid permease N-I is required for optimal diazotrophic growth and is repressed in the heterocysts of Anabaena sp. strain PCC 7120. Mol. Microbiol. 57: 1582-1592.
Pighin, J.A., H. Zheng, L.J. Balakshin, I.P. Goodman, T.L. Western, R. Jetter, L. Kunst, and A.L. Samuels. (2004). Plant cuticular lipid export requires an ABC transporter. Science 306: 702-704.
Pinkett, H.W., A.T. Lee, P. Lum, K.P. Locher, and D.C. Rees. (2007). An inward-facing conformation of a putative metal-chelate-type ABC transporter. Science 315: 373-377.
Podlesek, Z., A. Comino, B. Herzog-Velikonja, D. Zgur-Bertok, R. Komel, and M. Grabnar. (1995). Bacillus licheniformis bacitracin-resistance ABC transporter: relationship to mammalian multidrug resistance. Mol. Microbiol. 16: 969-976.
Posteraro, B., M. Sanguinetti, D. Sanglard, M. La Sorda, S. Boccia, L. Romano, G. Morace, and G. Fadda. (2003). Identification and characterization of a Cryptococcus neoformans ATP binding cassette (ABC) transporter-encoding gene, CnAFR1, involved in the resistance to fluconazole. Mol. Microbiol. 47: 357-371.
Pratte, B.S. and T. Thiel. (2006). High-affinity vanadate transport system in the cyanobacterium Anabaena variabilis ATCC 29413. J. Bacteriol. 188: 464-468.
Prévéral, S., L. Gayet, C. Moldes, J. Hoffmann, S. Mounicou, A. Gruet, F. Reynaud, R. Lobinski, J.M. Verbavatz, A. Vavasseur, and C. Forestier. (2009). A common highly conserved cadmium detoxification mechanism from bacteria to humans: heavy metal tolerance conferred by the ATP-binding cassette (ABC) transporter SpHMT1 requires glutathione but not metal-chelating phytochelatin peptides. J. Biol. Chem. 284: 4936-4943.
Prosecka, J., A.V. Orlov, Y.S. Fantin, V.V. Zinchenko, M.M. Babykin, and M. Tichy. (2009). A novel ATP-binding cassette transporter is responsible for resistance to viologen herbicides in the cyanobacterium Synechocystis sp. PCC 6803. FEBS J. 276: 4001-4011.
Quentin, Y. and G. Fichant. (2000). ABCdb: an ABC transporter database. J. Mol. Microbiol. Biotechnol. 2: 501-504.
Quintero, M.J., M.L. Montesinos, A. Herrero, and E. Flores. (2001). Identification of genes encoding amino acid permeases by inactivation of selected ORFs from the Synechocystis genomic sequence. Genome Res 11: 2034-2040.
Rafii, F. and M. Park. (2008). Detection and characterization of an ABC transporter in Clostridium hathewayi. Arch. Microbiol. 190: 417-426.
Raghuraman, G., P.E. Lapinski, and M. Raghavan. (2002). Tapasin interacts with the membrane-spanning domains of both TAP subunits and enhances the structural stability of TAP1 x TAP2 Complexes. J. Biol. Chem. 277: 41786-41794.
Raichaudhuri, A., M. Peng, V. Naponelli, S. Chen, R. Sánchez-Fernández, H. Gu, J.F. Gregory, 3rd, A.D. Hanson, and P.A. Rea. (2009). Plant Vacuolar ATP-binding Cassette Transporters That Translocate Folates and Antifolates in Vitro and Contribute to Antifolate Tolerance in Vivo. J. Biol. Chem. 284: 8449-8460.
Ramjeesingh, M., F. Ugwu, F.L. Stratford, L.J. Huan, C. Li, and C.E. Bear. (2008). The intact CFTR protein mediates ATPase rather than adenylate kinase activity. Biochem. J. 412: 315-321.
Randak, C.O. and M.J. Welsh. (2007). Role of CFTR's intrinsic adenylate kinase activity in gating of the Cl- channel. J. Bioenerg. Biomembr. 39: 473-479.
Rayapuram, N., J. Hagenmuller, J.M. Grienenberger, P. Giegé, and G. Bonnard. (2007). AtCCMA interacts with AtCcmB to form a novel mitochondrial ABC transporter involved in cytochrome c maturation in Arabidopsis. J. Biol. Chem. 282: 21015-21023.
Reid, G., P. Wielinga, N. Zelcer, I. van der Heijden, A. Kuil, M. de Haas, J. Wijnholds, and P. Borst. (2003). The human multidrug resistance protein MRP4 functions as a prostaglandin efflux transporter and is inhibited by nonsteroidal antiinflammatory drugs. Proc. Natl. Acad. Sci. USA 100: 9244-9249.
Reuter, G., T. Janvilisri, H. Venter, S. Shahi, L. Balakrishnan, and H.W. van Veen. (2003). The ATP binding cassette multidrug transporter LmrA and lipid transporter MsbA have overlapping substrate specificities. J. Biol. Chem. 278: 35193-35198.
Richard-Fogal, C.L., E.R. Frawley, and R.G. Kranz. (2008). Topology and function of CcmD in cytochrome c maturation. J. Bacteriol. 190: 3489-3493.
Richardson, J.S. and I.J. Oresnik. (2007). L-Rhamnose transport is sugar kinase (RhaK) dependent in Rhizobium leguminosarum bv. trifolii. J. Bacteriol. 189: 8437-8446.
Richardson, J.S., M.F. Hynes, and I.J. Oresnik. (2004). A genetic locus necessary for rhamnose uptake and catabolism in Rhizobium leguminosarum bv. trifolii. J. Bacteriol. 186: 8433-8442.
Riordan, J.R. (2008). CFTR function and prospects for therapy. Annu. Rev. Biochem. 77: 701-726.
Ritter, C.A., G. Jedlitschky, H. Meyer zu Schwabedissen, M. Grube, K. Köck, and H.K. Kroemer. (2005). Cellular export of drugs and signaling molecules by the ATP-binding cassette transporters MRP4 (ABCC4) and MRP5 (ABCC5). Drug Metab Rev 37: 253-278.
Rius, M., J. Hummel-Eisenbeiss, and D. Keppler. (2008). ATP-dependent transport of leukotrienes B4 and C4 by the multidrug resistance protein ABCC4 (MRP4). J Pharmacol Exp Ther 324: 86-94.
Rockwell, N.C., H. Wolfger, K. Kuchler, and J. Thorner. (2009). ABC transporter Pdr10 regulates the membrane microenvironment of Pdr12 in Saccharomyces cerevisiae. J. Membr. Biol. 229: 27-52.
Rodionov, D.A., P. Hebbeln, A. Eudes, J. ter Beek, I.A. Rodionova, G.B. Erkens, D.J. Slotboom, M.S. Gelfand, A.L. Osterman, A.D. Hanson, and T. Eitinger. (2009). A novel class of modular transporters for vitamins in prokaryotes. J. Bacteriol. 191: 42-51.
Rodionov, D.A., P. Hebbeln, M.S. Gelfand, and T. Eitinger. (2006). Comparative and functional genomic analysis of prokaryotic nickel and cobalt uptake transporters: evidence for a novel group of ATP-binding cassette transporters. J. Bacteriol. 188: 317-327.
Rodriguez, G.M. and I. Smith. (2006). Identification of an ABC transporter required for iron acquisition and virulence in Mycobacterium tuberculosis. J. Bacteriol. 188: 424-430.
Rosenberg, M.F., A.B. Kamis, R. Callaghan, C.F. Higgins, and R.C. Ford. (2003). Three-dimensional structures of the mammalian multidrug resistance P-glycoprotein demonstrate major conformational changes in the transmembrane domains upon nucleotide binding. J. Biol. Chem. 278: 8294-8299.
Roth, J.R., J.G. Lawrence, M. Rubenfield, S. Kieffer-Higgins, and G.M. Church. (1993). Characterization of the cobalamin (vitamin B12) biosynthetic genes of Salmonella typhimurium. J. Bacteriol. 175: 3303-3316.
Ruknudin, A., D.H. Schulze, S.K. Sullivan, W.J. Lederer, and P.A. Welling. (1998). Novel subunit composition of a renal epithelial KATP channel. J. Biol. Chem. 273: 14165-14171.
Russo, D.M., A. Williams, A. Edwards, D.M. Posadas, C. Finnie, M. Dankert, J.A. Downie, and A. Zorreguieta. (2006). Proteins exported via the PrsD-PrsE type I secretion system and the acidic exopolysaccharide are involved in biofilm formation by Rhizobium leguminosarum. J. Bacteriol. 188: 4474-4486.
Saito, A., T. Fujii, T. Shinya, N. Shibuya, A. Ando, and K. Miyashita. (2008). The msiK gene, encoding the ATP-hydrolysing component of N,N'-diacetylchitobiose ABC transporters, is essential for induction of chitinase production in Streptomyces coelicolor A3(2). Microbiology 154: 3358-3365.
Saum, R., A. Mingote, H. Santos, and V. Müller. (2009). Genetic analysis of the role of the ABC transporter Ota and Otb in glycine betaine transport in Methanosarcina mazei Gö1. Arch. Microbiol. 191: 291-301.
Saurin, W. and E. Dassa. (1994). Sequence relationships between integral inner membrane proteins of binding protein-dependent transport systems: evolution by recurrent gene duplications. Protein. Sci. 3: 325-344.
Saurin, W., M. Hofnung, and E. Dassa. (1999). Getting in or out: early segregation between importers and exporters in the evolution of ATP-binding cassette (ABC) transporters. J. Mol. Evol. 48: 22-41.
Schlösser, A., J. Jantos, K. Hackmann, and H. Schrempf. (1999). Characterization of the binding protein-dependent cellobiose and cellotriose transport system of the cellulose degrader Streptomyces reticuli. Appl. Environ. Microbiol. 65: 2636-2643.
Schlösser, A., T. Kampers, and H. Schrempf. (1997). The Streptomyces ATP-binding component MsiK assists in cellobiose and maltose transport. J. Bacteriol. 179: 2092-2095.
Schmidt, S., K. Pflüger, S. Kögl, R. Spanheimer, and V. Müller. (2007). The salt-induced ABC transporter Ota of the methanogenic archaeon Methanosarcina mazei Gö1 is a glycine betaine transporter. FEMS Microbiol. Lett. 277: 44-49.
Schmitt, L. and R. Tampé. (2002). Structure and mechanism of ABC transporters. Curr. Opin. Struct. Biol. 12: 754-760.
Schneider, E. and S. Hunke. (1998). ATP-binding-cassette (ABC) transport systems: functional and structural aspects of the ATP-hydrolyzing subunits/domains. FEMS Microbiol. Rev. 22: 1-20.
Schrodt, S., J. Koch, and R. Tampé. (2006). Membrane topology of the transporter associated with antigen processing (TAP1) within an assembled functional peptide-loading complex. J. Biol. Chem. 281: 6455-6462.
Schuetzer-Muehlbauer, M., B. Willinger, G. Krapf, S. Enzinger, E. Presterl, and K. Kuchler. (2003). The Candida albicans Cdr2p ATP-binding cassette (ABC) transporter confers resistance to caspofungin. Mol. Microbiol. 48: 225-235.
Schulz, H., R.A. Fabianek, E.C. Pellicioli, H. Hennecke, and L. Thöny-Meyer. (1999). Heme transfer to the heme chaperone CcmE during cytochrome c maturation requires the CcmC protein, which may function independently of the ABC-transporter CcmAB. Proc. Natl. Acad. Sci. USA 96: 6462-6467.
Seidler, U., A.K. Singh, A. Cinar, M. Chen, J. Hillesheim, B. Hogema, and B. Riederer. (2009). The role of the NHERF family of PDZ scaffolding proteins in the regulation of salt and water transport. Ann. N.Y. Acad. Sci. 1165: 249-260.
Shani, N., P.A. Watkins, and D. Valle. (1995). PXA1, a possible Saccharomyces cerevisiae ortholog of the human adrenoleukodystrophy gene. Proc. Natl. Acad. Sci. USA 92: 6012-6016.
Shao, H., D. James, R.J. Lamont, and D.R. Demuth. (2007). Differential interaction of Aggregatibacter (Actinobacillus) actinomycetemcomitans LsrB and RbsB proteins with autoinducer 2. J. Bacteriol. 189: 5559-5565.
Sharma, K.G., D.L. Mason, G. Liu, P.A. Rea, A.K. Bachhawat, and S. Michaelis. (2002). Localization, regulation, and substrate transport properties of Bpt1p, a Saccharomyces cerevisiae MRP-type ABC transporter. Eukaryot. Cell. 1: 391-400.
Shukla, S., V. Rai, P. Saini, D. Banerjee, A.K. Menon, and R. Prasad. (2007). Candida drug resistance protein 1, a major multidrug ATP binding cassette transporter of Candida albicans, translocates fluorescent phospholipids in a reconstituted system. Biochemistry 46: 12081-12090.
Shulami, S., O. Gat, A.L. Sonenshein, and Y. Shoham. (1999). The glucuronic acid utilization gene cluster from Bacillus stearothermophilus T-6. J. Bacteriol. 181: 3695-3704.
Singh, B. and K.H. Röhm. (2008). Characterization of a Pseudomonas putida ABC transporter (AatJMQP) required for acidic amino acid uptake: biochemical properties and regulation by the Aau two-component system. Microbiology 154: 797-809.
Sleator, R.D., H.H. Wemekamp-Kamphuis, C.G. Gahan, T. Abee, and C. Hill. (2005). A PrfA-regulated bile exclusion system (BilE) is a novel virulence factor in Listeria monocytogenes. Mol. Microbiol. 55: 1183-1195.
Smith, A.J., A. van Helvoort, G. van Meer, K. Szabo, E. Welker, G. Szakacs, A. Varadi, B. Sarkadi, and P. Borst. (2000). MDR3 P-glycoprotein, a phosphatidylcholine translocase, transports several cytotoxic drugs and directly interacts with drugs as judged by interference with nucleotide trapping. J. Biol. Chem. 275: 23530-23539.
Smriti, , P. Zou, and H.S. McHaourab. (2009). Mapping Daunorubicin-binding Sites in the ATP-binding Cassette Transporter MsbA Using Site-specific Quenching by Spin Labels. J. Biol. Chem. 284: 13904-13913.
Solbiati, J.O., M. Ciaccio, R.N. Farías, J.E. González-Pastor, F. Moreno, and R.A. Salomón. (1999). Sequence analysis of the four plasmid genes required to produce the circular peptide antibiotic microcin J25. J. Bacteriol. 181: 2659-2662.
Soriano, E.V., K.R. Rajashankar, J.W. Hanes, S. Bale, T.P. Begley, and S.E. Ealick. (2008). Structural similarities between thiamin-binding protein and thiaminase-I suggest a common ancestor. Biochemistry 47: 1346-1357.
Sperandio, B., C. Gautier, S. McGovern, D.S. Ehrlich, P. Renault, I. Martin-Verstraete, and E. Guédon. (2007). Control of methionine synthesis and uptake by MetR and homocysteine in Streptococcus mutans. J. Bacteriol. 189: 7032-7044.
Stauff, D.L., D. Bagaley, V.J. Torres, R. Joyce, K.L. Anderson, L. Kuechenmeister, P.M. Dunman, and E.P. Skaar. (2008). Staphylococcus aureus HrtA is an ATPase required for protection against heme toxicity and prevention of a transcriptional heme stress response. J. Bacteriol. 190: 3588-3596.
Stewart, J.B. and M.A. Hermodson. (2003). Topology of RbsC, the membrane component of the Escherichia coli ribose transporter. J. Bacteriol. 185: 5234-5239.
Stumpe, S. and E.P. Bakker. Requirement of a large K+-uptake capacity and of extracytoplasmic protease activity for protamine resistance of Escherichia coli. Arch. Microbiol. 167: 126-136.
Suzuki, H., T. Koyanagi, S. Izuka, A. Onishi, and H. Kumagai. (2005). The yliA, -B, -C, and -D genes of Escherichia coli K-12 encode a novel glutathione importer with an ATP-binding cassette. J. Bacteriol. 187: 5861-5867.
Taga, M.E., J.L. Semmelhack, and B.L. Bassler. (2001). The LuxS-dependent autoinducer AI-2 controls the expression of an ABC transporter that functions in AI-2 uptake in Salmonella typhimurium. Mol. Microbiol. 42: 777-793.
Taga, M.E., S.T. Miller, and B.L. Bassler. (2003). Lsr-mediated transport and processing of AI-2 in Salmonella typhimurium. Mol. Microbiol. 50: 1411-1427.
Tam, R. and M.H. Saier, Jr. (1993). Structural, functional, and evolutionary relationships among extracellular solute-binding receptors of bacteria. Microbiol Rev 57: 320-346.
Tanabe, T., T. Funahashi, H. Nakao, S. Miyoshi, S. Shinoda, and S. Yamamoto. (2003). Identification and characterization of genes required for biosynthesis and transport of the siderophore vibrioferrin in Vibrio parahaemolyticus. J. Bacteriol. 185: 6938-6949.
Taniguchi, N. and H. Tokuda. (2008). Molecular events involved in a single cycle of ligand transfer from an ATP binding cassette transporter, LolCDE, to a molecular chaperone, LolA. J. Biol. Chem. 283: 8538-8544.
Tauch, A., S. Krieft, A. Pühler, and J. Kalinowski. (1999). The tetAB genes of the Corynebacterium striatum R-plasmid pTP10 encode an ABC transporter and confer tetracycline, oxytetracycline and oxacillin resistance in Corynebacterium glutamicum. FEMS Microbiol. Lett. 173: 203-209.
Terasaka, K., J.J. Blakeslee, B. Titapiwatanakun, W.A. Peer, A. Bandyopadhyay, S.N. Makam, O.R. Lee, E.L. Richards, A.S. Murphy, F. Sato, and K. Yazaki. (2005). PGP4, an ATP binding cassette P-glycoprotein, catalyzes auxin transport in Arabidopsis thaliana roots. Plant Cell 17: 2922-2939.
Thöny-Meyer, L. (1997). Biogenesis of respiratory cytochromes in bacteria. Microbiol. Mol. Biol. Rev. 61: 337-376.
Thompson, S.A., O.L. Shedd, K.C. Ray, M.H. Beins, J.P. Jorgensen, and M.J. Blaser. (1998). Campylobacter fetus surface layer proteins are transported by a type I secretion system. J. Bacteriol. 180: 6450-6458.
Tikhonova, E.B., V.K. Devroy, S.Y. Lau, and H.I. Zgurskaya. (2007). Reconstitution of the Escherichia coli macrolide transporter: the periplasmic membrane fusion protein MacA stimulates the ATPase activity of MacB. Mol. Microbiol. 63: 895-910.
Tjalsma, H., A. Bolhuis, J.D. Jongbloed, S. Bron, and J.M. van Dijl. (2000). Signal peptide-dependent protein transport in Bacillus subtilis: a genome-based survey of the secretome. Microbiol. Mol. Biol. Rev. 64: 515-547.
Tommasini, R., E. Vogt, M. Fromenteau, S. Hörtensteiner, P. Matile, N. Amrhein, and E. Martinoia. (1998). An ABC-transporter of Arabidopsis thaliana has both glutathione-conjugate and chlorophyll catabolite transport activity. Plant J. 13: 773-780.
Torres, C., C. Galián, C. Freiberg, J.R. Fantino, and J.M. Jault. (2009). The YheI/YheH heterodimer from Bacillus subtilis is a multidrug ABC transporter. Biochim. Biophys. Acta. 1788: 615-622.
Tsujibo, H., M. Kosaka, S. Ikenishi, T. Sato, K. Miyamoto, and Y. Inamori. (2004). Molecular characterization of a high-affinity xylobiose transporter of Streptomyces thermoviolaceus OPC-520 and its transcriptional regulation. J. Bacteriol. 186: 1029-1037.
Tsuruoka, S., K. Ishibashi, H. Yamamoto, M. Wakaumi, M. Suzuki, G.J. Schwartz, M. Imai, and A. Fujimura. (2002). Functional analysis of ABCA8, a new drug transporter. Biochem. Biophys. Res. Commun. 298: 41-45.
Turi, T.G. and J.K. Rose. (1995). Characterization of a novel Schizosaccharomyces pombe multidrug resistance transporter conferring brefeldin A resistance. Biochem. Biophys. Res. Commun. 213: 410-418.
Ueda, K., K. Oinuma, G. Ikeda, K. Hosono, Y. Ohnishi, S. Horinouchi, and T. Beppu. (2002). AmfS, an extracellular peptidic morphogen in Streptomyces griseus. J. Bacteriol. 184: 1488-1492.
Valladares, A., M.L. Montesinos, A. Herrero, and E. Flores. (2002). An ABC-type, high-affinity urea permease identified in cyanobacteria. Mol. Microbiol. 43: 703-715.
Van Bibber, M., C. Bradbeer, N. Clark, and J.R. Roth. (1999). A new class of cobalamin transport mutants (btuF) provides genetic evidence for a periplasmic binding protein in Salmonella typhimurium. J. Bacteriol. 181: 5539-5541.
van der Does, C., C. Presenti, K. Schulze, S. Dinkelaker, and R. Tampé. (2006). Kinetics of the ATP hydrolysis cycle of the nucleotide-binding domain of Mdl1 studied by a novel site-specific labeling technique. J. Biol. Chem. 281: 5694-5701.
van der Heide, T. and B. Poolman. (2002). ABC transporters: one, two or four extracytoplasmic substrate-binding sites? EMBO Rep 3: 938-943.
van der Ploeg, J.R., M.A. Weiss, E. Saller, H. Nashimoto, N. Saito, M.A. Kertesz, and T. Leisinger. (1996). Identification of sulfate starvation-regulated genes in Escherichia coli: a gene cluster involved in the utilization of taurine as a sulfur source. J. Bacteriol. 178: 5438-5446.
van Endert, P.M. (1999). Role of nucleotides and peptide substrate for stability and functional state of the human ABC family transporters associated with antigen processing. J. Biol. Chem. 274: 14632-14638.
van Roermund, C.W., W.F. Visser, L. Ijlst, A. van Cruchten, M. Boek, W. Kulik, H.R. Waterham, and R.J. Wanders. (2008). The human peroxisomal ABC half transporter ALDP functions as a homodimer and accepts acyl-CoA esters. FASEB J. 22: 4201-4208.
van Veen, H.W. and W.N. Konings. (1998). The ABC family of multidrug transporters in microorganisms. Biochim. Biophys. Acta. 1365: 31-36.
van Veen, H.W., A. Margolles, M. Müller, C.F. Higgins, and W.N. Konings. (2000). The homodimeric ATP-binding cassette transporter LmrA mediates multidrug transport by an alternating two-site (two-cylinder engine) mechanism. EMBO. J. 19: 2503-2514.
Vatamaniuk, O.K., E.A. Bucher, M.V. Sundaram, and P.A. Rea. (2005). CeHMT-1, a putative phytochelatin transporter, is required for cadmium tolerance in Caenorhabditis elegans. J. Biol. Chem. 280: 23684-23690.
Velamakanni, S., Y. Yao, D.A. Gutmann, and H.W. van Veen. (2008). Multidrug transport by the ABC transporter Sav1866 from Staphylococcus aureus. Biochemistry 47: 9300-9308.
Villarreal, D.M., C.L. Phillips, A.M. Kelley, S. Villarreal, A. Villaloboz, P. Hernandez, J.S. Olson, and D.P. Henderson. (2008). Enhancement of recombinant hemoglobin production in Escherichia coli BL21(DE3) containing the Plesiomonas shigelloides heme transport system. Appl. Environ. Microbiol. 74: 5854-5856.
Vincent, P.A. and R.D. Morero. (2009). The structure and biological aspects of peptide antibiotic microcin J25. Curr. Med. Chem. 16: 538-549.
Wakabayashi, K., H. Nakagawa, A. Tamura, S. Koshiba, K. Hoshijima, M. Komada, and T. Ishikawa. (2007). Intramolecular disulfide bond is a critical check point determining degradative fates of ATP-binding cassette (ABC) transporter ABCG2 protein. J. Biol. Chem. 282: 27841-27846.
Wakabayashi, Y., H. Kipp, and I.M. Arias. (2006). Transporters on demand: intracellular reservoirs and cycling of bile canalicular ABC transporters. J. Biol. Chem. 281: 27669-27673.
Walshaw, D.L. and P.S. Poole. (1996). The general L-amino acid permease of Rhizobium leguminosarum is an ABC uptake system that also influences efflux of solutes. Mol. Microbiol. 21: 1239-1252.
Walshaw, D.L., S. Lowthorpe, A. East, and P.S. Poole. (1997). Distribution of a sub-class of bacterial ABC polar amino acid transporter and identification of an N-terminal region involved in solute specificity. FEBS Lett. 414: 397-401.
Wang, F., X. Xiao, A. Saito, and H. Schrempf. (2002). Streptomyces olivaceoviridis possesses a phosphotransferase system that mediates specific, phosphoenolpyruvate-dependent uptake of N-acetylglucosamine. Mol. Genet. Genomics 268: 344-351.
Wang, H., E.W. Lee, X. Cai, Z. Ni, L. Zhou, and Q. Mao. (2008). Membrane topology of the human breast cancer resistance protein (BCRP/ABCG2) determined by epitope insertion and immunofluorescence. Biochemistry 47: 13778-13787.
Wang, J., F. Sun, D.W. Zhang, Y. Ma, F. Xu, J.D. Belani, J.C. Cohen, H.H. Hobbs, and X.S. Xie. (2006). Sterol transfer by ABCG5 and ABCG8: in vitro assay and reconstitution. J. Biol. Chem. 281: 27894-27904.
Wang, Y., T.W. Loo, M.C. Bartlett, and D.M. Clarke. (2007). Correctors promote maturation of cystic fibrosis transmembrane conductance regulator (CFTR)-processing mutants by binding to the protein. J. Biol. Chem. 282: 33247-33251.
Ward, A., C.L. Reyes, J. Yu, C.B. Roth, and G. Chang. (2007). Flexibility in the ABC transporter MsbA: Alternating access with a twist. Proc. Natl. Acad. Sci. USA 104: 19005-19010.
Watanabe, S., Y. Oguchi, N. Yokota, and H. Tokuda. (2007). Large-scale preparation of the homogeneous LolA lipoprotein complex and efficient in vitro transfer of lipoproteins to the outer membrane in a LolB-dependent manner. Protein. Sci. 16: 2741-2749.
Webb, A.J. and A.H. Hosie. (2006). A member of the second carbohydrate uptake subfamily of ATP-binding cassette transporters is responsible for ribonucleoside uptake in Streptococcus mutans. J. Bacteriol. 188: 8005-8012.
Webb, A.J., K.A. Homer, and A.H. Hosie. (2008). Two closely related ABC transporters in Streptococcus mutans are involved in disaccharide and/or oligosaccharide uptake. J. Bacteriol. 190: 168-178.
Webb, E., K. Claas, and D. Downs. (1998). thiBPQ encodes an ABC transporter required for transport of thiamine and thiamine pyrophosphate in Salmonella typhimurium. J. Biol. Chem. 273: 8946-8950.
White, J.P., J. Prell, V.K. Ramachandran, and P.S. Poole. (2009). Characterization of a {gamma}-aminobutyric acid transport system of Rhizobium leguminosarum bv. viciae 3841. J. Bacteriol. 191: 1547-1555.
Willis, L.B. and G.C. Walker. (1999). A novel Sinorhizobium meliloti operon encodes an α-glucosidase and a periplasmic-binding-protein-dependent transport system for α-glucosides. J. Bacteriol. 181: 4176-4184.
Woodson, J.D., A.A. Reynolds, and J.C. Escalante-Semerena. (2005). ABC transporter for corrinoids in Halobacterium sp. strain NRC-1. J. Bacteriol. 187: 5901-5909.
Wooff, E., S.L. Michell, S.V. Gordon, M.A. Chambers, S. Bardarov, W.R. Jacobs, Jr, R.G. Hewinson, and P.R. Wheeler. (2002). Functional genomics reveals the sole sulphate transporter of the Mycobacterium tuberculosis complex and its relevance to the acquisition of sulphur in vivo. Mol. Microbiol. 43: 653-663.
Wu, L.F. and M.A. Mandrand-Berthelot. (1995). A family of homologous substrate-binding proteins with a broad range of substrate specificity and dissimilar biological functions. Biochimie 77: 744-750.
Wu, T.K., Y.K. Wang, Y.C. Chen, J.M. Feng, Y.H. Liu, and T.Y. Wang. (2007). Identification of a Vibrio furnissii oligopeptide permease and characterization of its in vitro hemolytic activity. J. Bacteriol. 189: 8215-8223.
Xu, C., J. Fan, W. Riekhof, J.E. Froehlich, and C. Benning. (2003). A permease-like protein involved in ER to thylakoid lipid transfer in Arabidopsis. EMBO. J. 22: 2370-2379.
Xu, J., Y. Liu, Y. Yang, S. Bates, and J.T. Zhang. (2004). Characterization of oligomeric human half-ABC transporter ATP-binding cassette G2. J. Biol. Chem. 279: 19781-19789.
Xu, Y., S.H. Sim, K.H. Nam, X.L. Jin, H.M. Kim, K.Y. Hwang, K. Lee, and N.C. Ha. (2009). Crystal structure of the periplasmic region of MacB, a noncanonic ABC transporter. Biochemistry 48: 5218-5225.
Yamanaka, H., H. Kobayashi, E. Takahashi, and K. Okamoto. (2008). MacAB is involved in the secretion of Escherichia coli heat-stable enterotoxin II. J. Bacteriol. 190: 7693-7698.
Yang, K., M. Wang, and W.W. Metcalf. (2009). Uptake of glycerol-2-phosphate via the ugp-encoded transporter in Escherichia coli K12. J. Bacteriol. [Epub: Ahead of Print]
Yoneyama, F., Y. Imura, K. Ohno, T. Zendo, J. Nakayama, K. Matsuzaki, and K. Sonomoto. (2009). Peptide-lipid huge toroidal pore: a new antimicrobial mechanism mediated by a lactococcal bacteriocin, lacticin Q. Antimicrob. Agents Chemother. [Epub: Ahead of Print]
Yoshimura, K. and T. Kouyama. (2008). Structural role of bacterioruberin in the trimeric structure of archaerhodopsin-2. J. Mol. Biol. 375: 1267-1281.
Yoshiura, K., A. Kinoshita, T. Ishida, A. Ninokata, T. Ishikawa, T. Kaname, M. Bannai, K. Tokunaga, S. Sonoda, R. Komaki, M. Ihara, V.A. Saenko, G.K. Alipov, I. Sekine, K. Komatsu, H. Takahashi, M. Nakashima, N. Sosonkina, C.K. Mapendano, M. Ghadami, M. Nomura, D.S. Liang, N. Miwa, D.K. Kim, A. Garidkhuu, N. Natsume, T. Ohta, H. Tomita, A. Kaneko, M. Kikuchi, G. Russomando, K. Hirayama, M. Ishibashi, A. Takahashi, N. Saitou, J.C. Murray, S. Saito, Y. Nakamura, and N. Niikawa. (2006). A SNP in the ABCC11 gene is the determinant of human earwax type. Nat. Genet. 38: 324-330.
Yost, C.K., A.M. Rath, T.C. Noel, and M.F. Hynes. (2006). Characterization of genes involved in erythritol catabolism in Rhizobium leguminosarum bv. viciae. Microbiology 152: 2061-2074.
Young, J. and I.B. Holland. (1999). ABC transporters: bacterial exporters-revisited five years on. Biochim. Biophys. Acta. 1461: 177-200.
Young, L., K. Leonhard, T. Tatsuta, J. Trowsdale, and T. Langer. (2001). Role of the ABC transporter Mdl1 in peptide export from mitochondria. Science 291: 2135-2138.
Yum, S., Y. Xu, S. Piao, S.H. Sim, H.M. Kim, W.S. Jo, K.J. Kim, H.S. Kweon, M.H. Jeong, H. Jeon, K. Lee, and N.C. Ha. (2009). Crystal structure of the periplasmic component of a tripartite macrolide-specific efflux pump. J. Mol. Biol. 387: 1286-1297.
Zhang, D.W., G.A. Graf, R.D. Gerard, J.C. Cohen, and H.H. Hobbs. (2006). Functional asymmetry of nucleotide-binding domains in ABCG5 and ABCG8. J. Biol. Chem. 281: 4507-4516.
Zhang, H., J.P. Herman, H. Bolton, Jr, Z. Zhang, S. Clark, and L. Xun. (2007). Evidence that bacterial ABC-type transporter imports free EDTA for metabolism. J. Bacteriol. 189: 7991-7997.
Zhang, L. and T.F. Mah. (2008). Involvement of a novel efflux system in biofilm-specific resistance to antibiotics. J. Bacteriol. 190: 4447-4452.
Zhang, Y. and V.N. Gladyshev. (2008). Molybdoproteomes and evolution of molybdenum utilization. J. Mol. Biol. 379: 881-899.
Zhang, Z., J.N. Feige, A.B. Chang, I.J. Anderson, V.M. Brodianski, A.G. Vitreschak, M.S. Gelfand, and M.H. Saier, Jr. (2003). A transporter of Escherichia coli specific for L- and D-methionine is the prototype for a new family within the ABC superfamily. Arch. Microbiol. 180: 88-100.
Zhao, C., W. Haase, R. Tampé, and R. Abele. (2008). Peptide specificity and lipid activation of the lysosomal transport complex ABCB9 (TAPL). J. Biol. Chem. 283: 17083-17091.
 

