TCID | Name | Domain | Kingdom/Phylum | Protein(s) |
---|---|---|---|---|
1.B.17.1.1 | TolC outer membrane exporter of hemolysin, drugs, siderophores such as enterobactin, etc. (Bleuel et al., 2005). The 3-d structure is available (PDB#1EK9). The three monomers form a continuous channel, and each monomer contributes 4 β-strands to the 12 stranded β-barrel (Koronakis et al. 2000). The Salmonella enterica subspecies Typhi homologue is the ST50 antigen (G4C2H4) used in tests for typhoid fever, and a 2.98 Å resolution structure revealed a trimer that forms an alpha-helical tunnel and a beta-barrel transmembrane channel traversing the periplasmic space and outer membrane, respectively (Guan et al. 2015). K. pneumoniae TolC plays a role in resistance towards most antibiotics, suggesting that it can interact with the AcrB efflux pump (Iyer et al. 2019). | Bacteria |
Proteobacteria | TolC of E. coli |
1.B.17.1.2 | PrtF outer membrane exporter of proteases | Bacteria |
Proteobacteria | PrtF of Erwinia chrysanthemi |
1.B.17.1.3 | The OMF, EexF (functions with ABC exporter, EexD (TC# 3.A.1.110.10) and MFP EexE (TC# 8.A.1.3.3)) (Gimmestad et al., 2006). | Bacteria |
Proteobacteria | EexF of Azotobacter vinelandii (C1DS86) |
1.B.17.1.4 | TolC of Sinorhizobium meliloti (affects secretion of proteins, polysaccharide, and multiple drugs (Cosme et al., 2008)) | Bacteria |
Proteobacteria | TolC of Sinorhizobium meliloti (Q92Q38) |
1.B.17.1.5 | Putative outer membrane factor of 420 aas | Bacteria |
Chlamydiae/Verrucomicrobia group | Outer membrane factor of Parachlamydia acanthamoebae |
1.B.17.1.6 | Uncharacterized protein of 425 aas with an N-terminal TMS. | Bacteria |
Proteobacteria | UP of Bdellovibrio exovorus |
1.B.17.1.7 | Outer membrane protein of 462 aas and 1 N-terminal TMS | Bacteria |
Proteobacteria | OMP of Bdellovibrio bacteriovorus |
1.B.17.2.1 | CnrC outer membrane exporter of Ni2+ and Co2+. Functions with TC# 2.A.6.1.1 and 8.A.1.2.1. | Bacteria |
Proteobacteria | CnrC of Alcaligenes eutrophus |
1.B.17.2.2 | CzcC outer membrane exporter of Co2+, Cd2+, Zn2+. Functions with CzcAB (2.A.6.1.2). | Bacteria |
Proteobacteria | CzcC of Alcaligenes eutrophus |
1.B.17.2.3 | CyaE outer membrane exporter of cyclolysin | Bacteria |
Proteobacteria | CyaE of Bordetella pertussis |
1.B.17.2.4 | Outer membrane efflux protein of the OEP or OMF family | Bacteria |
Proteobacteria | OEP of Myxococcus xanthus |
1.B.17.2.5 | Outer membrane efflux protein | Bacteria |
Firmicutes | Outer membrane efflux protein of Selenomonas sputigena |
1.B.17.2.6 | Outer membrane efflux porin, Oep | Bacteria |
Proteobacteria | Oep of Myxococcus xanthus |
1.B.17.2.7 | Bacteria |
Proteobacteria | Oep of Myxococcus xanthus | |
1.B.17.2.8 | Outer membrane efflux porin (Bhat et al. 2011). | Bacteria |
Proteobacteria | Oep of Myxococcus xanthus |
1.B.17.2.9 | Outer membrane efflux protein, Oep | Bacteria |
Proteobacteria | Oep of Myxococcus xanthus |
1.B.17.2.10 | Putative ABC-type glycolipid export outer membrane factor, HgdD, of 483 aas (Hahn et al., 2012). | Bacteria |
