TCDB is operated by the Saier Lab Bioinformatics Group
TCIDNameDomainKingdom/PhylumProtein(s)
*4.A.6.1.1









The mannose (glucose, 2-deoxyglucose, glucosamine, N-acetylglucosamine, N-acetylmannosamine, mannosamine and fructose) PTS porter/group translocator, ManXYZ (Rephaeli and Saier 1980; Plumbridge 2015). Catalyzes xylose facilitated diffusion in lactobacilli. The order of D-sugar substrate affinities is: glucose > mannose > 2-deoxyglucose > N-acetylglucosamine > glucosamine > N-acetylmannosamine > mannosamine > fructose (Rephaeli and Saier 1980).  The mechanism appears to be rapid equilibrium, random, bi-bi sequential (Rephaeli and Saier 1980). L-sugars are not transported. This system is allostericallly inhibited by a complex of DicB (62 aas, P09557) and MinC (231 aas, P18186) (Jeckelmann and Erni 2020). At the transcriptional level, the manXYZ operon is regulated by the Mlc transcriptional regulator, and at the translational level it is regulated by the DicF small RNA that is complementary to manXYZ (Jeckelmann and Erni 2020). The 3-d structure of the IIC/IID complex revealed that the N- and C-terminal halves form the transport and scaffold domains, respectively (Liu et al. 2019).  Two 3-helix bundles are mixed by an intersubunit helix swap yielding tight intersubunit contacts with a novel fold. An "elevator" mechanism has been proposed in which the transport domain moves vertically or rotates relative to a stationary scaffold domain, where both the transport and scaffold domains consist of α-helices of both the IIC aqnd IID domains. Only the IIC and IID proteins, not hte IIAB protein are required for lambda phage infectivity (Esquinas-Rychen and Erni 2001).

 

Bacteria
Proteobacteria
Mannose IIAB-IIC-IID (ManXYZ) complex of E. coli
*4.A.6.1.2









Bacteria
Firmicutes
Fructose IIA-IIB-IIC-IID complex of Bacillus subtilis
LevD (IIA), 146 aas, P26379
LevE (IIB), 163 aas, P26380
LevF (IIC), 268 aas, 7 TMSs, P26381
LevG (IID), 275 aas, 5 - 7 putative TMSs
*4.A.6.1.3









Sorbose porter (Wehmeier et al. 1995). It also supports mannose transport and phosphorylation.  In E. coli, this system does not support lambda phage infection although the Bacillus subtilis ortholog does (Martin-Verstraete et al. 1996).

Bacteria
Proteobacteria
Sorbose IIA-IIB-IIC-IID complex of Klebsiella pneumoniae
*4.A.6.1.4









N-acetyl galactosamine (GalNAc or Aga) porter (used the same IIA protein (AgaF) as does 4.A.6.1.5) (Brinkkötter et al. 2000).

Bacteria
Proteobacteria
AgaVWEF complex (IIAga) of E. coli
*4.A.6.1.5









Galactosamine (GalN or Gam) porter (used the same IIA protein (AgaF) as does 4.A.6.1.4) (Brinkkötter et al. 2000).

Bacteria
Proteobacteria
AgaBCDF complex (IIGam) of E. coli
*4.A.6.1.6









Glucose porter, ManLMN (Yebra et al., 2006)

Bacteria
Firmicutes
ManLMN of Lactobacillus casei
ManL (IIAB) (AAY63962)
ManM (IIC) (AAY63963)
ManN (IID) (AAY63964)
*4.A.6.1.7









The glucose/mannose/2-deoxyglucose/fructose phosphotransferase systems (phosphorylates without transport), ManLMN (Cochu et al., 2003)
Bacteria
Firmicutes
ManLMN of Streptococcus thermophilus
ManL (IIAB) (Q5M5W6)
ManM (IIC) (Q5M5W7)
ManN (IID) (Q5M5W8)
*4.A.6.1.8









The gluconate PTS uptake system. IIAGnt and IIBGnt form a high affinity 2:2 heterotetrameric complex (Brockmeier et al., 2009; Reinelt et al., 2009).

Bacteria
Firmicutes
The PTS gluconate uptake system of Enterococcus faecalis
IIAGnt (Q82ZC8)
IIBGnt (Q82ZC7)
IICGnt (Q82ZC5)
IIDGnt (Q82ZC6)
*4.A.6.1.9









The fucose PTS uptake transporter, IIA/IIB/IIC/IIDFuc (FcsABCD) (Manzoor et al. 2015). Expression in response to fucose is under the control of the FcsR transcriptional activator, and its DNA binding site has been identified (Manzoor et al. 2015).