Examples:

TC#NameOrganismal TypeExample
3.A.1.1 The Carbohydrate Uptake Transporter-1 (CUT1) Family
3.A.1.1.1Maltooligosaccharide porter. The 3-D structure has been reported by Oldham et al. (2007).MalEFGK of E. coli
MalE (receptor [R])
MalF (membrane [M])
MalG (membrane [M])
MalK (cytoplasmic [C])
 
3.A.1.1.2Multiple sugar (melibiose; raffinose, etc.) porterMsmEFGK of Streptococcus mutans
MsmE (R)
MsmF (M)
MsmG (M)
MsmK (C)
 
3.A.1.1.3Glycerol-phosphate porter. Transports both glycerol-3-P and glycerol-2-P (Yang et al. 2009).

UgpABCE of E. coli
UgpB (R)
UgpA (M)
UgpE (M)
UgpC (C)

 
3.A.1.1.4Lactose porterLacEFGK of Agrobacterium radiobacter
LacE (R)
LacF (M)
LacG (M)
LacK (C)
 
3.A.1.1.5Hexitol (glucitol; mannitol) porterSmoEFGK of Rhodobacter sphaeroides
SmoE (R)
SmoF (M)
SmoG (M)
SmoK (C)
 
3.A.1.1.6Cyclodextrin porterCymDEFG of Klebsiella oxytoca
CymE (R)
CymF (M)
CymG (M)
CymD (C)
 
3.A.1.1.7Maltose/trehalose porterMalEFGK of Thermococcus litoralis
MalE (R)
MalF (M)
MalG (M)
MalK (C) (not sequenced)
 
3.A.1.1.8Sucrose/maltose/trehalose porter (sucrose-inducible)AglEFGK of Sinorhizobium meliloti
AglE (R)
AglF (M)
AglG (M)
AglK (C)
 
3.A.1.1.9α-D-glucuronate porterGuaEFG(K?) of Bacillus stearothermophilus
GuaE (Orf2) (R)
GuaF (Orf3) (M)
GuaG (Orf4) (M)
GuaK (C) (not sequenced)
 
3.A.1.1.10Alginate (MW 27,000 Da) (and Alginate oligosaccharides) uptake porter. Sphingomonas species A1 is a 'pit-forming' bacterium that directly incorporates alginate into its cytoplasm through a pit-dependent transport system, termed a 'superchannel' (Murata et al., 2008). The pit is a novel organ acquired through the fluidity and reconstitution of cell surface molecules, and through cooperation with the transport machinery in the cells. It confers upon bacterial cells a more efficient way to secure and assimilate macromolecules (Murata et al., 2008).AlgSM1M2Q1Q2 of Sphingomonas sp.A1
AlgS (C)
AlgM1 (M)
AlgM2 (M)
AlgQ1 (R)
AlgQ2 (R)
 
3.A.1.1.11Saturated and unsaturated oligogalacturonide transporter, TogMNAB (transports di- to tetrasaccharide pectin degradation products which consist of D-galacuronate, sometimes with 4-deoxy-L-threo-5-hexosulose uronate at the reducing end of the oligosaccharide)Oligogalacturonide transporter TogMNAB of Erwinia chrysanthemi
TogM (M)
TogN (M)
TogA (C)
TogB (R)
 
3.A.1.1.12Palatinose (isomaltulose; 6-O-α-D-glucopyranosyl-D-fructose) uptake porterPalEFGK of Erwinia rhapontici
PalE (R)
PalF (M)
PalG (M)
PalK (C)
 
3.A.1.1.13Glucose, mannose, galactose porterGlcSTUV of Sulfolobus solfataricus
GlcS (R)
GlcT (M)
GlcU (M)
GlcV (C)
 
3.A.1.1.14Arabinose, fructose, xylose porterAraSTUV of Sulfolobus solfataricus
AraS (R)
AraT (M)
AraU (M)
AraV (C)
 
3.A.1.1.15Trehalose porterTreSTUV of Sulfolobus solfataricus
TreS (R)
TreT (M)
TreU (M)
TreV (C)
 
3.A.1.1.16Maltooligosaccharide porter (Maltose is not a substrate, but maltotriose is.)PF1933, 1936, 1937, 1938 of Pyrococcus furiosus
PF1938 (R)
PF1937 (M)
PF1936 (M)
PF1933 (C)
 
3.A.1.1.17Trehalose/maltose/sucrose porter (trehalose inducible)ThuEFGK of Sinorhizobium meliloti
ThuE (R)
ThuF (M)
ThuG (M)
ThuK (C)
 
3.A.1.1.18N-Acetylglucosamine/N,N'-diacetyl chitobiose porter (NgcK (C) not identified)NgcEFG of Streptomyces olivaceoviridis
NgcE (R)
NgcF (M)
NgcG (M)
 
3.A.1.1.19Platinose (isomaltulose) (6-O-α-D-glucopyranosyl-D-fructofuranose) porterPalEFGK of Agrobacterium tumefaciens
PalE (R)
PalF (M)
PalG (M)
PalK (C)
 
3.A.1.1.20The fructooligosaccharide porter, MsmEFGK (Barrangou et al., 2003) BacteriaMsmEFGK of Lactobacillus acidophilus
MsmE (R) AAO21856
MsmF (M) AAO21857
MsmG (M) AAO21858
MsmK (C) AAO21860
 
3.A.1.1.21The xylobiose porter; BxlEFG(K) (Tsujibo et al., 2004)BacteriaBxlEFGK of Streptomyces thermoviolaceus
BxlE (R) CAB88161
BxlF (M) CAB88162
BxlG (M) CAB88163
BxlK (C) Unknown
 
3.A.1.1.22

The maltose, maltotriose, mannotetraose (MalE1)/maltose, maltotriose, trehalose (MalE2) porter (Nanavati et al., 2005). For MalG1 (823aas) and MalG2 (833aas), the C-terminal transmembrane domain with 6 putative TMSs is preceded by a single N-terminal TMS and a large (600 residue) hydrophilic region showing sequence similarity to MLP1 and 2 (9.A.14; e-12 & e-7) as well as other proteins.