Cyanobacteria | HgdD of Thermosynechococcus sp. NK55a. |
1.B.17.2.11 | Uncharacterized OMF protein of 485 aas and 1 N-terminlal TMS. | Bacteria |
Proteobacteria | UP of Bdellovibrio bacteriovorus |
1.B.17.3.1 | NodT2 outer membrane exporter of lipooligosaccharides | Bacteria |
Proteobacteria | NodT2 of Rhizobium leguminosarum |
1.B.17.3.2 | FusA outer membrane exporter of fusaric acid | Bacteria |
Proteobacteria | FusA of Burkholderia cepacia |
1.B.17.3.3 | OpcM outer membrane exporter of multiple drugs | Bacteria |
Proteobacteria | OpcM of Burkholderia cepacia |
1.B.17.3.4 | SilC outer membrane exporter of silver ion, Ag+ | Bacteria |
Proteobacteria | SilC of Salmonella typhimurium |
1.B.17.3.5 | CusC outer membrane exporter of copper ion, Cu+, and silver ion Ag+. The crystal structure of CusC is known (Lei et al. 2013) providing evidnce concerning the folding mechanism giving rise to the channel. | Bacteria |
Proteobacteria | CusC (YlcB) of E. coli |
1.B.17.3.6 | VceC outer membrane exporter of drugs (Federici et al., 2005) | Bacteria |
Proteobacteria | VceC of Vibrio cholerae (A6XV56) |
1.B.17.3.7 | HI1462 outer membrane, low conductance, anion-selective exporter (selectivity is due to an arginine residue at the tunnel entrance). (Polleichtner and Anderson, 2006) | Bacteria |
Proteobacteria | HI1462 of Haemophilus influenzae (P45217) |
1.B.17.3.8 | Chromosomal NodTch (orthologous to 1.B.17.3.1) (478 aas) required for cell survival (Hernandez-Mendoza et al., 2007). | Bacteria |
Proteobacteria | NodTch of Rhizobium etli (B3PY75) |
1.B.17.3.9 | MdtP (acts with MdtO (TC# 2.A.85.6.1) and MdtN (TC# 8.A.1.1.3)) (Sulavik et al., 2001). | Bacteria |
Proteobacteria | MdtP of E. coli (P32714) |
1.B.17.3.10 | Outer membrane factor of 478 aas, MdtQ (YohG). Involved in resistance to puromycin, acriflavin and tetraphenylarsonium chloride (Sulavik et al. 2001). | Bacteria |
Proteobacteria | MdtQ of E. coli |
1.B.17.3.11 | TolC-like outer membrane factor protein, TdeA of 457 aas, required for leukotoxin and drug export (Crosby and Kachlany 2007). Functions with the MFP, LtxD (TC# 8.A.1.3.4) and the ABC exporter (TC# 3.A.1.109.8). | Bacteria |
Proteobacteria | TdeA of Aggregatibacter (Actinobacillus; Haemophilus) actinomycetemcomitans |
1.B.17.3.12 | The OMR, SilC, of 490 aas. Francisella tularensis, the causative agent of tularemia, contains three paralogs of OMRs, two, termed as TolC and FtlC, are important for tularemia pathogenesis. The third OM protein SilC, is homologous to the silver cation efflux protein of other bacteria. SilC is encoded in an operon encoding an Emr-type multi-drug efflux pump of F. tularensis. A ΔsilC mutant exhibited increased sensitivity towards antibiotics, oxidants and silver as well as diminished intramacrophage growth and attenuated virulence in mice. | Bacteria |
Proteobacteria | SilC of Francisella tularensis |
1.B.17.4.1 | Outer membrane factor of 459 aas. May function with an ABC exporter (A0LKG3/A0LKG4) and a membrane fusion protein (A0LKG1) (based on genomic context). | Bacteria |
Proteobacteria | OMF of Syntrophobacter fumaroxidans |