Bacteria
Firmicutes
FucTA, B, C, D (also called FcsABCD) of Streptococcus pneumoniae
FucTA (IIA) (Q97N91)
FucTB (IIB) (Q97N92)
FucTC (IIC) (Q97N93)
FucTD (IID) (Q97N94)
*4.A.6.1.10









The hexose (glucose and fructose demonstrated) PTS uptake system (Kim et al., 2011).

Bacteria
Firmicutes
The hexose uptake system IIAB, IIC, IID of Oenococcus oeni 
IIABhex (C) (Q04GK1) 
IIChex (M) (Q04GK0)
IIDhex (M) (Q04GJ9)
*4.A.6.1.11









Mannose enzyme II complex, IIAB, IIC, IID. IIC/IID serve allows entry of some bacteriocins including pediocin (class IIa), lactococcin A and lactococcin Z (class IIc) (Kjos et al., 2011; Daba et al. 2018). Transports and phosphorylates Glucose, Mannose and Glucosamine.  The IID component is the probably receptor for several bacteriocins, subclass IIa bacteriocins (pediocin-like; pediocins) and subclass IId ones - lactococcin A (LcnA), lactococcin B (LcnB), garvicin Q (GarQ), and garvicins A, B and C (GarA-C) (Tymoszewska et al. 2018). Individual amino acids localized mostly in the sugar channel-forming transmembrane parts of subunit IIC or in the extracellular parts of IID likely are involved in the interaction with each bacteriocin, and these have been specified (Tymoszewska et al. 2018).

Bacteria
Firmicutes
IIAB, IIC, and IID of Lactococcus lactis 
IIAB (D2BKY7)
IIC (D2BKY8) 
IID (D2BKY9) 
*4.A.6.1.12









Putative Hexose Enzyme II complex, IIABCD

Bacteria
Proteobacteria
IIABCD of Myxococcus xanthus IIA IIB IIC IID
*4.A.6.1.13









Fucosyl-α-1,3-N-acetylglucosamine PTS uptake porter, AlfEFG (next to an operon encoding a fucosidase (AlfB) and a transcriptional regulator of the GntR family, AlfR).  The fucosidase is specific for this disaccharide which is present in mammalian glycoproteins, glycolipids and milk (Rodríguez-Díaz et al. 2012).  Uptake is dependent of AlfF but not on the PTS Enzyme I, suggesting that uptake does not require phosphorylation, consistent with the activity of AlfB as a fucosidase.  Only the glucosamine moiety is utilized and the fucose moiety, after hydrolysis, is excreted (Rodríguez-Díaz et al. 2012).

Bacteria
Firmicutes
AlfEFG of Lactobacillus casei.
AlfE  (IIAB)
AlfF  (IIC)
AlfG  (IID)
*4.A.6.1.14









Probable PTS uptake porter (IIA - IID) for disaccharides of glucuronate and N-acetyglucosamine derived from degradation of hyaluronate and chondroitin by hyaluronidase (Marion et al. 2012). The cytoplasmic phosphorylated disaccharide (possibly glucuronyl-N-acetyglucosamine) may be hydrolyzed by the enzyme Ugl. 

Bacteria
Terrabacteria group
Hyaluronate disaccharide porter of Streptococcus pneumoniae
*4.A.6.1.15









The mannose PTS Enzymes IIABCD, ManLMN (MptACD). It is the primary inducible sugar transporting system, regulated by ManR, the activity of which is controlled by another mannose-like PTS system (see TC# 4.A.6.1.29) that transports sugars slowly but serves as a glucose sensor that inactivates the ManR activator by a phosphorylation/dephosphorylation mechanism (Aké et al. 2011; Zébré et al. 2015).

Bacteria
Firmicutes
Mannose PTS of Listeria monocytogenes
MptA, IIAB, 321 aas (Q7BC72)
MptC, IIC, 268 aas (Q7BC71)
MptD, IID, 303 aas (Q7BC70)

*4.A.6.1.16









Constitutively synthesized (at a low level) sensor, MpoABCD, controlling expression of the man operon-encoding the ManLMN (MptACD) transport system (see TC# 4.A.6.1.15). The Mpo system interacts with and phosphorylates ManR, the transcriptional regulator of the man operon (Aké et al. 2011). This system is a mannose PTS system, IIABCDMan or MpoABCD that transports its sugar substrates slowly and serves as a glucose (sugar substrate) sensor to regulate the activity of ManR by a phosphorylation/dephosphorylation mechanism. MptACD (TC# 4.A.6.1.15) is the primary inducible sugar transport system. ManR is an activator that is inactivated by a phosphorylation/dephosphorylation mechanism (Aké et al. 2011; Zébré et al. 2015).