MalE1E2FGK of Thermotoga maritima
MalE1 (R) (binds maltose, maltotriose and mannotetraose) (AAD36279)
MalE2 (R) (binds maltose, maltotriose and trehalose) (AAD36901)
MalF1 (M) (AAD36278)
MalG1 (M) (AAD36277)
[MalG2 (M) (AAD36899]
MalK (C) (AAD36351)

 
3.A.1.1.23The cellobiose/cellotriose (and possibly higher cellooligonucleosides), CebEFGMsiK [MsiK functions to energize several ABC transporters including those for maltose/maltotriose and trehalose] (Schlösser et al., 1997, 1999)BacteriaCebEFGMsiK of Streptomyces reticuli
CebE (R) (CAB46342)
CebF (M) (CAB46343)
CebG (M) (CAB46344)
MsiK (CAA70125)
 
3.A.1.1.24The glucose/mannose porter TTC0326-8 plus MalK1 (ABC protein, shared with 3.A.1.1.25) (Chevance et al., 2006).BacteriaTTC0326-8 + MalK1 of Thermus Thermophilus
TTC0326 (M) - Q72KX4
TTC0327 (M) - Q72KX3
TTC0328 (R) - Q72KX2
MalK1 or TTC0211 (C) - Q72L52
 
3.A.1.1.25The trehalose/maltose/sucrose/palatinose porter (TTC1627-9) plus MalK1 (ABC protein, shared with 3.A.1.1.24) (Chevance et al., 2006).BacteriaTTC1627-9 + MalK1 of Thermus thermophilus
TTC1627 (R) (Q72H68)
TTC1628 (M) (Q72H67)
TTC1629 (M) (Q72H66)
MalK1 (TTC0211) (C) (Q72L52)
 
3.A.1.1.26The maltose porter, MdxEFG and MsmXBacteriaThe maltose porter of Bacillus subtilis, MalEFG/MsmX.
MalE (R) - O06989
MalF (M) - O06990
MalG (M) - O06991
MsmX (C) - P94360
 
3.A.1.1.27Maltose/Maltotriose/maltodextrin (up to 7 glucose units) transporters MalXFGK (MsmK (3.A.1.1.28) can probably substitute for MalK; Webb et al, 2007).BacteriaMalXFGK of Streptococcus mutans:
MalX (R) (Q8DT28)
MalF (M) (Q8DT27)
MalG (M) (Q8DT26)
MalK (C) (Q8DT25)
 
3.A.1.1.28The raffinose/stachyose transporter, MsmEFGK (MalK (3.A.1.1.27) can probably substitute for MsmK; Webb et al., 2007).BacteriaMsmEFGK of Streptococcus mutans:
MsmE (Q00749)
MsmF (Q00750)
MsmG (Q00751)
MsmK (Q00752)
 
3.A.1.1.29Aldouronate transporter, LplA,B,C (Chow et al., 2007)BacteriaLplABC of Paenibacillus sp. JDR-2:
LplA (R)(A9QDR6)
LplB (M)(A9QDR7)
YtcP (M)(A9QDR8)
LplC - not identified
 
3.A.1.1.30Glucose porter, GtsABCD (Del Castillo et al., 2008)BacteriaThe glucose porter of Pseudomonas putida, GtsABCD:
GtsA (R) (Q88P38)
GtsB (M) (Q88P37)
GtsC (M) (Q88P36)
GtsD (C) (Q88P35)
 
3.A.1.1.31Glucose uptake porter, GlcABCD (Basa et al., 2007)GlcABCD of Pseudomonas putida (most like 3.A.1.1.24)
GlcE (R) (Q88P38)
GlcF (M) (Q88P37)
GlcG (M) (Q88P36)
GlcK (C) (Q88P35)
 
3.A.1.1.32The glucosylglycerol uptake transporter (functions in osmoprotection and also transports sucrose and trehalose (Mikkat and Hagemann, 2000) (most similar to 3.A.1.1.8).BacteriaGgtABCD of Synechocystis sp. strain PCC6803
GgtA (C) (Q55035)
GgtB (R) (Q55471)
GtC (M) (Q55472)
GgTD (M) (Q55473)
 
3.A.1.1.33The N,N'-diacetylchitobiose uptake transporter, DasABC/MsiK (MsiK energizes several ABC transporters (see 3.A.1.1.23)) (Saito et al., 2008)

Bacteria

DasABC MsiK of Streptomyces coelicolor
DasA (R) (Q8KN19)
DasB (M) (Q8KN18)
DasC (M) (Q8KN17)
MsiK (C) (Q9L0Q1)

 
3.A.1.2 The Carbohydrate Uptake Transporter-2 (CUT2) Family
3.A.1.2.1Ribose porter (RbsC has 10 TMSs with N- and C-termini in the cytoplasm (Stewart and Hermodson, 2003))RbsABCD of E. coli
RbsA (C)
RbsB (R)
RbsC (M)
 
3.A.1.2.2Arabinose porterAraFGH of E. coli
AraF (R)
AraG (C)
AraH (M)
 
3.A.1.2.3Galactose/glucose (methyl galactoside) porterMglABC of E. coli
MglA (C)
MglB (R)
MglC (M)
 
3.A.1.2.4Xylose porterXylFGH of E. coli
XylF (R)
XylG (C)
XylH (M)
 
3.A.1.2.5Multiple sugar (arabinose, xylose, galactose, glucose, fucose) putative porterChvE, GguAB of Agrobacterium tumefaciens
ChvE (R)
GguA (C)
GguB (M)
 
3.A.1.2.6D-allose porterAlsABC of E. coli
AlsB (R)
AlsA (C)
AlsC (M)
 
3.A.1.2.7Fructose/mannose/ribose porterFrcABC of Sinorhizobium meliloti
FrcA (C)
FrcB (R)
FrcC (M)
 
3.A.1.2.8AI2 autoinducer porter (Taga et al., 2001, 2003)LsrACDB of E. coli
LsrB (R) AAC74589
LsrA (C) AAC74586
LsrC (M) AAC74587
LsrD (M) AAC74588
 
3.A.1.2.9Rhamnose porter (Richardson et al., 2004) (Transport activity is dependent on rhamnokinase (RhaK; AAQ92412) activity (Richardson and Oresnik, 2007) This could be an example of group translocation!)RhaSTP of Rhizobium leguminosarum bv. trifolii
RhaS (R) AAQ92407
RhaT (C) AAQ92408
RhaP (M) AAQ92409
 
3.A.1.2.10The purine nucleoside permease (probably transports guanosine, adenosine, 2'-deoxyguanosine, inosine and xanthosine with decreasing affinity in this order) (Deka et al., 2006)PnrA-E of Treponema pallidum
PnrA (R) (TmpC; Tp0319) (P29724)
PnrB (?51 aas; 1 TMS; Tp0320) (O83340)
PnrC (C) (533 aas; duplicated; Tp0321) (NP_218761)
PnrD (M) (400 aas; 10 TMSs; Tp0322) (NP_218762)
PnrE (M) (316 aas; 10 TMSs; Tp0323) (NP_218763)
 
3.A.1.2.11The erythritol permease, EryEFG (Yost et al., 2006)BacteriaEryEFG of Sinorhizobium meliloti
EryE (C) (CAC48737)
EryF (M) (CAC48738)
EryG (R) (CAC48735)
 
3.A.1.2.12The (deoxy)ribonucleoside permease; probably takes up all deoxy- and ribonucleosides (cytidine, uridine, adenosine and toxic analogues, fluorocytidine and fluorouridine tested), but not ribose or nucleobases (Webb and Hosie, 2006)BacteriaRnsABCD of Streptococcus mutans
RnsA (R) (AAN58814)
RnsB (C) (AAN58813)
RnsC (M) (AAN58812)
RnsD (M) (AAN58811)
 
3.A.1.2.13The probable autoinducer 2 (AI2) uptake porter (Shao et al., 2007) (50-70% identical to RbsABC of E. coli; TC# 3.A.1.2.1)BacteriaRbsDABC of Aggregatibacter actinomycetemcomitans (Actinobacillus succinogens)
RbsA(C) (A6VKS8)
RbsB(R) (A6VKT0)
RbsC(M) (A6VKS9)
 
3.A.1.3 The Polar Amino Acid Uptake Transporter (PAAT) Family
3.A.1.3.1Histidine; arginine/lysine/ornithine porterHisJ (histidine receptor)-ArgT (arg/lys/orn receptor)-HisMPQ of Salmonella typhimurium
HisJ (R)
ArgT (R)
HisM (M)
HisQ (M)
HisP (C)
 
3.A.1.3.2Glutamine porterGlnHPQ of E. coli
GlnH (R)
GlnP (M)
GlnQ (C)
 
3.A.1.3.3Arginine porterArtI (arginine receptor #1)/ArtJ (arginine receptor #2)-ArtMQP of E. coli
ArtP (C)
ArtQ (M)
ArtM (M)
ArtJ (R)
ArtI (R)
 
3.A.1.3.4Glutamate/aspartate porterGltIJKL of E. coli
GltI (R)
GltJ (M)
GltK (M)
GltL (C)
 
3.A.1.3.5Octopine porterOccQMPT of Agrobacterium tumefaciens
OccT (R)
OccQ (M)
OccM (M)
OccP (C)
 
3.A.1.3.6Nopaline porterNocQMPT of Agrobacterium tumefaciens
NocT (R)
NocQ (M)
NocM (M)
NocP (C)
 
3.A.1.3.7Glutamate/glutamine/aspartate/asparagine porterBztABCD of Rhodobacter capsulatus
BztA (R)
BztB (M)
BztC (M)
BztD (CC)
 
3.A.1.3.8General L-amino acid porter; transports basic and acidic amino acids preferentially, but also transports aliphatic amino acids (catalyzes both uptake and efflux)AapJQMP of Rhizobium leguminosarum
AapJ (R)
AapQ (M)
AapM (M)
AapP (C)
 
3.A.1.3.9Glutamate porterGluABCD of Corynebacterium glutamicum
GluA (C)
GluB (R)
GluC (M)
GluD (M)
 
3.A.1.3.10Cystine/diaminopimelateCys/Dap porter of E. coli
CysX (R)
CysY (M)
CysZ (C)
 
3.A.1.3.11Arginine/ornithine (but not lysine) porterAotJQMP of Pseudomonas aeruginosa
AotJ (R)
AotQ (M)
AotM (M)
AotP (C)
 
3.A.1.3.12Arginine/lysine/histidine/glutamine porterBgtAB of Synechocystis PCC6803
BgtA (C)
BgtB (R-M)
 
3.A.1.3.13Uptake system for L-cystine (Km=2.5 μM), L-cystathionine, L-djenkolate, and S-methyl-L-cysteine (Burguičre et al., 2004, 2005)TcyJKLMN (YtmJKLMN) of Bacillus subtilis
TcyJ (R) (NP_390816)
TcyK (R) (O34852)
TcyL (M) (O34315)
TcyM (M) (O34931)
TcyN (C) (O34900)
 
3.A.1.3.14Uptake system for L-cystine (Burguičre et al., 2004)TcyABC (YckKJI) of Bacillus subtilis
TcyA (R) (P42199)
TcyB (M) (P42200)
TcyC (C) (P39456)
 
3.A.1.3.15Putative uptake system for arginine, YqiXYZ (Sekowska et al., 2001)BacteriaYqiXYZ of Bacillus subtilis
YqiX (R) (P54535)
YqiY (M) (P54536)
YqiZ (C) (P54537)
 
3.A.1.3.16Uptake system for glutamate and aspartate (Leon-Kempis et al., 2006)PEB1 transport system Campylobacter jejuni
PEB1a (R) (Q0P9X8)
PED1b (M) (A1VZQ3)
PEB1c (C) (A3ZI83)
 
3.A.1.3.17Basic amino acid uptake transporter, BgtAB (BgtA is shared with NatFGH/BgtA; 3.A.1.3.18; Pernil et al., 2008)BgtAB of Anabaena sp. PCC7120
BgtA (C) (Q8YPM6)
BgtB (R-M) (Q8YSA2)
 
3.A.1.3.18Acidic and neutral amino acid uptake transporter NatFGH/BgtA. BgtA is shared with BgtAB (3.A.1.3.17; Pernil et al., 2008)NatFGH-BgtA of Anabaena sp. PCC7120
BgtA (C) (Q8YPM6)
NatF (R) (Q8YPM9)
NatG (M) (Q8YPM8)
NatH (M) (Q8YPM7)
 
3.A.1.3.19Acidic amino acid uptake porter, AatJMQP (Singh and Röhm, 2008)BacteriaAatJMQP of Pseudomonas putida
AatJ (R) Q88NY2
AatM (M) Q88NY3
AatQ (M) Q88NY4
AatP (C) Q88NY5
 
3.A.1.3.20The ectoine/hydroxyectoine uptake porter, EhuABCD (Crystal structure of EhuB has been determined; Hanekop et al., 2007)BacteriaEhuABCD of Sinorhizobium meliloti
EhuA (C) Q92WC9
EhuB (R) Q92WC8
EhuC (M) Q92WC7
EhuD (M) Q92WC6
 
3.A.1.4 The Hydrophobic Amino Acid Uptake Transporter (HAAT) Family
3.A.1.4.1Leucine; leucine/isoleucine/valine porter (also transports phenylalanine and tyrosine; Koyanagi et al., 2004)LivK (leucine-specific receptor)-LivJ (Leu/Ile/Val receptor)-LivHMGF of E. coli
LivJ (R)
LivK (R)
LivH (M)
LivM (M)
LivG (C)
LivF (C)
 
3.A.1.4.2Leucine/proline/alanine/serine/glycine (and possibly histidine) porterNatA-E neutral amino acid porter of Synechocystis sp.PCC6803
NatA (C)
NatB (R)
NatC (M)
NatD (M)
NatE (C)
 
3.A.1.4.3General L- (and D-)amino acid uptake porter (transports acidic, basic, polar, semipolar and hydrophobic amino acids). The amino and carboxyl groups do not need to be α since γ-aminobutyric acid (GABA) is a substrate. The system may function with additional binding proteins since L-alanine uptake is not dependent on BraC.BraCDEF of Rhizobium leguminosarum
BraC (R)
BraD (M)
BraE (M)
BraF (C)
 
3.A.1.4.4The high-affinity (<1 μM) urea porterUrtA-E urea porter of Anabaena sp. PCC7120
UrtA (R)
UrtB (M)
UrtC (M)
UrtD (C)
UrtE (C)
 
3.A.1.4.5The high affinity urea/thiourea/hydroxyurea porter (Beckers et al., 2004)UrtA-E of Corynebacterium glutamicum
UrtA (R) CAF19637
UrtB (M) CAF19636
UrtC (M) CAF19638
UrtD (C) CAF19639
UrtE (C) CAF19640
 
3.A.1.4.6The neutral amino acid permease, N-1 (transports pro, phe, leu, gly, ala, ser, gln and his, but gln and his are not transported via NatB) (Picossi et al., 2005)NatA-E of Anabaena sp. strain PCC7120
NatA (C) BAB73003
NatB (R) BAB73533
NatC (M) BAB73004
NatD (M) BAB73241
NatE (C) BAB74611
 
3.A.1.5 The Peptide/Opine/Nickel Uptake Transporter (PepT) Family
3.A.1.5.1Oligopeptide porter (also takes up amino glycoside antibiotics such as kanamycin, streptomycin and neomycin as well as cell wall-derived peptides such as murein tripeptide). It transports substrate peptides of 2-5 amino acids with highest affinity for tripeptides. Also transports δ-aminolevulinic acid (ALA). [May be regulated by PTS Enzyme INtr-aspartokinase.] ATP-binding to OppDF may result in donation of peptide to OppBC and simultaneous release of OppA (Doeven et al., 2008).OppABCDF of Salmonella typhimurium
OppA (R)
OppB (M)
OppC (M)
OppD (C)
OppF (C)
MppA (R) (in E. coli)
 
3.A.1.5.2Dipeptide porter. Also transports δ-aminolevulinic acid (ALA) and heme (Létoffé et al., 2008).

DppABCDE of Bacillus subtilis
DppA (C)
DppB (M)
DppC (M)
DppD (C)
DppE (R)

 
3.A.1.5.3Nickel porterNikABCDE of E. coli
NikA (R)
NikB (M)
NikC (M)
NikD (C)
NikE (C)
 
3.A.1.5.4Agrocinopine (an opine)/Agrocin 84 (an antibiotic) porter (Kim and Farrand, 1997)AccABCDE of Agrobacterium tumefaciens
AccA (R)
AccB (C)
AccC (C)
AccD (M)
AccE (M)
 
3.A.1.5.5Probable cationic peptide porter (may also take up peptide antibiotics and protamine; implicated in K+ homeostasis) [SapD can stimulate the K+ uptake activities of TrkH and TrkG (TC #2.A.38.1.1) in the presence of ATP] (Mason et al., 2006)BacteriaSapABCDF of Salmonella typhimurium
SapA (R)
SapB (M)
SapC (M)
SapD (C)
SapF (C)
 
3.A.1.5.6The β-glucoside (cellobiose (β-1,4), cellotriose, cellotetraose, cellopentaose, laminaribiose (β-1,3), laminaritriose, sophorose) uptake porter, CbtABCDFArchaeaThe β-glucoside uptake porter of Pyrococcus furiosus, CbtABCDF
CbtA (R)
CbtB (M)
CbtC (M)
CbtD (C)
CbtF (C)
 
3.A.1.5.7The α-galactoside (melibiose, raffinose) uptake porter, AgpABCDFBacteriaThe α-galactoside uptake porter of Rhizobium meliloti
AgpA (R)
AgpB (M) (not identified)
AgpC (M) (not identified)
AgpD (C) (not identified)
AgpF (C) (not identified)
 
3.A.1.5.8

Maltose and maltooligosaccharide porter

Archaea

MalEFGK of Sulfolobus solfataricus
MalE (R)
MalF (M)
MalG (M)
MalK (C-C)

 
3.A.1.5.9Cellobiose and cellooligosaccharide porterArchaeaCbtABCDF of Sulfolobus solfataricus
CbtA (R)
CbtB (M)
CbtC (M)
CbtD (C)
CbtF (C)
 
3.A.1.5.10Oligopeptide porter (transports peptides of 4-35) amino acyl residues; di- and tripeptides are not transported; hydrophobic basic peptides are preferred). OppA determines the specificity of the system (Doeven et al., 2004). A large cavity in OppA binds proline-rich peptides preferentially (Berntsson et al., 2009).

Bacteria

OppABCDF of Lactococcus lactis
OppA (R) (Q9CEK0)
OppB (M) (P0A4N7)
OppC (M) (P0A4N9)
OppD (C) (Q07733)
OppF (C) (P0A2V4)

 
3.A.1.5.11

Glutathione porter (Suzuki et al., 2005)

Bacteria

YliABCD of E. coli
YliA (C-C) (P75796)
YliB (R) (P75797)
YliC (M) (P75798)
YliD (M) (P75799)

 
3.A.1.5.12Probable rhamnose porter (Conners et al., 2005)BacteriaRtpABCDF of Thermotoga maritima
RtpA (R) (TM1067)
RtpB (M) (TM1066)
RtpC (M) (TM1065)
RtpD (C) (TM1064) Q9X0F4
RtpF (C) (TM1063) Q9X0F3
 
3.A.1.5.13Probable xylose/xyloside porter (Conners et al., 2005)BacteriaXylABCDF of Thermotoga maritima
XylA (R) (TM0071) Q9WXS6
XylB (M) (TM0072) Q9WXS7
XylC (M) (TM0073) Q9WXS8
XylD (C) (TM0074) Q9WXS9
XylF (C) (TM0075) Q9WXT5
 
3.A.1.5.14Probable cellobiose porter (Conners et al., 2005)BacteriaCbtABCDF of Thermotoga maritima
CbtA (R) (TM1223) Q9X0V0
CbtB (M) (TM1222) Q9X0U9
CbtC (M) (TM1221) Q9X0U8
CbtD (C) (TM1220) Q9X0U7
CbtF (C) (TM1219) Q9X0U6
 
3.A.1.5.15Probable mannose/mannoside porter (Conners et al., 2005)BacteriaMbtABCDF of Thermotoga maritima
MbtA (R) (TM1746) Q9X268
MbtB (M) (TM1747) Q9X269
MbtC (M) (TM1748) Q9X270
MbtD (C) (TM1749) Q9X271
MbtF (C) (TM1750) Q9X272
 
3.A.1.5.16Probable β-glucoside porter (Conners et al., 2005)BglpABCDF of Thermotoga maritima
BglpA (R) (TM0031) Q9WXN8
BglpB (M) (TM0030) Q9WXN7
BglpC (M) (TM0029) Q9WXN6
BglpD (C) (TM0028) Q9WXN5
BglpF (C) (TM0027) Q9WXN4
 
3.A.1.5.17

The proline betaine uptake porter (Alloing et al., 2006)

PrbABCD of Sinorhizobium meliloti
PrbA (R) (Q92NF1)
PrbB (M) (Q92NF0)
PrbC (M) (Q92NE9)
PrbD (C-C) (Q92NE8)

 
3.A.1.5.18The oligopeptide transporter OppA1-5, B1, C1, DF (functions with five binding proteins of differing induction properties and peptide specificities; OppA1-3 are chromosomally encoded; OppA4 and 5 are plasmid encoded.) (Medrano et al., 2007)BacteriaOppA1-5,B1,C1,D,F of Borrelia burgdorferi
OppA1 (R): O51307
OppA2 (R): O54584
OppA3 (R): O51308
OppA4 (R): O31315
OppA5 (R): O50927
OppB1 (M): O31307
OppC1 (M): O51310
OppD (C): O31309
OppF (C): O31310
 
3.A.1.5.19The major oligopeptide uptake porter, Opp-3 (of four paralogues, this is the only one that mediates nitrogen nutrition (Hiron et al., 2007).BacteriaOpp-3 of Staphylococcus aureus
OppB (M) = (Q2FZR7)
OppC (M) = (Q2FZR6)
OppD (C) = (Q2FZR5)
OppF (C) = (Q2FZR4)
OppA (R) = (Q2FZR3)
 
3.A.1.5.205-6 amino acyl oligopeptide transporter AppA-F (Koide and Hoch, 1994).BacteriaAppABCDF of Bacillus subtilis
AppA(R) (P42061)
AppB(M) (P42062)
AppC(M) (P42063)
AppD(C) (P42064)
AppF(C) (P42065)
 
3.A.1.5.21

The Microcin C uptake porter, YejABEF (other substrate unknown) (Novikova et al., 2007)

Bacteria

YejABEF of E. coli:
YejA (R) (P33913)
YejB (M) (P0AFU1)
YejE (M) (P33915)
YejF (C-C) (P33916)

 
3.A.1.5.22The peptide transporter OppA,B,C,D,F (influences biofilm formation; Lee et al., 2004). Similar to 3.A.1.5.1, OppA is similar to the Vibrio furnissii OppA that provides several functions: hemolysis, antibiotic resistance, and virulence (Wu et al., 2007).BacteriaOppABCDF of Vibrio fluvialis:
OppA (R) (Q5V9S2)
OppB (M) (Q5V9S1)
OppC (M) (Q5V9S0)
OppD (C) (Q5V9R9)
OppF (C) (Q5V9R8)
 
3.A.1.5.23

The Ethylene diamine tetraacetate (EDTA) uptake porter, EppABCD (Zhang et al., 2007).

Bacteria

EppABCD of EDTA-degrading bacterium BNC1:
EppA (R) (Q9F9T7)
EppB (M) (Q9F9T6)
EppC (M) (Q9F9T5)
EppD (C-C) (Q9F9T4)

 
3.A.1.5.24

The antimicrobial peptide (protamine, melittin, polymyxin B, human defensin (HBD)-1 and HBD-2 exporter, YejABEF (Eswarappa et al., 2008). Prefers N-formyl methionine peptides, such as Microcin C (of prokaryotic origin) to non formylated peptides (of eukaryotic origin) (Novikova et al., 2007).

YejABEF of Salmonella enterica
YejA (R) (Q8ZNK0)
YejB (M) (Q7CQ74)
YejE (M) (Q8ZNJ9)
YejF (C-C) (Q8ZNJ8)

 
3.A.1.6 The Sulfate/Tungstate Uptake Transporter (SulT) Family
3.A.1.6.1Sulfate/thiosulfate porterSbp (sulfate receptor)-CysP (thiosulfate receptor)-CysTWA of E. coli
Sbp (R)
CysP (R)
CysT (M)
CysW (M)
CysA (C)
 
3.A.1.6.2Tungstate porter. (TupA, the receptor, exhibits an extremely high affinity for tungstate (Kd <1 nM) and discriminates between tungstate and molybdate (Andreesen and Makdessi, 2007))TupABC of Eubacterium acidaminophilum
TupA (R)
TupB (M)
TupC (C)
 
3.A.1.6.3Sulfate porterCysAWT SubI-sulfate porter of Mycobacterium tuberculosis
CysA (C)
CysW (M)
CysT (M)
SubI (R)
 
3.A.1.6.4Vanadate porter (Pratte and Thiel, 2006) (most similar to TupABC (3.A.1.6.2))VupABC of Anabaena variabilis ATCC29413
VupA (R) (ABA23645)
VupB (M) (ABA23644)
VupC (C) (ABA23643)
 
3.A.1.6.5Tungsten (KM=20pM)/molybdate (KM=10nM) porter (Bevers et al., 2006)

WtpABC of Pyrococcus furiosus
WtpA (R) (Q8U4K5)
WtpB (M) (Q8U4K4)
WtpC (C) (Q8U4K3)

 
3.A.1.6.6The Molybdate/Tungstate Transporter, ModA-C (Zhang and Gladyshev, 2008).

Archaeon

ModABC of Pyrobaculum calidifontis
ModA (R) (A3MW02)
ModB (M) (A3MW01)
ModC (C) (A3MW00)

 
3.A.1.7 The Phosphate Uptake Transporter (PhoT) Family
3.A.1.7.1Phosphate porterPhoS (phosphate receptor)-PstABC of E. coli
PhoS (R)
PstA (M)
PstC (M)
PstB (C)
 
3.A.1.7.2Phosphate transporter, PstSCAB (Gebhard and Cook, 2007).PstSCAB of Mycobacterium smegmatis
PstS (R) (Q7WTY8)
PstC (M) (Q7WTY7)
PstA (M) (Q7WTY6)
PstB (C) (P0C560)
 
3.A.1.8 The Molybdate Uptake Transporter (MolT) Family
3.A.1.8.1Molybdate porterModABC of E. coli
ModA (R)
ModB (M)
ModC (C)
 
3.A.1.8.2

The molybdate/tungstate ABC transporter, ModBC. The trans-inhibited 3-d structure of ModBC, is available (3D31.A and 3D31.B)(Gerber et al., 2008)

Archaea

ModBC of Methanosarcina acetivorans
ModB (Q8TJ86)
ModC (Q8TTV2)

 
3.A.1.9 The Phosphonate Uptake Transporter (PhnT) Family
3.A.1.9.1Phosphonate/organophosphate ester porter (broad specificity)PhnCDE of E. coli
PhnC (C)
PhnD (R)
PhnE (M)
 
3.A.1.9.2Phosphonate/phosphate porter, PhnDCE (Gebhard and Cook, 2007)BacteriaPhnDCE of Mycobacterium smegmatis
PhnC (C) (A0QQ70)
PhnD (R) (A0QQ71)
PhnE (M) (A0QQ68)
 
3.A.1.10 The Ferric Iron Uptake Transporter (FeT) Family
3.A.1.10.1Ferric iron (Fe3+) porterSfuABC of Serratia marcescens
SfuA (R)
SfuB (M)
SfuC (C)
 
3.A.1.10.2Ferric iron (Fe3+) porterFut A1A2BC of SynechocystisPCC6803
FutA1 (R)
FutA2 (R)
FutB (M)
FutC (C)
 
3.A.1.10.3Ferric iron (Fe3+) porter (selective for trivalent cations, Fe3+, Ga3+ and Al3+) (Anderson et al., 2004)FbpABC (HitABC) of Haemophilus influenzae
FbpA (R) (AAC21773)
FbpB (M) (AAC21774)
FbpC (C) (AAC21775)
 
3.A.1.11 The Polyamine/Opine/Phosphonate Uptake Transporter (POPT) Family
3.A.1.11.1Polyamine (putrescine/spermidine) porterPotABCD of E. coli
PotA (C)
PotB (M)
PotC (M)
PotD (R)
 
3.A.1.11.2Putrescine porterPotGHIF of E. coli
PotG (C)
PotH (M)
PotI (M)
PotF (R)
 
3.A.1.11.3Mannopine porterMotABCD of Agrobacterium tumefaciens plasmid pTi15955
MotA (R)
MotB (C)
MotC (M)
MotD (M)
 
3.A.1.11.4Chrysopine porterChtGHIJK of Agrobacterium tumefaciens
ChtG (C)
ChtH (R)
ChtI (R)
ChtJ (M)
ChtK (M)
 
3.A.1.11.52-aminoethyl phosphonate porterPhnSTUV of Salmonella typhimurium
PhnS (R)
PhnT (C)
PhnU (M)
PhnV (M)
 
3.A.1.11.6The γ-aminobutyrate (GABA) uptake system, GtsABCD (White et al., 2009).

Bacteria

GtsABCD of Rhizobium leguminosarum
GtsA (R) (Q1M7Q4)
GtsB (M) (Q1M7Q3)
GtsC (M) (Q1M7Q2)
GtsD (C) (Q1M7Q1)

 
3.A.1.12 The Quaternary Amine Uptake Transporter (QAT) Family (Similar to 3.A.1.16 and 3.A.1.17)
3.A.1.12.1Glycine betaine/proline porter (also transports proline betaine, carnitine, dimethyl proline, homobetaine, γ-butyrobetaine and choline with low affinity)ProVWX of E. coli
ProW (M)
ProX (R)
ProV (C)
 
3.A.1.12.2Glycine betaine porter (also transports dimethylsulfonioacetate and dimethylsulfoniopropionate)OpuAA, AB, AC of Bacillus subtilis
OpuAA (C)
OpuAB (M)
OpuAC (R)
 
3.A.1.12.3Choline porterOpuBA, BB, BC, BD of Bacillus subtilis
OpuBA (C)
OpuBB (M)
OpuBC (R)
OpuBD (M)
 
3.A.1.12.4Uptake system for choline, L-carnitine, D-carnitine, glycine betaine, proline betaine, crotonobetaine, γ-butyrobetaine, dimethylsulfonioacetate, dimethylsulfoniopropionate, ectoine and choline-O-sulfateOpuCA, CB, CC, CD of Bacillus subtilis
OpuCA (C)
OpuCB (M)
OpuCC (R)
OpuCD (M)
 
3.A.1.12.5Uptake system for glycine-betaine (high affinity) and proline (low affinity) (OpuAA-AC or BusAA-AB of Lactococcus lactis). BusAA, the ATPase subunit, has a C-terminal tandem cystathionine β-synthase (CBS) domain which is the cytoplasmic K+ sensor for osmotic stress (osmotic strength) (Biemans-Oldehinkel et al., 2006; Mahmood et al., 2006). BusAA-AB of Lactococcus lactis
BusAA (C-CBS)
BusAB (M-R)
 
3.A.1.12.6Uptake system for hisitidine, proline, proline-betaine and glycine-betaineHutXWV of Sinorhizobium meliloti
HutX (R)
HutW (M)
HutV (C)
 
3.A.1.12.7High affinity (3 μM) choline-specific uptake system (Dupont et al., 2004)ChoXWV of Sinorhizobium meliloti
ChoX (R) (AAM00244)
ChoW (M) (AAM00245)
ChoV (C) (AAM00246)
 
3.A.1.12.8A proline/glycine betaine uptake system. Also reported to be a bile exclusion system that exports oxgall and other bile compounds, BilEA/EB or OpuBA/BB (required for normal virulence) (R.D. Sleator et al., 2005). BacteriaOpuBA/BB or BilEA/EB of Listeria monocytogenes
OpuBA (C) (Q93A35)
OpuBB (M-R) (Q93A34)
 
3.A.1.12.9The salt-induced glycine betaine OtaABC transporter (Schmidt et al., 2007)ArchaeaOtaABC of Methanosarcina mazei Go1
OtaA (C) Q8U4S5
OtaB (M) Q8U4S4
OtaC (R) Q8U4S3
 
3.A.1.12.10The OpuC transporter selective for glycine betaine > choline, acetylcholine, carnitine and proline betaine (contains tandem cystathionine-β-synthase (CBS) domains in the ABC component of OpuC that are required for osmoregulatory function (Chen and Beattie, 2007)). OpuCA, CB, CC of Pseudomonas syringae
OpuCC (R) (Q87WH3)
OpuCB (M) (Q87WH4)
OpuCA (C) (Q87WH5)
 
3.A.1.12.11The glycine betaine uptake porter, GbpABCD (Saum et al., 2009).

Archaea

GbpABCD of Methanosarcina mazei
GbpA (R) (Q8Q040)
GbpB (M) (Q8Q043)
GbpC (M) (Q9Q042)
GbpD (C) (Q8Q041)

 
3.A.1.13 The Vitamin B12 Uptake Transporter (B12T) Family (Similar to 3.A.1.14)
3.A.1.13.1Vitamin B12 porter. The 3-D structure of BtuCDF has been solved to 2.6Ĺ (Hvorup et al., 2007).BtuCDF of E. coli
BtuC (M)
BtuD (C)
BtuF (R)
 
3.A.1.14 The Iron Chelate Uptake Transporter (FeCT) Family (Similar to 3.A.1.13 and 3.A.1.15)
3.A.1.14.1Iron (Fe3+) or ferric-dicitrate porter (Braun and Herrmann, 2007)FecBCDE of E. coli
FecB (R)
FecC (M)
FecD (M)
FecE (C)
 
3.A.1.14.2Iron (Fe3+)-enterobactin porterFepBCDG of E. coli
FepB (R)
FepC (C)
FepD (M)
FepG (M)
 
3.A.1.14.3Iron (Fe3+)-hydroxamate (ferrichrome, coprogen, aerobactin, ferrioxamine B, schizakinen, rhodotorulic acid) porter, albomycin porterFhuBCD of E. coli
FhuB (M-M; 20 TMSs; 10+10)
FhuC (C)
FhuD (R)
 
3.A.1.14.4Iron-chrysobactine porterCbrABCD of Erwinia chrysanthemi
CbrA (R)
CbrB (M)
CbrC (M)
CbrD (C)
 
3.A.1.14.5Heme (hemin) uptake porterHmuTUV of Yersinia pestis
HmuT (R)
HmuU (M)
HmuV (C)
 
3.A.1.14.6The iron-vibriobactin/enterobactin uptake porterViuPDGC of Vibrio cholerae
ViuP (R)
ViuD (M)
ViuG (M)
ViuC (C)
 
3.A.1.14.7Iron (Fe3+)-hydroxamate porter (transports Fe3+-ferrichrome and Fe3+-ferrioxamine B with FhuD1, and these compounds plus aerobactin and coprogen with FhuD2).FhuBCD1D2 of Staphylococcus aureus
FhuB (M)
FhuC (C)
FhuD1 (R)
FhuD2 (R)
 
3.A.1.14.8The iron-vibrioferrin uptake porter (Tanabe et al., 2003) PvuBCDE of Vibrio parahaemolyticus
PvuB (R) (BAC16540)
PvuC (M) (BAC16541)
PvuD (M) (BAC16542)
PvuE (C) (BAC16543)
 
3.A.1.14.9The Corrinoid porter, BtuCDE (Woodson et al., 2005)ArchaeaBtuCDE of Halobacterium sp. strain NRC-1
BtuC (M) (AAG19698)
BtuD (C) (NP_444218)
BtuE (R) (AAG19697)
 
3.A.1.14.10The heme porter, Shp/HtsABC (Shp) is a cell surface heme binding protein that transfers the heme directly to HstA (Nygaard et al., 2006). The crystal structure of the heme binding domain of Shp has been solved (Aranda et al., 2007). HtsABC, along with the FhuC ATPase, is required for the uptake of staphyloferrin A (Beasley et al. 2009).

Bacteria

Shp/HtsABC of Streptococcus pyogenes
Shp (R1) (291 aas; AB179309)
HtsA (R2) (294 aas; AB179210)
HtsB (M) (340 aas; Q99YA3)
HtsC (C) (278 aas; Q99YA4)

 
3.A.1.14.11The putative metal-chelate-type ABC transporter HI1470(C)/HI1471(M) (3D structure known at 2.4 Ĺ resolution; Pinkett et al., 2007)BacteriaHI1470/HI1471 of Haemophilus influenzae
HI1470 (C) (Q57399)
HI1471 (M; 10 or 12 TMSs) (Q57130)
 
3.A.1.14.12Desferrioxamine B uptake porter, DesABC (Barona-Gomez et al., 2006)BacteriaDesABC of Streptomyces coelicolor
DesA (R) (CAB76300)
DesB (M-M; 18 TMSs; 9+9 TMSs) (CAB76299)
DesC (C) (CAB76301)
 
3.A.1.14.13Coelichelin uptake porter, CchCDEF (Barona-Gomez et al., 2006)BacteriaCchCDEF of Streptomyces coelicolor
CchC (M) (CAB53327)
CchD (M) (CAB53326)
CchE (C) (CAB53325)
CchF (R) (CAB53324)
 
3.A.1.14.14The Fe3+ uptake porter; SiuABD (Montańez et al., 2005)BacteriaSiuABD of Streptococcus pyogenes
SiuA (C) Spy0386
SiuD (R) Spy0385
SiuB (M) Spy0384
 
3.A.1.14.15The Fe3+ uptake porter, SiaABC (Montańez et al., 2005)BacteriaSiaABC of Streptococcus pyogenes
SiaA (R) Spy1795
SiaB (M) Spy1794
SiaC (C) Spy1793
 
3.A.1.14.16

Uptake transporter for the catecholic trilactone (2, 3-dihydroxybenzoate-glycine-threonine)3 siderophore bacillibactin (for ferric iron scavenging), FeuABC (Gaballa and Helmann, 2007; Miethke et al., 2006).

Bacteria

FeuABC of Bacillus subtilis
FeuA (R) (P40409)
FeuB (M) (P40410)
FeuC (M) (P40411)

 
3.A.1.14.17The heme-specific uptake porter, HemTUV (Létoffé et al., 2008).BacteriaHemTUV of Serratia proteamaculans
HemT (R) - (A8GDS8)
HemU (M) - (A8GDS7)
HemV (C) - (A8GDS6)
 
3.A.1.14.18Heme acquisition ABC uptake transporter, IsdDEF (Liu et al., 2008)IsdDEF of Staphylococcus aureus
IsdD (?) (358aas, 2TMSs) (Q5HGV2)
IsdE (R) (295aas, 1TMS) (Q7A652)
IsdF (M) (273aas; 8TMSs) (Q7A651)
 
3.A.1.14.19The heme uptake porter, ShuTUV (Burkhard and Wilks, 2008).BacteriaShuTUV of Shigella dysenteriae
ShuT(R) (Q32AX9)
ShuU(M) (Q32AY2)
ShuV(C) (Q32AY3)
 
3.A.1.14.20Heme uptake porter, HugBCD (Villarreal et al., 2008); also called HmuTUV.

Bacteria

HugBCD of Plesiomonas shigelloides
HugB (R) (Q93SS3)
HugC (M) (Q93SS2)
HugD (C) (Q93SS1)

 
3.A.1.15 The Manganese/Zinc/Iron Chelate Uptake Transporter (MZT) Family (Similar to 3.A.1.12, 3.A.1.14 and 3.A.1.16)
3.A.1.15.1Manganese (Mn2+) porterMntABC of Synechocystis 6803
MntA (C)
MntB (M)
MntC (R)
 
3.A.1.15.2Manganese (Mn2+) and zinc (Zn2+) porterScaABC of Streptococcus gordonii
ScaA (R)
ScaB (M)
ScaC (C)
 
3.A.1.15.3Zinc (Zn2+) porterAdcABC of Streptococcus pneumoniae
AdcA (R)
AdcB (M)
AdcC (C)
 
3.A.1.15.4Iron and manganese porterYfeABCD of Yersinia pestis
YfeA (R)
YfeB (C)
YfeC (M)
YfeD (M)
 
3.A.1.15.5Zinc (Zn2+) porter (required for Zn2+ homeostasis and virulence of Salmonella enterica; Ammendola et al., 2007).ZnuABC (YebLMI) of E. coli
ZnuA (R)
ZnuC (C)
ZnuB (M)
 
3.A.1.15.6Iron (Fe2+)/Zinc (Zn2+)/Copper (Cu2+) porterMtsABC of Streptococcus pyogenes
MtsA (R)
MtsB (C)
MtsC (M)
 
3.A.1.15.7Manganese (Mn2+) (Km=0.1 μM) and iron (Fe2+) (5 μM) porter (inhibited by Cd2+ > Co2+ > Ni2+, Cu2+) (most similar to YfeABCD of Yersinia pestis (TC #3.A.1.15.4))SitABCD of Salmonella typhimurium
SitA (R)
SitB (C)
SitC (M)
SitD (M)
 
3.A.1.15.8Manganese (Mn2+), zinc (Zn2+) and possibly iron (Fe2+) porter (Hazlett et al., 2003)TroABCD of Treponema pallidum
TroA (R) P96116
TroB (C) P96117
TroC (M) P96118
TroC (M) P96119
 
3.A.1.15.9Manganese (Mn2+) and Iron (Fe2+) porter, SitABCD (Davies and Walker, 2007)BacteriaSit ABCD of Sinorhizobium meliloti
SitA (R) - (Q92LL5)
SitB (M) - (Q92LL4)
SitC (C) - (Q92LL3)
SitD (M) - (Q92LL2)
 
3.A.1.15.10The Mn2+/Zn2+ transporter MntABC (KB of Mn2+ and Zn2+ is 0.1μM which bind with equal affinity to the same site (Lim et al., 2008)BacteriaMntABC of Neisseria meningitidis:
MntA (C) (A1IQK5)
MntB (M) (A1IQK4)
MntC (R) (Q5FA63)
 
3.A.1.15.11The zinc uptake porter, YcdHI-YceA (Gaballa et al., 2002).