Bacteria
Firmicutes
MpoABCD of Listeria monocytogenes
MpoA (IID)
MpoB (IIC)
MpoC (IIB)
MpoD (IIA)
*4.A.6.1.17









D-glucosaminate group translocating uptake porter, DgaABCD (IIA-141 aas, IIB-161 aas, IIC-249 aas, and IID-285 aas, respectively) (Miller et al. 2013).  Salmonella enterica subsp. enterica serovar Typhimurium (S. Typhimurium) uses d-glucosaminate (2-amino-2-deoxy-d-gluconic acid) as a carbon and nitrogen source via DgaABCD (d-glucosaminate PTS permease components EIIA, EIIB, EIIC, and EIID). Two other genes in the dga operon (dgaE and dgaF) are required for wild-type growth with d-glucosaminate. Transcription of dgaABCDEF is dependent on RpoN (σ54) and an RpoN-dependent activator gene, dgaR. Introduction of a plasmid bearing dgaABCDEF under the control of the lac promoter into E. coli strains allowed them to grow on minimal medium containing d-glucosaminate. d-Glucosaminate is transported and phosphorylated at the C-6 position by DgaABCD. DgaE converts the resulting d-glucosaminate-6-phosphate to 2-keto-3-deoxygluconate 6-phosphate (KDGP), which is subsequently cleaved by the aldolase DgaF to form glyceraldehyde-3-phosphate and pyruvate. DgaF catalyzes the same reaction as that catalyzed by Eda, a KDGP aldolase in the Entner-Doudoroff pathway, and the two enzymes can substitute for each other in their respective pathways. Orthologs of the dga genes are largely restricted to certain enteric bacteria and a few Firmicutes (Miller et al. 2013).

Bacteria
Proteobacteria
DgaABCD of Samonella enterica Typhimurium
*4.A.6.1.18









Uptake porter/group translocator of galacto N-biose (Gal-β-1,3-GalNAc: galactose linked β-1,3 to N-acetylgalactosamine), lacto N-biose (Gal-β-1,3-GlcNAc: galactose linked β-1,3 to N-acetylglucosamine), and D-N-acetylgalactosamine (Bidart et al. 2014). The system is designated the GnbABCD system where GnbA = IIA, GnbB = IIB, GnbC = IIC, and GnbD = IID of the mannose-type PTS Enzyme II complex.  These disaccaride substrates are human milk oligosaccharides and glycoconjugates (Bidart et al. 2014).

Bacteria
Firmicutes
GnbABCD of Lactobacillus casei
GnbA, IIA, 126 aas
GnbB. IIB, 160 aas
GnbC, IIC, 305 aas
GnbD, IID, 273 aas
*4.A.6.1.19









PTS uptake system for glucoselysine and fructoselysine, GfrABCD (Miller et al. 2015).  Two glycases, GfrE and GfrF, are requred for the utilization of these two compounds for growth, respectively, and GfrF was shown to hydrolyze fructoselysine-6-P to lysine and fructose-6-P.  Expression of the operon, gfrABCDEF, is regulated by a transcriptional activator, GfrR and sigma factor RpoN (Miller et al. 2015).  GfrD affects proteolytic processing, a necessary but insufficient step for CadC activation, rendering CadC able to activate target genes involved in lysine metabolism (Lee et al. 2013).

Bacteria
Proteobacteria
GfrABCD of Salmonella typhimurium
GfrA, IIA, 140 aas
GfrB, IIB, 153 aas
GfrC, IIC, 259 aas
GfrD, IID, 278 aas
*4.A.6.1.20









Putative sorbose PTS Enzyme II complex, IIA, IIB, IIC and IID.  The IIC protein is of 230 aas with 6 - 8 putative TMSs.  The genes encoding IIC and IID are in an operon with an Enzyme I (TC# 8.A.7.1.5) and an HPr (TC# 8.A.8.1.5).

Bacteria
Deferribacteres
IIC/D of Caldithrix abyssi
*4.A.6.1.21









Putative Mannose Enzyme II complex including IIA, IIB, IIC and IID; IIC has 231 aas and 6 TMSs.

Bacteria
Proteobacteria
Mannose Enzyme II complex of Desulfuromonas acetoxidans
*4.A.6.1.22









PTS Mannose-like Enzyme II complex.  IIC, 257 aas and 6 TMSs.  Hits 4.A.6.2.1, 3.1 and 4.1 with scores of e-6 - e-12.