YcdHI-YceA of Bacillus subtilis
AdcA (YcdH) (R) (O34966)
AdcC (YcdI) (C) (O34946)
AdcB (YceA) (M) (O34610)

 
3.A.1.16 The Nitrate/Nitrite/Cyanate Uptake Transporter (NitT) Family (Similar to 3.A.1.12 and 3.A.1.17)
3.A.1.16.1Nitrate/nitrite porterNrtABCD of Synechococcus sp. (PCC 7942)
NrtA (R)
NrtB (M)
NrtC (C)
NrtD (C)
 
3.A.1.16.2Bispecific cyanate/nitrite transporter (functions in both cyanate and nitrite assimilation; Maeda and Omata, 2009).

CynABD of Synechococcus PCC7942
CynA (R)
CynB (M)
CynD (C)

 
3.A.1.16.3Bicarbonate porter (activated by low [CO2] mediated by CmpR; (Nishimura et al., 2008))CmpABCD of Synechococcus sp.
CmpA (R)
CmpB (M)
CmpC (C)
CmpD (C)
 
3.A.1.17 The Taurine Uptake Transporter (TauT) Family (Similar to 3.A.1.12 and 3.A.1.16)
3.A.1.17.1Taurine (2-aminoethane sulfonate) porterTauABC of E. coli
TauA (R)
TauB (C)
TauC (M)
 
3.A.1.17.2Aromatic sulfonate porterSsuABC of Pseudomonas putida
SsuA (R)
SsuB (C)
SsuC (M)
 
3.A.1.17.3The putative hydroxymethylpyrimidine uptake permease, HI0354-7 (Rodionov et al., 2002)BacteriaHI0354-7 of Haemophilus influenzae
HI0354 (C) (P44656)
HI0355 (M) (Q57306)
HI0357 (R) (P44658)
 
3.A.1.17.4The taurine uptake system, TauABC (Krejcík et al., 2008).

TauABC of Neptuniibacter caesariensis
TauA (Q2BM68)
TauB (Q2BM69)
TauC (Q2BM70)

 
3.A.1.17.5The phthalate uptake system, OphFGH (Chang et al. 2009).

Bacteria

OphFGH of Burkholderia capacia
OphF (R) (C0LZR7)
OphG (M) (C0LZR8)
OphH (C) (C0LZR9)

 
3.A.1.18 The Cobalt Uptake Transporter (CoT) Family
3.A.1.18.1Cobalt (Co2+) porter (Rodionov et al., 2006)CbiMNOQ of Salmonella typhimurium
CbiM (M) (Q05594)
CbiN (R) (Q05595)
CbiO (C) (Q05596)
CbiQ (M) (Q05598)
 
3.A.1.19 The Thiamin Uptake Transporter (ThiT) Family (Most similar to 3.A.1.10, 3.A.1.6 and 3.A.1.8 in that order)
3.A.1.19.1Thiamin, thiamin monophosphate and thiamin pyrophosphate porter. The 2.25 Ĺ structure of ThiB (TbpA) has been solved (Soriano et al., 2008). ThiBPQ of Salmonella typhimurium (functionally characterized and partially sequenced) and E. coli (fully sequenced but not functionally characterized)
ThiB; TbpA (R)
ThiP; YabK (M)
ThiQ; YabJ (C)
 
3.A.1.20 The Brachyspira Iron Transporter (BIT) Family (Most similar to 3.A.1.6, 3.A.1.8 and 3.A.1.11)
3.A.1.20.1The iron transporter, BitABCDEFBitABCDEF of Brachyspira (Serpulina) hyodysenteriae
BitA (R)
BitB (R)
BitC (R)
BitD (C)
BitE (M)
BitF (M)
 
3.A.1.21 The Siderophore-Fe3+ Uptake Transporter (SIUT) Family
3.A.1.21.1The Fe3+-Yersiniabactin uptake transporter, YbtPQ (Brem et al., 2001; Fetherston et al., 1999)YbtPQ of Yersinia pestis
YbtP (M-C)
YbtQ (M-C)
 
3.A.1.21.2The Fe3+-carboxymycobactin transporter, IrtAB (Rodriguez and Smith, 2006)IrtAB of Mycobacterium tuberculosis
IrtA (M-C) (P63391)
IrtB (M-C) (P63393)
 
3.A.1.22 The Nickel Uptake Transporter (NiT) Family
3.A.1.22.1Nickel (Ni2+) porter CbiKMQO of Actinobacillus pleuropneumoniae
CbiK (R)
CbiM (M)
CbiQ (M)
CbiO (C)
 
3.A.1.23 The Nickel/Cobalt Uptake Transporter (NiCoT) Family
3.A.1.23.1Nickel (Ni2+) porter (Chen and Burne, 2003)UreMQO of Streptococcus salivarius
UreM (M) (Q79CJ1)
UreQ (M) (Q79CJ0)
UreO (C) (Q79CI9)
UreK (R) (Unknown)
 
3.A.1.23.2Putative cobalt (Co2+) porter (Chen and Burne, 2003)CbiMQOK of Clostridium acetobutylicum
CbiM (M) (AAK79333)
CbiQ (M) (AAK79335)
CbiO (C) (AAK79336)
CbiK (R?) (AAK79334)
 
3.A.1.24 The Methionine Uptake Transporter (MUT) Family (Similar to 3.A.1.3 and 3.A.1.12)
3.A.1.24.1The L- and D-methionine porter (also transports formyl-L-methionine) (Zhang et al., 2003). The 3.7A structure of MetNI has been solved. An allosteric regulatory mechanism operates at the level of transport activity so increased intracellular levels of the transported ligand stabilize an inward-facing, ATPase-inactive state of MetNI to inhibit further ligand translocation into the cell (Kadaba et al., 2008).MetNIQ (abc-yaeE-yaeC) of E. coli
MetN (C) AAC73310
MetI (M) AAC73309
MetQ (R) AAC73308
 
3.A.1.24.2The L- and D-methionine porter (also transports methionine sulfoxide (Hullo et al., 2004)MetNPQ (YusCBA) of Bacillus subtilis
MetN (C) CAB15264
MetP (M) CAB15263
MetQ (R) CAB15262
 
3.A.1.24.3The methionine porter, AtmBDE (Sperandio et al., 2007)bacteriaAtmBDE of Streptococcus mutans
AtmB (R) (Q8K8K9)
AtmD (C) (Q8K8K8)
AtmE (M) (Q8K8K7)
 
3.A.1.24.4L-Methionine uptake porter, MetQNI

Bacteria

MetQNI of Corynebacterium glutamicum
MetQ (R) (Q8NSN1)
MetN (C) (Q8NSN2)
MetI (M) (Q8NSN3)

 
3.A.1.25 The Biotin Uptake Transporter (BioMNY) Family
3.A.1.25.1

The biotin uptake porter (binding receptor lacking) (see also the VUT or ECF family; BioY; 2.A.88.1.1) (Rodionov et al., 2006; Hebbeln et al., 2007). BioN (the EcfT component of the biotin transporter) appears to be required for intramolecular signaling and subunit assembly (Neubauer et al., 2009).

Bacteria

BioMNY of Rhizobium etli
BioM (C) (226 aas; 0 TMSs; AAT52196)
BioN (M) (202 aas; 5 TMSs; AAT52197)
BioY )M) (189 aas; 6 TMSs; AAT52198)

 
3.A.1.26 The Putative Thiamine Uptake Transporter (ThiW) Family
3.A.1.26.1

The putative ABC porter (COG4732), ThiW; 718 aas; 5 TMSs; domain order: M-C-C; plus the putative ATPase binding subunit, CbiQ homologue (binding receptor unknown)

Bacteria

ThiW/CbiQ of Chloroflexus aurantiacus
ThiW (A9WGB0)
CbiQ (A9WGA9)

 
3.A.1.26.2

ThiW homologue/CbiQ homologue (ThiW: 647 aas; M-C-C; 5-6TMSs)

Archaea

ThiW/ChiQ of Methanocorpusculum labreanum
ThiW (A2SPE8)
CbiQ (A2SPE9)

 
3.A.1.26.3

ThiW homologue (711 aas; M-C-C) (No known binding receptor) plus a CbiQ homologue

Bacteria

ThiW/CbiQ homologues of Actinomyces odontolyticus
ThiW (A7BAX2)
CbiQ (A7BAX3)

 
3.A.1.26.4

ThiW/CbiQ homologues (ThiW: 697 aas; M-C-C) (No known binding receptor)

Bacteria

ThiW/CbiQ homologues of Mycobacterium tuberculosis
ThiW (P63399)
CbiQ (P64997)

 
3.A.1.26.5

ThiW/CbiQ/CbiO homologues (ThiW: 174 aas; 5 putative TMSs)

Bacteria

ThiW/CbiQ/CbiO homologues of Roseiflexus castenholzii
ThiW (A7NRF9)
CbiQ (A7NRG1)
CbiO (A7NRG0)

 
3.A.1.26.6

The ThiW/CbiQ/CbiO1/CbiO2 homologues (ThiW: 184 aas; 1-6 TMSs)

Archaea

ThiW/CbiQ/CbiO1/CbiO2 homologues of Aeropyrum pernix
ThiW (Q9Y974)
CbiQ (Q9Y982)
CbiO1 (Q9Y979)
CbiO2 (Q9Y977)

 
3.A.1.27 The γ-Hexachlorocyclohexane (HCH) Family (Similar to 3.A.1.12 and 3.A.1.24)
3.A.1.27.1The γ-hexachlorocyclohexane (γHCH) uptake permease, LinKLMN (most similar to 3.A.1.12.4, the QAT family) (Endo et al., 2007)BacteriaLinKLMN of Sphingobium japonicum
LinK (M) (BAF51698)
LinL (C) (BAF51699)
LinM (R) (BAF51700)
LinN (lipoprotein) (BAF51701)
 
3.A.1.27.2The chloroplast lipid (Trigalactosyl acyl glycerol (TDG)) transporter, Tdg1,2,3 (Lu et al., 2007). Lipids such as mono- and digalactolipids are synthesized in the endoplasmic reticulum (ER) of plant cells and transferred to the thylakoid membranes of chloroplasts. Mutations in an outer chloroplastic envelope protein with 350 aas and 7 putative TMSs in the last 250 residues may catalyze translocation as part of a lipid transfer complex (Xu et al., 2003).Plant ChloroplastTdg 1,2,3 of Arabidopsis thaliana:
Tdg1 (M) (Q8L4R0)
Tdg2 (R) (Q3EB35)
Tdg3 (C) (Q9AT00)
 
3.A.1.28.1The putative queuosine uptake transporter, QrtTUVW (Rodionov et al., 2009) (most similar to 2.A.88.2.1)

Bacteria

QrtTUVW of Salmonella enterica su. typh.
QrtT (M) (Q8XGV9)
QrtU (M) (Q8Z3V9)
QrtV (C) (Q8Z3V8)
QrtW (C) (Q8Z3V7)

 
3.A.1.29.1The putative methionine precursor/uptake transporter, MtsTUV (T is most similar to 3.A.1.23.2; U is most similar to 2.A.36.7.1 and 3.A.1.14.2; V is most similar to 3.A.1.23.2 and 3.A.1.25.1) (Rodionov et al., 2009)

Bacteria

MtsTUV of Lactobacillus johnsoni
MtsT (C) (Q74I63)
MtsU (M) (Q74I62)
MtsV (M) (Q74I61)

 
3.A.1.30.1The putative thiamin precursor uptake transporter, YkoEDC (Rodionov et al., 2009) (E is most similar to 3.A.1.4.3; D is most similar to 3.A.1.26.2; C is most similar to 3.A.1.23.2).

Bacteria

YkoEDC of Bacillus subtilis
YkoE (M) (O34738)
YkoD (C-C) (O34362)
YkoC (M) (O34572)

 
3.A.1.31.1The putative uptake transporter of unknown substrate specificity, HtsTUV (Rodionov et al., 2009) (U is most similar to 3.A.1.25.1; V is most similar to 3.A.1.26.1).

Bacteria

HtsTUV of Bifidobacterium longum
HtsT (M) (Q8G6E7)
HtsU (M) (Q8G6E8)
HtsV (C-C) (Q8G6E9)

 
3.A.1.32.1The putative cobalamin precursor uptake transporter, CbrTUV (Rodionov et al., 2009) (CbrT is most similar to 2.A.1.15.1; CbrU is most similar to 3.A.1.26.1 (MFS; e-4); CbrV is most similar to 2.A.53.11.1 and 3.A.1.2.2 (score of 0.035)) (CbrT has 6 putative TMSs; CbrV has 8-10 putative TMSs).

Bacteria

CbrTUV of Streptomyces coelicolor
CbrT (M) (Q9KXJ5)
CbrU (C-C) (Q9KXJ6)
CbrV (M) (Q9KXJ7)

 
3.A.1.33.1The putative methylthio adenosine uptake transporter (Rodionov et al., 2009).  MtaTUV (MtaT and MtaU are most similar to 3.A.1.26.1 (ThiW); MtaV is most similar to 3.A.1.25.1 (BioN) and 3.A.1.23.2 (CbiQ)).

Bacteria

MtaTUV of Thermoanaerobacter tengcongensis
MtaT (M) (Q8R9M1)
MtaU (C-C) (Q8R9L8)
MtaV (M) (Q8R9L9)

 
3.A.1.101 The Capsular Polysaccharide Exporter (CPSE) Family
3.A.1.101.1Capsular polysaccharide exporterGram-negative bacteriaKpsMT of E. coli KpsM
KpsM (M) - (P24584)
KpsT (C) - (P24586)
 
3.A.1.101.2Vi polysaccharide exporter, VexBC (Hashimoto et al, 1993).Gram-negative bacteriaVexBC of Salmonella typhi
VexB (M) - (P43109)
VexC (C) - (P43110)
 
3.A.1.102 The Lipooligosaccharide Exporter (LOSE) Family
3.A.1.102.1Lipooligosaccharide exporter (nodulation proteins, NodIJ)Gram-negative bacteriaNodIJ of Rhizobium galegae
NodJ (M)
NodI (C)
 
3.A.1.103 The Lipopolysaccharide Exporter (LPSE) Family
3.A.1.103.1Lipopolysaccharide exporterGram-negative bacteriaRfbAB of Klebsiella pneumoniae
RfbA (M)
RfbB (C)
 
3.A.1.103.2Heteropolysaccharide O-antigen exporter (Feng et al., 2004). The C-terminal cytoplasmic domain of Wzt (a IgG-like β-sandwich) determines the specificity of the transporter for either O8 or O9a O-PS (Cuthbertson et al., 2007).

Gram-negative bacteria

Wzm/Wzt of E. coli
Wzm (M) (AAS99164)
Wzt (C) (AAS99165)

 
3.A.1.104 The Teichoic Acid Exporter (TAE) Family
3.A.1.104.1Teichoic acid exporterGram-positive bacteriaTagGH of Bacillus subtilis
TagG (M)
TagH (C)
 
3.A.1.105 The Drug Exporter-1 (DrugE1) Family
3.A.1.105.1Daunorubicin; doxorubicin (drug resistance) exporterGram-positive bacteriaDrrAB of Streptomyces peucetius
DrrA (C)
DrrB (M)
 
3.A.1.105.2Oleandomycin (drug resistance) exporterGram-positive bacteriaOleC4-OleC5 of Streptomyces antibioticus
OleC4 (C)
OleC5 (M)
 
3.A.1.105.3The 4A-4E-O-dideacetyl-chromomycin A3 (biosynthetic precursor of chromomycin) exporter (may also export chromomycin and mithramycin (Menendez et al., 2007).Gram-positive Bacteria CmrAB of Streptomyces greseus
CmrA(C) (Q70J75)
CmrB(M) (Q70J76)
 
3.A.1.105.4The pyoluteorin efflex pump, PltHIJKNγ-proteobacteriaPltHIJKN of Pseudomonas sp. M18:
PltH (336aas; MFP) - (Q4VWD0)
PltI (589aas; C-C) - (Q4VWC9)
PltJ (377aas; M; COG0842; similar to 9.B.74.2 (ABC-2)) - (Q4VWC8)
PltK (372aas; M; The C-terminal hydrophobic half has 5TMSs and is most similar to PltJ, and then to 9.B.74.2, but it is also homologous to 3.A.1.105.2 and 3.A.1.102.1) - (Q4VWC7)
PltN (480aas; OMF) - (Q4VWC6)
 
3.A.1.106 The Lipid Exporter (LipidE) Family
3.A.1.106.1Phospholipid, LPS, lipid A and drug exporter (flippase), MsbA (essential for export to the outer membrane). MsbA also confers drug resistance to azidopine, daunomycin, vinblastine, Hoechst 33342 and ethidium (Reuter et al., 2003). Four x-ray structures, trapped in different conformations, two with and two without nucleotide, have been solved (Ward et al., 2007). They suggest an alternating accessibility mode of transport with major conformational changes.Gram-negative bacteriaMsbA (M-C) of E. coli
 
3.A.1.106.2The homodimeric Sav1866 multidrug exporter (transports doxorubicin, verapamil, ethidium, tetraphenylphosphonium, vinblastine and the fluorescent dye, Hoechst 33342; 3-D structure known at 3 Å resolution; Dawson and Locher, 2006; Velamakanni et al., 2008)

Gram-positive Bacteria

Sav1866 of Staphylococcus aureus (M-C) 2HYDA/2HYDB (578 aas)

 
3.A.1.106.3The dimeric multidrug resistance exporter, ABC1/2 (exports the peptide antimicrobrials, nisin and polymyxin; (Margolles et al., 2006) (both ABC1 and ABC2 also show striking similarity to family 3.A.1.117).Gram-positive Bacteria ABC1/2 of Brevibacterium longum:
ABC-1 (M-C) (ZP_00121338)
ABC-2 (M-C) (ZP_00121339)
 
3.A.1.106.4The duplicated ABC transporter, CgR_1214 (1247 aas; MC(poorly conserved) MC(well conserved))BacteriaCgR_1214 of Corynebacterium glutamicum (MCMC) (A4QD95)
 
3.A.1.106.5The heterodimeric multidrug efflux pump, SmdAB (exports norfloxacin, tetracycline, 4',6-diamidino-2-phenylindole (DAPI), and Hoechst 33342) (Matsuo et al., 2008).BacteriaSmdAB of Serratia marcescens:
SmdA (M-C) (A7VN01)
SmdB (M-C) (A7VN02)
 
3.A.1.106.6Multidrug efflux pump, Rv0194 (exports & causes resistance to ampicillin, streptomycin and chloramphenicol by 32- to 64-fold and to vancomycin and tetracycline by 4- to 8-fold (Danilchanka et al., 2008)).BacteriaRv0194 of Mycobacterium tuberculosis (MCMC) (O53645)
 
3.A.1.106.7The Salmochelin/Enterobactin secretory exporter, IroC (Crouch et al., 2008).BacteriaIroC of Salmonella enterica (MCMC) (Q8RMB7)
 
3.A.1.106.8The heterodimeric YheHI MDR transporter (Torres et al., 2009) (activates KinA during sporulation initiation)

Bacteria

YheHI of Bacillus subtilis

YheH (M-C) (O07549)

YheI (M-C) (O07550)

 
3.A.1.107 The Putative Heme Exporter (HemeE) Family
3.A.1.107.1Putative heme exporter, CcmABC=CycVWZ (Note: CcmC may function independently of CcmAB) (Feissner et al., 2006; Christensen et al., 2007)Gram-negative bacteriaCycVWZ of Bradyrhizobium japonicum
CycV (C)
CycW (M)
CycZ (M)
 
3.A.1.107.2The mitochondrial ABC transporter involved in cytochrome c maturation, CcmA/CcmB. (Note: CcmA is nuclearly encoded while CcmB is mitochondrially encoded) (Rayapuram et al., 2007) Plant MitochondriaCcmA/CcmB of Arabidopsis thaliana
CcmA(C) (Q9C8T1)
CcmB(M) (P93280)
 
3.A.1.107.3CcmABCD exporter; CcmD (69aas, 1TMS) is required for the release of CcmE (which binds heme in the periplasm) from CcmABC. CcmC (9.B.14.2.3) is required for the transfer of heme to CcmE in the periplasm (Richard-Fogal et al., 2008)CcmABCD of E. coli
CcmA (C) (Q8XE58)
CcmB (M; 7 TMSs) (P0ABM0)
CcmC (M; 6 TMSs) (P0ABM1)
CcmD (M; 1 TMS) (P0ABM7)
 
3.A.1.108 The β-Glucan Exporter (GlucanE) Family
3.A.1.108.1β-Glucan exporterGram-negative bacteriaNdvA (M-C) of Rhizobium meliloti
 
3.A.1.109 The Protein-1 Exporter (Prot1E) Family
3.A.1.109.1α-Hemolysin exporterGram-negative bacteriaHlyB (M-C) of E. coli
 
3.A.1.109.2Cyclolysin exporter, CyaB (Glaser et al., 1988) (Possesses an N-terminal lysosomal sorting signal within the amino-terminal transmembrane domain; Kamakura et al., 2008).

Gram-negative bacteria

CyaB (M-C) of Bordetella pertussis

 
3.A.1.109.3LapA adhesin protein exporter, LapB (Hinsa et al., 2003)BacteriaLapB of Pseudomonas putida
LapB (MC) (AAN65800)
 
3.A.1.109.4The biofilm inducible ABC-type drug resistance pumps, PA1875-PA1877 (Zhang and Mah, 2008). PA1875-PA1877 of Pseudomonas aeruginosa
PA1875 (OMF; 425 aas) (Q9I2M2)
PA1876 (ABC; M-C; 723 aas) (Q9I2M1)
PA1877 (MFP; 395 aas) (Q9I2M0)
 
3.A.1.110 The Protein-2 Exporter (Prot2E) Family
3.A.1.110.1Microcin E492 exporter, MceFGH (MceF has 5 or 6 TMSs; MceG has 6 TMSs; MceH has 1 N-terminal TMS) (Bieler et al., 2006; Lagos et al., 1999)MceFGH of Klebsiella pneumoniae
MceF (M) (Q93GK6)
MceG (C-M-C) (Q93GK5)
MceH (MFP) (Q93GK4)
 
3.A.1.110.2Colicin V exporterEnteric bacteriaCvaB (M-C) of E. coli
 
3.A.1.110.3The multiple protein exporter, PrsD/PrsE (exports EPS glycanases, PlyA and PlyB, as well as Rhizobium adhering proteins) (Russo et al., 2006). 12 substrates have been identified; PrsDE provide the major route of protein export in R. leguminosarum (Krehenbrink and Downie, 2008).Gram-negative bacteriaPrsD/PrsE of Rhizobium leguminosarum
PrsD(M-C) (O05693)
PrsE(MFP) (O05694)
 
3.A.1.110.4Alkaline protease exporterGram-negative bacteriaAprD (M-C) of Pseudomonas aeruginosa
 
3.A.1.110.5S-layer protein exporterGram-negative bacteriaRsaD (M-C) of Caulobacter crescentus
 
3.A.1.110.6Exporter for lipase, LipA, protease, PrtA and S-layer protein SlaAGram-negative bacteriaLipB (M-C) of Serratia marcescens
 
3.A.1.110.7Exporter for heme-binding protein and metaloproteaseGram-negative bacteriaHasD (M-C) of Serratia marcescens
 
3.A.1.110.8Surface layer protein exporterGram-negative bacteriaSapD (M-C) of Campylobacter fetus
 
3.A.1.110.9Exporter of HasA lipase, and alkaline proteaseGram-negative bacteriaHasD (M-C) of Pseudomonas fluorescens
 
3.A.1.110.10The AlgE-type Mannuronan C-5-Epimerase exporter, EexD (PrtD) (Gimmestad et al., 2006).BacteriaEexD of Azotobacter vinelandii (Q4IU88)
 
3.A.1.111 The Peptide-1 Exporter (Pep1E) Family
3.A.1.111.1Hemolysin/bacteriocin (cytolysin) exporter with associated proteolytic activityGram-positive bacteriaCylT (M-C) (CylB) of Enterococcus faecalis
 
3.A.1.111.2Subtilin (toxic peptide) exporterGram-positive bacteriaSpaB (M-C) of Bacillus subtilis
 
3.A.1.111.3Nisin exporterGram-positive bacteriaNisT (M-C) of Lactococcus lactis
 
3.A.1.111.4Bacteriocin immunity protein, SmbG (198 aas; 6TMSs in a 2+2+2 arrangement. (Exports bacteriocins and causes resistance to antibiotics such as tetracycline, penicillin and triclosan). Upregulated by exposure to antibiotics (Matsumoto-Nakano and Kuramitsu, 2006)Gram-positive bacteriaSmbG (M-C) of Streptococcus mutans (Q5TLL2)
 
3.A.1.111.5The lacticin Q exporter, LcnDR3 (Yoneyama et al., 2009).

Gram-positive bacteria

LcnDR3 (M-C) of Lactococcus lactis (P37608)

 
3.A.1.112 The Peptide-2 Exporter (Pep2E) Family
3.A.1.112.1Competence factor (CSF; a heptadecapeptide) exporterGram-positive bacteriaComA (M-C) of Streptococcus pneumoniae (functions with putative MFP accessory protein, ComB)
 
3.A.1.112.2Pediocin PA-1 exporterGram-positive bacteriaPedD (M-C) of Pediococcus acidilactici
 
3.A.1.112.3Bacteriocin (lactococcin) exporterGram-positive bacteriaLcnC (M-C) of Lactococcus lactis (functions with putative MFP accessory protein LcnD)
 
3.A.1.112.4Sublancin exporter, SunTGram-positive bacteriaSunT (M-C) of Bacillus subtilis
 
3.A.1.113 The Peptide-3 Exporter (Pep3E) Family
3.A.1.113.1Modified cyclic peptide (syringomycin) exporter, SyrD Gram-negative bacteriaSyrD (M-C) of Pseudomonas syringae
 
3.A.1.113.2Pyoverdin (siderophore) exporterGram-negative bacteriaPvdE (M-C) of Pseudomonas aeruginosa
 
3.A.1.113.3The microcin J25 (21 aa cyclic peptide antibiotic) exporter, YojI (Delgado et al., 2005) (TolC is also required for export; Vincent and Morero, 2009).

Gram-negative bacteria

YojI of E. coli (P33941)

 
3.A.1.114 The Probable Glycolipid Exporter (DevE) Family
3.A.1.114.1Probable glycolipid exporter (under nitrogen control in heterocysts), DevABC-HgdD (Moslavac et al., 2007)CyanobacteriaDevABC-HgdD of Anabaena variabilis (sp. strain PCC7120)
DevA (C)
DevB (MFP)
DevC (M)
HgdD (TolC like)
 
3.A.1.115 The Na+ Exporter (NatE) Family
3.A.1.115.1Na+ efflux pump NatABGram-positive bacteriaNatAB of Bacillus subtilis
NatA (M)
NatB (C)
 
3.A.1.116 The Microcin B17 Exporter (McbE) Family
3.A.1.116.1Microcin B17 exporterEnteric bacteriaMcbEF of E. coli
McbE (M)
McbF (C)
 
3.A.1.117 The Drug Exporter-2 (DrugE2) Family
3.A.1.117.1The multidrug exporter, LmrA (can also substitute for MsbA [TC #3.A.1.106.1] to export lipid A; Reuter et al., 2003). Gram-positive bacteriaLmrA (M-C) of Lactococcus lactis
 
3.A.1.117.2Hop resistance protein, HorAGram-positive bacteriaHorA (M-C) of Lactobacillus brevis
 
3.A.1.118 The Microcin J25 Exporter (McjD) Family
3.A.1.118.1The cyclic peptide antibiotic, microcin J25 exporter, McjD (TolC is also required for export; Vincent and Morero, 2009).

Gram-negative bacteria

McjD (M-C) of E. coli

 
3.A.1.119 The Drug/Siderophore Exporter-3 (DrugE3) Family
3.A.1.119.15-Hydroxystreptomycin and other streptomycin-like aminoglycoside exporter, StrVWGram-positive bacteriaStrVW of Streptomyces glaucescens
StrV (M-C)
StrW (M-C)
 
3.A.1.119.2Tetracycline/oxytetracycline/oxacillin exporter, TetABGram-positive bacteriaTetAB (StrAB) of Corynebacterium striatum
TetA (M-C)
TetB (M-C)
 
3.A.1.119.3Exochelin exporter, ExiTGram-positive bacteriaExiT of Mycobacterium smegmatis
(MC-M-C)
 
3.A.1.120 The (Putative) Drug Resistance ATPase-1 (Drug RA1) Family
3.A.1.120.1Macrolide ATPase (membrane constituent unknown) Gram-positive bacteriaSrmB (C-C) of Streptomyces ambofaciens
 
3.A.1.120.2Tylosin ATPase (membrane constituent unknown) Gram-positive bacteriaTlrC (C-C) of Streptomyces fradiae
 
3.A.1.120.3Oleandomycin resistance ATPase (membrane constituent unknown)Gram-positive bacteriaOleB (C-C) of Streptomyces antibioticus
 
3.A.1.120.4Carbomycin resistance ATPase (membrane constituent unknown)Gram-positive bacteriaCarbomycin, CarA (C-C), protein of Streptomyces thermotolerans
 
3.A.1.120.5The acetate resistance ABC acetate exporter (Nankano et al., 2006)Gram-negative bacteriaAatA (C-C) of Acetobacter aceti (BAE71146)
 
3.A.1.120.6

The Uup protein (required for bacterial competitiveness (Murat et al., 2008); 39% identical to 3.A.1.120.5).

Gram-negative bacteria

Uup of E. coli (P43672)

 
3.A.1.121 The (Putative) Drug Resistance ATPase-2 (Drug RA2) Family
3.A.1.121.1Erythromycin ATPase (membrane constituent unknown) Gram-positive bacteriaMsrA (C-C) of Staphylococcus epidermidis
 
3.A.1.121.2Pristinamycin resistance protein, VgaGGram-positive bacteriaVgaB (C-C) of Staphylococcus aureus
 
3.A.1.121.3Antibiotic (virginiamycin and lincomycin) resistance protein, VmlRGram-positive bacteriaVmlR (C-C) of Bacillus subtilis (P39115)
 
3.A.1.121.4The two component ABC-4-type transporter (Rafii and Park, 2008)Bacteria and archaeaThe ABC-4 M/C-C transporter of Clostridium hathewayi (Q83XH0)
(Q83XH1)
 
3.A.1.122 The Macrolide Exporter (MacB) Family
3.A.1.122.1Macrolide (14- and 15- but not 16-membered lactone macrolides including erythromycin) exporter, MacAB (both MacA and MacB are required for activity) (Tikhonova et al., 2007). MacAB also functions (probably with TolC) to export heat-stable enterotoxin II (Yamanaka et al., 2008). The crystal structure of MacA is available (Yum et al., 2009). MacB is a dimer whose ATPase activity and macrolide-binding capacity are regulated by the membrane fusion protein MacA (Lin et al., 2009). Xu et al. (2009) have reported the crystal structure of the periplasmic region of MacB.

Gram-negative bacteria

MacAB of E. coli:
MacA(MFP) (P75830)
MacB(C-M) (P75831)

 
3.A.1.122.2The SpdC antimicrobial peptide resistance efflux pump, YknXYZ (Butcher and Helmann, 2006)BacteriaYknXYZ of Bacillus subtilis:
YknX (MFP) (O31710)
YknY (C) (O31711)
YknZ (M) (O31712)
 
3.A.1.122.3The enterocin AS-48 exporter, As-48FGHGram-positive bacteriaAs-48FGH on plasmid pMBL of Enterococcus faecalis:
As-48F (MFP) (Q7AUQ4)
As-48H (M) (Q8RKC0)
As-48G (C) (Q8RKC1)
 
3.A.1.122.4Probable Heme exporter, HrtAB (Stauff et al., 2008)BacteriaHrtAB of Staphylococcus aureus:
HrtA (C) (Q7A3X3)
HrtB (M) (Q7A7X2)
 
3.A.1.122.5ABC transporter of unknown function (DUF214 protein) (4TMSs)/ABC protein [Msed1528/Msed1530] ArchaeaMsed1528/Msed1530 of Metallosphaera sedula (M) (A4YGY2)
 
3.A.1.122.6ABC transporter of unknown function (DUF214 protein) (4TMSs)/ABC protein [MA2839/MA2840]ArchaeaMA2839/MA2840 of Methanosarcina acetivorans
MA2839 (M) (Q8TM31)
MA2840 (C) (Q8TM30)
 
3.A.1.122.7ABC transporter of unknown function (Duf214 protein (409aas; 4TMSs:1+3)/ABC protein)ArchaeaDuf214 protein/ ABC protein of Methanococcus voltae:
Duf214 protein (M) (A8TDX0)
ABC protein (C) (A8TDW7)
 
3.A.1.122.8Putative ABC3 permease, PC1,2,3.BacteriaPC1,2,3 of Treponema denticola:
PC1 (C) - Q73MJ2
PC2 (M) - Q73MJ3
PC3 (M) - Q73MJ4
 
3.A.1.122.9Duf214 protein (405aas)/ ABC proteinArchaeaDuf214/ABC system of Caldivirga maquilingensis:
Duf214 protein (M) (A8M8Z1)
 
3.A.1.122.10Duf214 (423aas)/ ABC systemArchaeaDuf214/ABC system of Sulfolobus tokodaii:
Duf214 protein (M) (Q973J4)
 
3.A.1.123 The Peptide-4 Exporter (Pep4E) Family
3.A.1.123.1Pep5 lantibiotic exporter, PepTGram-positive bacteriaPepT (M-C) of Staphylococcus epidermidis
 
3.A.1.123.2Aureocin A70 multipeptide bacteriocin (AurA, AurB, AurC, AurD) exporter, AurTGram-positive bacteriaAurT (M-C) of Staphylococcus aureus
 
3.A.1.123.3The one component lantibiotic exporter, GdmT (Sibbald et al., 2006) Gram-positive bacteriumGdmT (M-C) of Staphylococcus gallinarum (A3QNP2)
 
3.A.1.124 The 3-component Peptide-5 Exporter (Pep5E) Family
3.A.1.124.1The 3-component nisin immunity exporter, NisFEGGram-positive bacteriaNisFEG of Lactococcus lactis
NisF (C)
NisE (M)
NisG (M)
 
3.A.1.124.2The 3-component subtilin immunity exporter, SpaEFGGram-positive bacteriaSpaEFG of Bacillus subtilis
SpaE (M)
SpaF (C)
SpaG (M)
 
3.A.1.124.3The lantibiotic Nukacin ISK-1 (TC# 1.C.21.1.5)/NukH (BAD01013; 92aas) exporter, NukEFG (Okuda et al., 2008)Gram-positive bacteriaNukEFG of Staphylococcus warneri
NukE (M) (Q75V14)
NukF (C) (Q75V15)
NukG (M) (Q75V13)
 
3.A.1.124.4The macedocin exporter, McdEFG (Papadelli et al., 2007) Gram-positive bacteriaMcdEFG of Streptococcus macedonicus
McdE (M; 254 aas) (A6MER6)
McdG (M; 245 aas) (A6MER7)
McdF (C; 304 aas) (A6MER5)
 
3.A.1.124.5The salivaricin exporter, SboEFG (Hyink et al., 2007)Gram-positive bacteriaSboEFG of Streptococcus salivarius
SboE (M; 249 aas) (Q09IH9)
SboF (C; 303 aas) (Q09II0)
SboG (M; 242 aas) (Q09IH8)
 
3.A.1.125 The Lipoprotein Translocase (LPT) Family
3.A.1.125.1Lipoprotein translocation system (translocates lipoproteins from the inner membrane to periplasmic chaperone, LolA, which transfers the lipoproteins to an outer membrane receptor, LolB, which anchors the lipoprotein to the outer membrane of the Gram-negative bacterial cell envelope) (see 1.B.46; Narita et al., 2003; Ito et al., 2006; Watanabe et al., 2007). The structure of ligand-bound LolCDE has been solved (Ito et al., 2006). LolC and LolE each have 4 TMSs (1+3). Unlike most ATP binding cassette transporters mediating the transmembrane flux of substrates, the LolCDE complex catalyzes the extrusion of lipoproteins anchored to the outer leaflet of the inner membrane. The LolCDE complex is unusual in that it can be purified as a liganded form, which is an intermediate of the lipoprotein release reaction (Taniguchi and Tokuda, 2008). LolCDE has been reconstituted from separated subunits (Kanamaru et al., 2007).Gram-negative bacteriaLolCDE of E. coli
LolC (M)
LolD (C)
LolE (M)
 
3.A.1.125.2Putative lipoprotein LolCDE homologue LolCE (10TMSs:1+6+3)/LolDBacteriaLolCE/LolD of Mycobacterium tuberculosis
LolCE (M) (Q7D911)
LolD (C) (O53899)
 
3.A.1.125.3Duf214 protein (843aas; 10TMSs:1+6+3)BacteriaDuf214 protein/ ABC protein of Frankia sp. CcI3:
Duf214 protein (M) - Q2J9P4
[LolD/FtsE/SalX]-type ABC protein (C) - Q2J9P5
 
3.A.1.126 The β-Exotoxin I Exporter (βETE) Family
3.A.1.126.1Exporter of β-exotoxin I, BerABBacteriaβ-exotoxin exporter, BerAB, of Bacillus thuringiensis
BerA (C)
BerB (M)
 
3.A.1.127 The AmfS Peptide Exporter (AmfS-E) Family
3.A.1.127.1Exporter of AmfS extracellular peptidic morphogen (Chater and Horinouchi, 2003; Ueda et al., 2002)BacteriaAmfS exporter, AmfAB of Streptomyces griseus
AmfA (MC) (BAA33537)
AmfB (MC) (BBA33538)
 
3.A.1.128 The SkfA Peptide Exporter (SkfA-E) Family
3.A.1.128.1Exporter of SkfA processed peptide (spO31422), SkfEF (González-Pastor et al., 2003)

Bacteria

SkfEF (YbdAB) of Bacillus subtilis
SkfE (C) O31427
SkfF (M-M) O31438

 
3.A.1.128.2Putative ABC exporter, Teth 514-0346 & 0347

Bacteria

Teth 514-0346 & 0347 of Thermoanaerobacter sp. x514:
Teth514-0346 (C) (B0K2P2)
Teth514-0347 (M-M) (B0K2P3)

 
3.A.1.128.3Putative ABC exporter, CLK2533/CLK2534

Bacteria

CLK2533/CLK2534 of Clostridium botulinum
CLK2533 (M-M) (B1L0U0)
CLK2534 (C) (B1L0U1)

 
3.A.1.128.4Putative ABC exporter Tiet1371/1372

Bacteria

Tiet1371/72 of Thermotoga lettingae
Tiet1371 (M-M) (A8F6Z4)
Tiet1372 (C) (A8F6Z5)

 
3.A.1.129 The CydDC Cysteine Exporter (CydDC-E) Family
3.A.1.129.1Cysteine exporter, CydDC (periplasmic cysteine is required for cytochrome bd assembly) (Cruz-Ramos et al., 2004)BacteriaCydDC of E. coli
CydD (M-C) (P29018)
CydC (M-C) (P23886)
 
3.A.1.130 The Multidrug/Hemolysin Exporter (MHE) Family
3.A.1.130.1The multidrug/hemolysin exporter, CylA/B (note: CylK (AAF01071) may influence its activity)(Gottschalk et al., 2006)BacteriaCylA/B of Streptococcus agalactiae
CylA (C) (Q9X432)
CylB (M) (Q9X433)
 
3.A.1.131 The Bacitracin Resistance (Bcr) Family
3.A.1.131.1The 3 component bacitracin-resistance efflex pump, BcrABC (Podlesek et al., 1995) (BcrA is most similar to SpaF (3.A.1.124.2), but BcrB (6TMSs) and BcrC are not sufficiently similar to detect similarity in BLAST searches). BcrC (5TMSs) belongs to the PAP2 phosphatase superfamily).BacteriaBcrABC of Bacillus licheniformis
BcrA (C) - (P42332)
BcrB (M) - (P42333)
BcrC (M) - (P42334)
 
3.A.1.132 The Gliding Motility ABC Transporter (Gld) Family
3.A.1.132.1The GldAFG putative ABC transporter required for ratchet-type gliding motility; may function in secretion of a macromolecule such as an exopolysaccharide. (Agarwal et al., 1997; Hunnicutt et al., 2002). Soluble GldG homologues (no TMSs) are found in eukaryotes (e.g. intraflagellar protein transporter, IPT52 of Chlamydomonas reinhardtii; XP_001692161)BacteriaGldAFG of Flavobacterium johnsoniae:
GldA (C; 298 aas) - (O30489)
GldF (M; 241 aas; 6TMSs (2+2+2) - (Q93LN1)
GldG (M-periplasm; putative auxillary subunit with 2TMSs at the N and C-termini; 561 aas)- (Q93LN0).
 