Bacteria
Firmicutes
PTS EII complex of Peptoclostridium difficile
*4.A.6.1.23









Putative Enzyme II complex consisting of IIA, IIB, IIC and IID; IIC has 240 aas and 6 putative TMSs.

Bacteria
Gemmatimonadetes
Putative EII complex of Gemmatimonas aurantiaca
*4.A.6.1.24









Mannose (Man)-type PTS with IIA (129 aas), IIB (167 aas) and IICD (534 aas). The Enzyme I and HPr proteins of this system are 8.A.7.1.6 and 8.A.8.1.6, respectively.  The IICD protein appears to have 8 TMSs in the IIC domain and 5 TMSs in the IID domain.

Archaea
Crenarchaeota
Mannose PTS (IIA, IIB, and IICD) of Thermofilum pendens
IIA of 129 aas
IIB of 167 aas
IICD of 534 aas
*4.A.6.1.25









D-ribitol (D-aldonitol) (a pentitol) PTS Enzyme II complex RtlABCD (Bourand et al. 2013).

Bacteria
Firmicutes
RtlABCD of Lactobacillus casei
*4.A.6.1.26









L-Sorbose PTS enzyme II complex, SorABCD (enzymes IIABCD, respectively (Yebra et al. 2000)). Two operons, encoding the strcutural genes (one homologous to D-glucitol-6-P dehydrogenase) as well as the regulatory genes, are induced by growth on L-sorbose.

Bacteria
Firmicutes
SorABCD of Lactobacillus casei
SorA, 164 aas
SorB, 138 aas
SorC, 277 aas
SorD, 282 aas
*4.A.6.1.27









The Mannose Enzyme IIA/IIB/IIC-IID proteins of the PTS in which the two domains of IIC and IID are fused in a single polypeptide chain, but the IIA and IIB domains are separate proteins (Navdaeva et al. 2011).

Bacteria
Firmicutes
Mannose transport system of Caldanaerobacter subterraneus subsp. tengcongensis (Thermoanaerobacter tengcongensis)
IIA, 136 aas (Q8RD55)
IIB, 167 aas (Q8RD54)
IIC-IID, 554 aas (Q8RD53)
*4.A.6.1.29









Mannose PTS system, IIABCDMan or MpoABCD that transports its sugar substrates slowly and serves as a glucose sensor to regulate the activity of ManR by a phosphorylation/dephosphorylation mechanism. The mannose PTS Enzymes, ManLMN (MptACD), is regulated by ManR. MptACD is the primary inducible sugar transporting system. ManR is regulated by MpoABCD which transports sugars slowly and serves as a glucose (sugar) sensor that inactivates the ManR activator by a phosphorylation/dephosphorylation mechanism (Aké et al. 2011; Zébré et al. 2015).

Bacteria
Firmicutes
MpoABCD of Listeria monocytogenes

*4.A.6.2.1









Uncharacterized PTS Enzyme II complex with a putative IIC protein of 225 aas and 6 TMSs in a 3 + 3 arrangement.  The IIA, IIB and IIC components are encoded adjacent to each other in a single operon.

Bacteria
Proteobacteria
UP of Desulfovibrio hydrothermalis
*4.A.6.2.2









Putative Mannose-type PTS Enzyme II complex. IIC has 248 aas and 6 TMSs.

EII complex of Desulfohalobium retbaense
*4.A.6.3.1









Uncharacterized putative Enzyme II complex including IIA, IIB, IIC and IID.  The IIC protein is of 227 aas with 6 predicted TMSs.

Bacteria
Deferribacteres
Enzyme II complex of Mucispirillum schaedleri
*4.A.6.4.1









Putative mannose/fructose/sorbose PTS Enzyme IIC of 304 aas with 11 predicted TMSs.  No IIA, IIB or IID domain for the mannose/sorbose PTS family was identified in the entire proteome of A. arabaticum.

Bacteria
Firmicutes
Putative PTS Enzyme IIC of Acetohalobium arabaticum
*4.A.6.4.2









Uncharacterized protein of 304 aas and 11 TMSs

Bacteria
Firmicutes
UP of Halobacteroides halobius
*4.A.6.5.1









Putative multi-domain sensor signal transduction histidine kinase of 562 aas with 6 N-terminal TMSs.

Bacteria
Proteobacteria
Putative sensor kinase with an N-terminal 6 TMS domain resembling PTS Mannose-like IIC proteins of Roseibium sp. TrichSKD4