3.A.1.132.2The NosDFY Copper ABC transporter (Chan et al., 1997)BacteriaNosDFY of Sinorhizobium meliloti
NosD (R; periplasmic copper binding receptor)(Q52899)
NosF (C; like GldA) (Q52900)
NosY (M; like GldF) (O07330)
 
3.A.1.132.3The uncharacterized ABC transporter with GldF-GldG homologues fusedBacteriaGldAFG homologues of Magnetococcus sp. MC-1
GldFG (M-Aux; 964 aas) (A0L4K8)
GldA (C; 399 aas) (A0L4L0)
 
3.A.1.132.4The uncharacterized ABC transporter with GldF-GldG homologues fusedBacteriaGldAFG homologues of Hahella chejuensis
GldF-G (M-Aux; 978 aas) (Q2SDB0)
GldA (C; 315 aas) (Q2SDB1)
 
3.A.1.133 The Peptide-6 Exporter (Pep6E) Family
3.A.1.133.1The modified YydF* peptide exporter, YydIJ (Butcher et al., 2007)BacteriaYydIJ of Bacillus subtilis:
YydI (C) (Q45593)
YydJ (M) (Q45592)
 
3.A.1.133.2A 6TMS homologue of YydJ (ORF1) of 280aasBacteriaORF1 of Flavobacteria bacterium BBFL7 (Q26C21)
 
3.A.1.134 The Peptide-7 Exporter (Pep7E) Family
3.A.1.134.1The lantibiotic, salivericin A exporter, SalXYGram-positive bacteriaSalXY of Streptococcus salivarius
SalX (C)
SalY (M)
 
3.A.1.134.2The bacitracin-resistance (putative bacitracin exporter), MbrAB. Participate with BreSR to control its own gene expression (Bernard et al., 2007).Gram-positive bacteriaMbrAB of Streptococcus mutans
MbrA (C)
MbrB (M)
 
3.A.1.134.3The bacitracin exporter, BceAB (Ohki et al., 2003)Gram-positive bacteriaBceAB (YtsCD) of Bacillus subtilis BceA (C) CAB15016
BceB (M) CAB15015
 
3.A.1.134.4The bacitracin/vancoresmycin (a tetramic acid antibiotic) resistance exporter (Becker et al. 2009) (most like 3.A.1.134.2)

SPR0812/SPR0813 of Streptococcus pnenmoiae

SPR0812(C)(Q8DQ75)

SPR0813 (M)(Q8DQ76)

 
3.A.1.135 The Drug Exporter-4 (DrugE4) Family
3.A.1.135.1The heterodimeric multidrug exporter, YdaG/YbdA [YdaG most closely resembles LmrA (27% I), but YdbA most closely resembles MsbA (3.A.1.106.1) (29% I).] (Both proteins are ABC half transporters; only the heterodimer is active; ethidium, daunomycin and BCECF-AM are substrates; Lubelski et al., 2004) These proteins have been renamed LmrC and LmrD (Lubelski et al., 2006)Gram-positive bacteriaYdaG/YdbA of Lactococcus lactis YdaG (M-C) (AAK04408)
YdbA (M-C) (AAK04409)
 
3.A.1.135.2The heterodimeric putative multidrug exporter, RscA/RscB; probably orthologous to YdaG/YbdA (TC #3.A.1.117.4) [Transcription is activated by stress conditions (heat, acid) and repressed by a 2-component system, CovRS (Dalton et al., 2006)]Gram-positive bacteriaRscAB of Streptococcus pyogenes RscA (M-C) (568 aas) (Q9A1K5)
RscB (M-C) (594 aas) (Q9A1K4)
 
3.A.1.136 The Uncharacterized ABC-3-type (U-ABC3-1) Family
3.A.1.136.1Putative ABC3 permease complex U-ABC3-1a (403aas; 4TMSs:1+3)BacteriaU-ABC3-1a of Treponema denticola (M) (Q73MJ0)
 
3.A.1.136.2Putative ABC3-type antimicrobial peptide transporter, fused ATPase-porter protein, U-ABC3-1b (667aas; 4TMSs:1+3)BacteriaU-ABC3-1b of Lactobacillus brevis (CM) (Q03RZ6)
 
3.A.1.137 The Uncharacterized ABC-3-type (U-ABC3-2) Family
3.A.1.137.1Putative ABC-3-type permease complex, ABC3-2aArchaeaABC3-2a of Pyrobaculum calidifontis:
ABC3-2a (M) (A3MWP2)
ABC3-2a (C) (A3MWP1)
 
3.A.1.138 The Unknown ABC-2-type (ABC2-1) Family
3.A.1.138.1Unknown ABC-2 transporter complex-1, U-ABC2-TC-1ArchaeaU-ABC2-TC-1 of Picrophilus torridus:
U-ABC2-TC-1a (M) (Q6KYW9)
U-ABC2-TC-1a (C) (Q6KYW8)
 
3.A.1.139 The UDP-Glucose Exporter (U-GlcE) Family (UPF0014 Family)
3.A.1.139.1

UDP-glucose exporter, STAR1/STAR2 (sensitive to aluminum rhizotoxicity) (Probable Type I topology)

Plants

STAR1/STAR2 of Oryza sativa
STAR1 (C) (Q5Z8H2)
STAR2 (M) (Q5W7C1)

 
3.A.1.139.2The YbbM protein (SwissProt family UDF0014; 7 putative TMSs)

Bacteria

YbbM of E. coli (P77307)

 
3.A.1.140 The FtsX/FtsE Septation (FtsX/FtsE) Family
3.A.1.140.1

The putative FtsX/FtsE ABC transporter (Arends et al., 2009) (FtsX is of the type III topology).

Bacteria

FtsX/FtsE of E. coli
FtsX (P0AC31)
FtsE (P0A9R7)

 
3.A.1.141 The Ethyl Viologen Exporter (EVE) Family (DUF990 Family)
3.A.1.141.1

The ethyl (methyl; benzyl) viologen export pump, EvrABC (EvrB and EvrC of 6 TMSs are members of the large DUF990 superfamily (Prosecka et al., 2009); They appear to be of the ABC-2 topological type).

Bacteria

EvrABC of Synechocystis sp. PCC6803
P73329 slr1910, ABC protein (EvrA)
P74256 slr1174, membrane protein (EvrB)
P74757 slr0610, membrane protein (EvrC)

 
3.A.1.141.2

ABC transporter of unknown specificity, AbcABC

Bacteria

AbcABC of Thermoanaerobacter tengcongensis
AbcA (M) (Q8R6Q6)
AbcB (M) (Q8R6Q5)
AbcC (C) (Q8R6Q4)

 
3.A.1.201 The Multidrug Resistance Exporter (MDR) Family (ABCB)
3.A.1.201.1Broad specificity multidrug resistance (MDR) efflux pump (exports organic cations and amphiphilic compounds of unrelated chemical structure) (These include: anti-biotics, viral agents, cancer agents, hypertensives, depressants, histamines, emetics, and the protease inhibitor, lopinavir. Pgp also exports immunosuppressants, detergents, long-chain fatty acids, HIV protease inhibitors, synthetic tetramethylrosamine analogues, calcein M, etc.); peptide efflux pump; phospholipid (e.g., phosphatidyl serine), cholesterol and sterol flippase (also called ABCB1 and p-gp))Animals, fungi, bacteriaMDR1 of Homo sapiens
 
3.A.1.201.2Bile salt export pump, BSEP or SPGP (associated with progressive familial intrahepatic cholestasis-2 (also called ABCB11) and benign recurrent intrahepatic cholestasis (Kagawa et al., 2007)). Unconjugaged bile salts and glycine conjugates > taurine conjugates. AnimalsBSEP of Homo sapiens
 
3.A.1.201.3Short chain fatty acid phosphatidylcholine translocase (phospholipid flippase), MDR3 (associated with progressive familial intrahepatic cholestasis-3). (Narrow drug specificity relative to MDR1. Exports digoxin, paclitaxel, vinblastin and bile acids.) (also called ABCB4)AnimalsMDR3 of Homo sapiens
 
3.A.1.201.4The multidrug resistance/chloroquine resistance protein, Pfmdr1 ProtozoaPfmdr1 of Plasmodium falciparum (P13568)
 
3.A.1.201.5Auxin efflux pump Pgp1 (MDR1) (regulated by Twd1, an FK506-binding protein immunophilin prolyl/peptidyl isomerase; 8.A.11.1.1 (Bouchard et al., 2006))PlantsPgp1 of Arabidopsis thaliana (Q9ZR72)
 
3.A.1.201.6Auxin efflux pump Pgp19 (MDR11) (regulated by Twd1, an FK506-binding protein immunophilin prolyl/peptidyl isomerase; 8.A.11.1.1 (Bouchard et al., 2006))PlantsPgp19 of Arabidopsis thaliana (Q9LJX2)
 
3.A.1.201.7Auxin efflux pump Pgp4; functions in the basipetal redirection of auxin from the root tip. Strongly expressed in root cap and epidermal cells (Terasaka et al., 2005)PlantsPgp4 of Arabidopsis thaliana (MCMC) O80725
 
3.A.1.201.8The aluminum chelate (aluminum sensitivity (ALS1)) protein; expressed in root vacuoles half-type ABC transporter (not induced by aluminum; Larsen et al., 2007).PlantsALS1 (M-C) of Arabidopsis thaliana (Q0WML0)
 
3.A.1.201.9Marine skate liver bile salt exporter, BSEP (1348 aas) (transports taurocholine in an ATP-dependent fashion (Cai et al., 2001)) (Most similar to 3.A.1.201.2)AnimalsBSEP of Raja erinacea (MC MC) (Q90Z35)
 
3.A.1.201.10Mussel ABCB/p-glycoprotein-like transporter (1311aas). Transports verapamil, pentachlorphenol, vinblastine, trifluoperazine, emetine, quinidine, forskolin, cyclosporin, and PSC833 compounds that block efflux of fluorescent dye substrates from the gills (T. Luckenbach & D. Epel, 2008).EukaryotesABCB-like transporter of Mytilus californianus (ABS83556)
 
3.A.1.202 The Cystic Fibrosis Transmembrane Conductance Exporter (CFTR) Family (ABCC)
3.A.1.202.1Cystic fibrosis transmembrane conductance regulator (CFTR)(also called ABCC7); cyclic AMP-dependent chloride channel; also catalyzes nucleotide (ATP-ADP)-dependent glutathione flux (Kogan et al., 2003) (may also activate inward rectifying K+ channels). The underlying mechanism by which ATP hydrolysis controls channel opening is described by Gadsby et al., (2006). The most common cause of cystic fibrosis (CF) is defective folding of a cystic fibrosis transmembrane conductance regulator (CFTR) mutant lacking Phe508 (DeltaF508)(Riordan, 2008). The DeltaF508 protein appears to be trapped in a prefolded state with incomplete packing of the transmembrane segments, a defect that can be repaired by direct interaction with correctors such as corr-4a, VRT-325, and VRT-532 (Wang et al., 2007). CFTR interacts directly with MRP4 (3.A.1.208.7) to control Cl- secretion (Li et al., 2007). It has intrinsic adenylate kinase activity that may be of functional importance (Randak and Welsh, 2007). The intact CFTR protein mediates ATPase rather than adenylate kinase activity (Ramjeesingh et al., 2008). Regulated by Na+/H+ exchange regulatory cofactors (NHERF; O14745; TC #8.A.24.1.1) (Seidler et al., 2009).

Animals

CFTR of Homo sapiens

 
3.A.1.203 The Peroxysomal Fatty Acyl CoA Transporter (P-FAT) Family (ABCD)
3.A.1.203.1Peroxysomal long chain fatty acyl (LCFA) transporter associated with Zellweger SyndromeAnimalsPMP70 of Homo sapiens
 
3.A.1.203.2Peroxysomal long chain fatty acyl (LCFA) Coenzyme A import porterYeastPat1 (758-870 aas; 5 TMSs)/Pat2 (853 aas; 4 TMSs) of Saccharomyces cerevisiae
 
3.A.1.203.3The peroxysomal long chain fatty acid (LCFA) half transporter, ABCD1 (ALD, the adrenoleukodystrophy protein) (functions as a homodimer and accepts acyl-CoA esters (van Roermund et al. 2008)).

Animals

LCFA transporter of Homo sapiens

 
3.A.1.203.4The BacA (Rv1819c) porter (selective bleomycin and antimicrobial peptides) (essential for maintenance of extended chronic infection) (Domenech et al., 2009).

BacA of Mycobacterium tuberculosis (Q50614)

 
3.A.1.203.5Peroxisomal importer, Comatose, of substrates for β-oxidation (transports precursors 2,4-dichlorophenoxybutyric acid (2,4-DB) and indole butyric acid (IBA) (Dietrich et al., 2009)).

Plants

Comatose of Arabidopsis thaliana (Q94FB9)

 
3.A.1.204 The Eye Pigment Precursor Transporter (EPP) Family (ABCG)
3.A.1.204.1Eye pigment precursor transporterAnimals, yeastWhite of Drosophila melanogaster
 
3.A.1.204.2

Drug resistance transporter, ABCG2 (MXR; ABCP) (human breast cancer resistance protein). It exports haem in haempoietic cells (Latunde-Dada et al., 2006) as well as cytotoxic agents (mitoxantrone, flavopiridol, methotrexate, 7-hydroxymethotrexate, methotrexate diglutamate, topotecan, and resveratrol), fluorescent dyes (Hoechst 33342) and other toxic substances (PhIP and pheophorbide a) (Özvegy-Laczka et al., 2005). It also transports folate and sterols: estradiol, and probably cholesterol, progesterone, testosterone and tamoxifen (Janvilisri et al., 2003; Breedveld et al., 2007). It is a homotetramer (Xu et al., 2004). It forms a homodimer bound via a disulfide bond at Cys-603 which stabilizes the protein against ubiquitin-mediated degradation in proteosomes (Wakabayashi et al., 2007). It has 6 established TMSs with the N- and C- termini inside (Wang et al., 2008).

Animals, yeast

ABCG2 (ABCP) of Homo sapiens (Q9UNQ0)

 
3.A.1.204.3Breast cancer resistance protein, BCRP (ABCG) (MDR pump) (exports from human breast cancer cell line MCF-7: miloxantrone, daunorubicin, doxorubicin and rhodamine123). Also transports reduced folates as well as mono-, di- and tri-glutamate derivatives of folic acid and methotrexate (Assaraf et al., 2006).AnimalsBCRP of Homo sapiens (AAC97367)
 
3.A.1.204.4The plant cuticular wax exporter, CER5 (in the plasma membrane of epidermal cells; secretes wax to the plant surface) (Pighin et al., 2004)Plants CER5 (C-M) of Arabidopsis thaliana (AAU44368)
 
3.A.1.204.5The ABCG5 (sterolin-1)/ABCG8 (sterolin-2) heterodimeric neutral sterol (cholesterol and plant sterols) (e.g., sitosterol) (phosphoryl donors ATP > CTP > GTP > UTP) exporter; present in the apical membranes of enterocytes and hepatocytes. Cholesteryl oleate, phosphatidyl choline and enantiomeric cholesterol are poorly transported (mutation of either ABCG5 or ABCG8 cause sitosterolemia and coronary atherosclerosis) (Zhang et al., 2006; Wang et al., 2006)AnimalsABCG5/ABCG8 of Homo sapiens
ABCG5 (Q9H222)
ABCG8 (Q9H221)
 
3.A.1.204.6The efflux porter for phosphatidylcholine and its analogues as well as toxic alkyl phospholipids, ABCG4 (Castanys-Munoz et al., 2007)Protozoa ABCG4 of Leishmania infantum (A4HWI7)
 
3.A.1.204.7Multidrug resistance efflux pump, AbcG6, causes camptothecin-resistant parasites (Bosedasgupta et al., 2008)EukaryotaAbcG6 of Leishmania donovani (A8WEV1)
 
3.A.1.204.8The epidermal plasma membrane cuticular lipid (wax) exporter, ABCG11 (wbc11); may interact with CER5 (Bird et al., 2007).

Plants

ABCG11 of Arabidopsis thaliana (Q8RXN0)

 
3.A.1.205 The Pleiotropic Drug Resistance (PDR) Family (ABCG)
3.A.1.205.1Pleiotropic drug resistance (PDR) exporter; steroid exporter; sporidesmin toxicity suppressor (Sts1); MDR; cyclic nucleotide exporter; amphipathic anion exporter. Its ATPase activity is inhibited by its substrate, clotrimazole; can use ATP, GTP and maybe UTP to drive efflux (Golin et al., 2007). YeastPdr5 (Sts1; Ydr1) of Saccharomyces cerevisiae (P33302)
 
3.A.1.205.2Drug/Sterol/Mutagen exporter, Snq2pYeastSnq2p of Saccharomyces cerevisiae (P32568)
 
3.A.1.205.3Weak acid exporter, Pdr12p (exports preservative anions including propionate, sorbate and benzoate) (Mollapour et al., 2008)YeastPdr12p of Saccharomyces cerevisiae (Q02785)
 
3.A.1.205.4

Multidrug resistance protein, Cdr1 (confers resistance to cycloheximide and antifungal agents such as azoles and terbinafine) (Holmes et al., 2006; Schuetzer-Muehlbauer et al., 2003); also, transports phospholipids (Shukla et al., 2007). It is the major fluconazole efflux system in fluconazole-resistant C. albicans (Holmes et al., 2008).

Yeast

Cdr1 of Candida albicans (P43071)

 
3.A.1.205.5Multidrug resistance protein, Cdr2 (confers resistance to azole and other antifungal agents/terbinafine, amorolfine, aspofungin, etc. as well as a variety of metabolic inhibitors) (Schuetzer-Muehlbauer et al., 2003)YeastCdr2 of Candida albicans (P78595)
 
3.A.1.205.6Multidrug resistance protein, CnAFR1 (confers resistance to azole antifungal drugs including fluconazole) (Posteraro et al., 2003)FungiCnAFR1 of Cryptococcus neoformans (Q8X0Z3)
 
3.A.1.205.7The multidrug resistance protein, AtrB (confers resistance to all major classes of fungicides as well as natural toxic compounds substrates include: anilinopyrimidine, benzimidazole, phenylpyrrole, phenylpyridylamine, strobirulin, azoles, dicarboximides, quintozene, acriflavin, and rhodamine 6G as well as natural toxins such as camptothecin (an alkaloid) and the stilbene phytoalexin, resveratrol) (Andrade et al., 2000). FungiAtrB of Aspergillus nidulans (P78577)
 
3.A.1.205.8The multidrug resistance protein, Pdr11p, mediates sterol uptake by promoting movement of sterols from the plasma membrane to the endoplasmic reticulum where esterification occurs (Li and Prinz, 2004).YeastPdr11p of Saccharomyces cerevisiae (P40550)
 
3.A.1.205.9The plasma membrane Cd2+/Pb2+ efflux pump (heavy metal resistance pump), PDR8 (present in root hair and epidermal cells; it may export a broad range of substrates) (Kim et al., 2007)PlantsPDR8 of Arabidopsis thaliana (Q9XIE2)
 
3.A.1.205.10Pleiotropic drug resistance (PDR) exporter, PDR12 (function as a pump to exclude Pb2+ ions and/or Pb2+- containing toxin compounds) (Lee et al., 2005)PlantsPDR12 of Arabidopsis thaliana (Q9M9E1)
 
3.A.1.205.11The brefeldin resistance protein, Bfr1, (also exports actinomycin D, cerulenin, and cytochalasin B) (Turi and Rose, 1995; Nagao et al., 1995).YeastBfr1 of Schizosaccharomyces pombe (P41820)
 
3.A.1.205.12The plasma membrane Pdr10, a negative regulator for incorporation of Pdr12 (TC# 3.A.1.205.3) into detergent-resistant membranes, a novel role for members of the ABC transporter superfamily (Rockwell et al., 2009) (most like 3.A.1.205.1; 67% identity).

Yeast

PDR10 of Saccharomyces cerevisiae (P51533)

 
3.A.1.206 The a-Factor Sex Pheromone Exporter (STE) Family (ABCB)
3.A.1.206.1a-Factor sex pheromone exporter (Ste6)YeastSte6 of Saccharomyces cerevisiae
 
3.A.1.207 The Eukaryotic ABC3 (E-ABC3) Family
Description:

(functions unknown; ABC-type ATPases have not been identified.)

3.A.1.207.1The hypothetical protein, HP (1209aas; 10TMSs:1+6+3; 2-4 are homologous to 8-10; the FtsX domain) (P. tetraurelia has at least 5 paralogues.)CiliatesHP of Paramecium tetraurelia (M) (A0ECD9)
 
3.A.1.207.2Putative permeases; Duf214 protein (1234aas; 10TMSs: 1+6+3; 2-4 are homologous to 8-10 (the FtsX domain))CiliatesPutative permease of Tetrahymena thermophila (M) (Q22NS1)
 
3.A.1.207.3Hypothetical protein, HP (1465aas; 8TMSs:1+6+1) (D. discoideum has several paralogues)Slime moldHP of Dictyostelium discoideum (M) - Q8ST07
 
3.A.1.207.4

Hypothetical protein, HP, 1129aas (homologous are found in many unicellular eukaryotes)

Amoeba

HP of Entamoeba histolytica (M) (C4LT38)

 
3.A.1.208 The Drug Conjugate Transporter (DCT) Family (ABCC)
3.A.1.208.1Multi-drug resistance-associated protein, MRP1-like protein (MLP1 or MRP1) (Exporter of leukotrienes, glutathione and cysteinyl conjugates of organic anions, drugs, unmodified hydrophobic xenobiotics and hydrophilic conjugated endobiotics). Vincristine and glutathione are co-transported. MRP1 catalyzes export of glutathione during apoptosis (Hammond et al., 2007). Also transports reduced folates as well as mono-, di- and tri-glutamate derivatives of folic acid and methotrexate (Assaraf et al., 2006).AnimalsMRP1 of Rattus norvegicus (O88269)
 
3.A.1.208.2Hepatic canalicular conjugate exporter (the Dubin-Johnson Syndrome protein) (transports bilirubin glucuronides; E2 17 β glucuronide, dianionic bile salts such as taurocholate, taurochenodeoxycholate sulfate and taurolithocholate sulfate; reduced glutathione; glutathione conjugates; cysteinyl leukotrienes; arsenic-glutathione complexes and glutathione disulfide; also exports anthracyclines, epipodophyllotosine, Vinca alkaloids, cisplatin, methotrexate, and the protease inhibitor, lopinavir) (also called ABCC2) AnimalscMRP (MRP2; cMOAT) of Homo sapiens (Q92887)
 
3.A.1.208.3Oligomycin-resistance protein YOR1 in plasma membrane (confers resistance to oligomycin, rhodamine B, tetracycline, verapamil, eosin Y and ethidium bromide; Grigoras et al., 2007)).YeastYOR1 of Saccharomyces cerevisiae (P53049)
 
3.A.1.208.4SUR1 sulfonylurea receptor; subunit and regulator of α-cell ATP-sensitive K+ channel (TC #1.A.2); determines ATP sensitivity; no inherent transport function known; associated with persistent hyperinsulinemic hypoglycemia of infancy due to focal adenomatous hyperplasia (also called ABCC8). Gain-of-function mutations in the genes encoding the ATP-sensitive potassium (K(ATP)) channel subunits Kir6.2 (KCNJ11) and SUR1 (ABCC8) cause neonatal diabetes mellitus. Because mutant channels are inhibited less strongly by MgATP, this increases K(ATP) currents in pancreatic beta cells, thus reducing insulin secretion and producing diabetes (de Wet et al., 2007).AnimalsSUR1 of Homo sapiens (Q09428)
 
3.A.1.208.5Vacuolar multidrug resistance efflux pump, AtMRP2 (catalyzes vacuolar uptake of glutathione conjugates (i.e., 2,4-dinitrophenyl-GS), glucuronide conjugates (i.e., 17 β-estradiol 17(β-D-glucuronide), and reduced glutathione). Also exports the herbicide, 1-chloro-2, 4-dinitrobenzene, and chlorophyll degradation catabolites (Frelet-Barrand et al., 2008).PlantsAtMRP2 of Arabidopsis thaliana (O64590)
 
3.A.1.208.6Metal-thiol conjugate exporter, PgpA; glutathione and trypanothione conjugates are exported; confers arsenite and antimonite resistance (trypanothione is glutathione-spermidine). ProtozoaPgpA of Leishmania tarentolae (P21441)
 
3.A.1.208.7MRP4 (exporter of cyclic nucleotides (cAMP, cGMP)and other nucleotide analogues), purine analogues, methotrexate, bile acids, prostaglandins E1 and E2, reduced folates, 9(2-phosphonylmethyoxyethyl)adenine, leukotrienes, estradiol 17-β-D-glucuronide) and drug sulfate conjugates (inhibited by nonsteroidal antiinflammatory drugs (Reid et al., 2003; Rius et al., 2007)). When overexpressed, it can lower the intracellular concentration of nucleoside/nucleotide analogs, such as the antiviral compounds PMEA (9-(2-phosphonylmethoxyethyl)adenine) or ganciclovir, and of anticancer nucleobase analogs, such as 6-mercaptopurine, after their conversion into the respective nucleotides. MRP4 interacts directly with CFTR (3.A.1.202.1) to control Cl- secretion (Li et al., 2007). Thus, MRP4 is a broad specificity organic anion exporter (Ritter et al., 2005).AnimalsMRP4 (MOAT-B) of Homo sapiens (O15439)
 
3.A.1.208.8Drug resistance pump; ABCC1 (MRP1), exports chemotherapeutic agents, organic anions such as leukotriene C4 (LTC4), 17-β-estradiol 17-β-D-glucuronide, glucuronide-X (E217βG, etoposide-glucuronide), estrone-3-sulfate, folic acid and methotrexate, arsenic triglutathione, arsenic and antimonial oxyanians, glutathione (GSH), GSSG, glutathione conjugate (GSH-X; LTC4, DNP-SG, EA-SG, NEH-SG), sulfate-X (E1S, DHEAS), HIV protease inhibitors, anthracyclines, epipodophyllotoxins, and Vinca alkaloids. Changing charged residues in TMS6 (K332, H335 and D336) gave rise to specific changes in specificity (Chen et al., 2006; Haimeur et al., 2002; Leslie et al., 2004)AnimalsMRP1 of Homo sapiens (P33527)
 
3.A.1.208.9Canicular multispecific organic anion transporter, MRP3 (also called ABCC3) (most similar in sequence to MRP2). MRP3 exports epipodophyllotoxins, etoposide and teniposide, estradiol 17-β-D-glucuronide, leukotriene C4, dinitrophenyl S-glutathione, epoposide glucuronide, methotrexate, bilirubin-glucuronides, bile acids, GSH-X (LTC4, DNP-SG) and sulfate-X (taurolithocholate-3-sulfate).AnimalsMRP3 of Homo sapiens (O15438)
 
3.A.1.208.10Multidrug (anthracycline) resistance organic anion efflux pump (ABC-C6; MRP6; MOAT-E - the pseudoxanthoma elasticum disease protein) exports glutathione conjugates including lencotriene C4, DNP, and N-ethylmaleimide S-glutathione; also exports anthracyclines, epipodophyllotoxins, cisplatin, and probably exports probenecid, benzbromarone and indomethacin. AnimalsABCC6 (MRP6) of Homo sapiens (O95255)
 
3.A.1.208.11Vacuolar metal resistance and drug detoxification protein, yeast cadmium factor (YCF1); transports cadmium-glutathione conjugates, glutathione S-conjugated leucotriene C4, organic glutathione S-conjugates, unconjugated bilirubin and reduced glutathioneYeastYCF1 of Saccharomyces cerevisiae (P39109)
 
3.A.1.208.12Bile acid transporter, BAT1 (in vacuoles)YeastBAT1 of Saccharomyces cerevisiae (P32386)
 
3.A.1.208.13Cyclic nucleotide (cAMP and cGMP) efflux pump, MRP8 (ABCC11); also exports other nucleoside and nucleotide analogues, and confers resistance to fluoropyrimidines and the anti-AIDS drug, 2',3'-dideoxycytidine (Guo et al., 2003). Human earwax consists of wet and dry types. Dry earwax is frequent in East Asians, whereas wet earwax is common in other populations. A SNP, 538G --> A (rs17822931), in the ABCC11 gene is responsible for determination of earwax type. Cells with allele A show a lower excretory activity for cGMP than those with allele G. The 538G --> A SNP is the first example of DNA polymorphism determining a visible genetic trait (Yoshiura et al., 2006).AnimalsMRP8 (ABCC11) of Homo sapiens (Q9BX80)
 
3.A.1.208.14The vacuole (tonoplast) ZmMrp3 anthocyanin pigment transporter (ABCF) (Goodman et al., 2004)PlantsZmMrp3 of Zea mays
ZmMrp3 (MC-MC) (Q6J0P5)
 
3.A.1.208.15The general organic anion exporter, MRP5 (MOATC). It exports cyclic AMP, cyclic GMP, 5'-FUMP, glutathione and glutathione conjugates and antimonial tartrate). Also transports reduced folates as well as mono-, di- and tri-glutamate derivatives of folic acid and methotrexate (Assaraf et al., 2006). When overexpressed, it can lower the intracellular concentration of nucleoside/nucleotide analogs, such as the antiviral compounds PMEA (9-(2-phosphonylmethoxyethyl)adenine) or ganciclovir, and of anticancer nucleobase analogs, such as 6-mercaptopurine, after their conversion into the respective nucleotides (Ritter et al., 2005).AnimalsMRP5 of Homo sapiens (O15440)
 
3.A.1.208.16The vacuolar Abc2p (SPAC3F10.11c) transporter for xenobiotics, glutathione S-conjugates and monochlorobimane (Iwaki et al., 2006)YeastAbc2p of Schizosaccharomyces pombe (MCMC; 1478 aas) (Q10185)
 
3.A.1.208.17The vacuolar glutathione-conjugate and chlorophyll catabolite transporter, MRP3 (Tommasini et al., 1998)PlantsMRP3 of Arabidopsis thaliana (Q9LK64)
 
3.A.1.208.18Vacuolar glutathione conjugate, glutathione exporter; mediates cadmium detoxification and ade2 pigmentation in vivo (Sharma et al., 2002). (Most similar to Ycf1 of S. cerevisiae (TC# 3.A.1.208.11; 41% identity))PlantsBpt1 of Saccharomyces cerevisiae (P14772)
 
3.A.1.208.19Mussel ABCC/MRP-like transporter, MdlB (1498aas). Transports verapamil, pentachlorphenol, vinblastine, trifluoperazine, emetine, quinidine, forskolin, cyclosporin, and PSC833 compounds that block efflux of fluorescent dye substrates from the gills (T. Luckenbach & D. Epel, 2008).EukaryotesABCC-like transporter of Mytilus californianus (ABS83557)
 
3.A.1.208.20The possible HCO3- transporter, HLA3 (Duanmu et al., 2009).

Algae

HLA3 of Chlamydomonas reinhardtii (A8I268)

 
3.A.1.208.21The vacuolar MRP1 (sequesters in the vacuole glutathione conjugates, folate mono-glutamates (pteroyl-1-glutamate) and antifolates (methotrexate); (Raichaudhuri et al. 2009) (86% identical to MRP2 (3.A.1.208.5))

Plants

MRP1 of Arabidopsis thaliana (Q9C8G9)

 
3.A.1.208.22

The thale cress protein ATMRP5 (ATABCC5), a high-affinity inositol hexakisphosphate transporter; involved in guard cell signaling and phytate storage (Nagy et al., 2009).

Plants

MRP5/ABCC5 of Arabidopsis thaliana (Q7GB25)

 
3.A.1.209 The MHC Peptide Transporter (TAP) Family (ABCB)
3.A.1.209.1MHC heterodimeric peptide exporter (TAP) (from cytoplasm to the endoplasmic reticulum) (TAP1=ABCB2; TAP2=ABCB3) (defects in TAP1 or TAP2 cause immunodeficiency) (TAP1/TAP2 is stabilized by tapasin isoforms 1, 2 and 3) (Raghuraman et al., 2002). TAP1 has 10 TMSs, 4 unique N-terminal TMSs and 6 TMSs that form the translocation pore with N- and C-termini in the cytosol (Schrodt et al., 2006). The TAP2 nucleotide binding site appears to be the main catalytic active site driving transport suggesting asymmetry in the transporter (Perria et al., 2006). Animals, yeastTAP1/TAP2 of Homo sapiens
 
3.A.1.209.2The lysosomal ABC B9 (TAPL) polypeptide transporter with broad length specificity and preference for positively charged peptides (Zhao et al., 2008) (takes up peptides into lysosomes of dendritic cells and macrophages; induced during differentiation from monocytes (Demirel et al., 2007).

TAPL of Homo sapiens (Q9NP78)

 
3.A.1.210 The Heavy Metal Transporter (HMT) Family (ABCB)
3.A.1.210.1The putative mitochondrial iron transporter, ATM1 (possibly specific for iron-sulfur clusters)Yeast; animals, protozoa bacteriaATM1 of Saccharomyces cerevisiae
 
3.A.1.210.2The vacuolar heavy metal tolerance protein precursor, HMT1 (transports phytochelins and Cd2+·phytochelin complexes) (Prévéral et al., 2009).

Yeast; animals, protozoa bacteria

HMT1 of Schizosaccharomyces pombe

 
3.A.1.210.3The ABC transporter homologueYeast; animals, protozoa bacteriaABC transporter homologue in Rickettsia prowazekii
 
3.A.1.210.4ABC7 iron transporter (X-linked sideroblastis anemia protein) (also called ABCB7)Yeast; animals, protozoa bacteriaABC7 iron transporter of Homo sapiens
 
3.A.1.210.5Multidrug resistance homologues, Pfmdr2, proteinYeast; animals, protozoa bacteriaPfmdr2 protein of Plasmodium falciparum
 
3.A.1.210.6Mitochondrial outer membrane anionic porphyrin uptake half ABC transporter, ABCB6 (expressed in many mammalian tissues including fetal liver) in response to intracellular porphyrin; porphyrin uptake activates de novo porphyrin (haem) biosynthesis (Krishnamurthy et al., 2006). AnimalsABCB6 of Homo sapiens (Q9NP58; 842 aas)
 
3.A.1.210.7The heavy metal tolerance protein, CeHMT-1 (exports phytochelatin (γ(Glu-Cys)n)-Cd2+ complexes) (Vatamaniuk et al., 2005)AnimalsCeHMT-1 of Caenorhabditis elegans (AAM33380)
 
3.A.1.210.8Mitochondrial ABC transporter, ATM3 involved in iron homeostasis. There are three isoforms ATM1, ATM2 and ATM3 (Chen et al., 2007). ATM3 can replace the yeast iron/sulfur cluster exporter better than ATM1 or ATM2. It is most similar to the human and yeast homologues, TC# 3.A.1.210.4 and 3.A.1.210.1, 51% and 47% identical, respectively.PlantsATM3 of Arabidopsis thaliana (Q9LVM1)
 
3.A.1.210.9

The Ni2+/Co2+ exporter AtmA (Mikolay and Nies, 2009).

Bacteria

AmA of Cuperiavidus metallidurans (Q1LRE9).

 
3.A.1.211 The Cholesterol/Phospholipid/Retinal (CPR) Flippase Family (ABCA)
3.A.1.211.1The cholesterol/phospholipid flippase, ABC1 (called ABCA1 in humans; Tangier disease proteins; 2261 aas; sp: O95477). An amphipathic helical region of the N-terminal barrel of the phospholipid transfer protein (PLTP) is critical for ABCA1-dependent cholesterol efflux (Oram et al., 2008). PLTP helix 144-163 removes lipid domains formed by ABCA1, stabilizing ABCA1, interacting with phospholipids, and promoting phospholipid transfer by direct interactions with ABCA1. May transport sphingosine-1-phosphate (Kobayashi et al., 2009).

Animals and plants

ABC1 of Mus musculus

 
3.A.1.211.2The retinal-specific ABC transporter (RIM protein, ABCR or ABCA4) (Stargardt's disease protein, involved in retinal/macular degeneration) in the rod outer segment. May flip retinal, or more likely, N-retinylidene-phosphatidylethanolamine, a product generated from the photobleaching of rhodopsin, from the lumen to the cytoplasmic side of disc membranes following the photobleaching of rhodopsin, insuring that retinoids do not accumulate in disc membranes (Molday, 2007; Molday et al. 2009)

Animals

RIM protein (ABCR) of Homo sapiens

 
3.A.1.211.3Multidrug resistance pump, ABCA2 (ABC2)AnimalsABCA2 of Homo sapiens
 
3.A.1.211.4The aced cell death 7 (ced-7) protein (translocates molecules that mediate adhesion between dying and engulfing embryonic cells during programmed death). AnimalsCed-7 of Caenorhabditis elegans (P34358)
 
3.A.1.211.5The surfactant-secreting porter, ABCA3 (exports lipids and proteins into lamellar bodies). Fatal surfactant deficiency (FSD) can result from mutations in ABCA3, causing abnormal intracellular localization (type I) or decreased ATP hydrolysis (type II). ABCA3 is found in lamellar bodies of lung alveolar type II cells where it probably secretes surfactants (mixture of lipids; e.g., PC) and proteins (e.g., surfactant proteins A, B, C and D) stored in lamellar bodies and exocytosed (Matsumura et al., 2006). ABCA3 plays an essential role in pulmonary surfactant lipid metabolism and lamellar body biogenesis, probably by transporting these lipids as substrates (Ban et al., 2007). Cheong et al. (2007) have shown that ABCA3 is critical for lamellar body biogenesis in mice. They suggest it functions in surfactant-protein B processing and lung development late in gestation. AnimalsABCA3 of Homo sapiens (Q99758)
 
3.A.1.211.6Xenobiotic transporter, ABCA8 (transports estradiol-β-glucuronide, taurocholate, LTC4, para-amino-hippurate and ochratoxin-A (Tsuruoka et al., 2002) Animals ABCA8 of Homo sapiens (O94911)
 
3.A.1.211.7Half sized ABCA exporter, AbcAAmoebaAbcA of Dictyostelium discoideum
M-C 655 aas; (Q94479)
 
3.A.1.212 The Mitochondrial Peptide Exporter (MPE) Family (ABCB)
3.A.1.212.1The mitochondrial peptide exporter, Mdl1p (exports peptides of 6-21 amino acyl residues from the mitochondrial matrix as well as degradation products of misassembled respiratory chain complexes) (Janas et al., 2003; van der Does et al., 2006; Gompf et al., 2007). A leaderless Mdl1p targets to the ER membrane instead of to the mitochondria (Gompf et al., 2007).YeastMdl1p of Saccharomyces cerevisiae (P33310)
 
3.A.1.212.2ABC mitochondrial peptide/MDR half transporter, MdlB. High copy number suppressor of ATM1 [iron-sulfur cluster transporter (3.A.1.210.1)]BacteriaMd1B of Saccharomyces cerevisiae (M-C) (P33311)