| TCID | Name | Domain | Kingdom/Phylum | Protein(s) |
|---|---|---|---|---|
|
1.B.22.1.1 | PulD protein secretin. Involved in protein secretion via the Type II MTB system (TC# 3.A.15). PulD allows the efflux of small fluorescent molecules with a permeation cutoff similar to that of general porins and is constitutively open (Disconzi et al. 2014). | Bacteria |
Proteobacteria | PulD of Klebsiella oxytoca |
|
1.B.22.1.2 | XcpQ secretin protein | Bacteria |
Proteobacteria | XcpQ of Pseudomonas aeruginosa |
|
1.B.22.1.3 | The dodecameric secretin, GspD of 650 aas. The 3-d structure is known (PDB 5WQ8) (Korotkov et al. 2013). It reveals a double β-barrel channel with about 60 β-strands in each barrel (Yan et al. 2017). | Bacteria |
Proteobacteria | GspD of E. coli |
|
1.B.22.2.1 | PilQ fimbrial subunit secretin | Bacteria |
Proteobacteria | PilQ of Pseudomonas aeruginosa |
|
1.B.22.2.2 | The Type IV pilus biogenesis/competence secretin precursor, PilQ (may serve as a pore for (1) pilus export, (2) DNA uptake, (3) heme uptake, (4) antimicrobial uptake (Tønjum et al., 1998); Binds DNA (Assalkhou et al., 2007); Structure known to 12 Å resolution (Collins et al., 2004) The pilus biogenesis factor, PilW (ABX73034) facilitates formation and/or stability of secretin (PilQ) multimers. The 3-D structure of PilW is known (Trindade et al., 2008). | Bacteria |
Proteobacteria | PilQ of Neisseria meningitidis (Q9ZHF3) |
|
1.B.22.2.3 | Fimbrial usher, HofQ of 760 aas | Bacteria |
Chlamydiae/Verrucomicrobia group | HofQ of Chlamydia trachomatis |
|
1.B.22.2.4 | The secretin, PilQ (SglA) of 901 aas, required for pilus biogenesis, social motility and development of fruiting bodies (Wall et al. 1999). | Bacteria |
Proteobacteria | PilQ of Myxococcus xanthus |
|
1.B.22.3.1 | HrpH hypersensitivity response secretin | Bacteria |
Proteobacteria | HrpH of Pseudomonas syringae |
|
1.B.22.3.2 | InvG invasion protein secretin | Bacteria |
Proteobacteria | InvG of Salmonella typhimurium |
|
1.B.22.3.3 | YscC secretin | Bacteria |
Proteobacteria | YscC of Yersinia enterocolitica |
|
1.B.22.4.1 | ComE competence protein secretin | Bacteria |
Proteobacteria | ComE of Haemophilus influenzae |
|
1.B.22.4.2 | HofQ, may facilitate double stranded DNA uptake in E. coli (Sun et al., 2009). | Bacteria |
Proteobacteria | HofQ of E. coli (Q1R5P6) |
|
1.B.22.4.3 | HofQ competence protein, the outer membrane DNA translocase (Tarry et al., 2011). The 2.3Å structures of the extramembraneous domains are known (Tarry et al., 2011). | Bacteria |
Proteobacteria | HofQ of Aggregatibacter actinomycetemcomitans (C6ALC5) |
|
1.B.22.4.4 | DNA uptake porin, HofQ, of 428 aas and 1 N-terminal TMS and 36 beta strands, is required for the use of extracellular DNA as a nutrient. | Bacteria |
Proteobacteria | HofQ of Klebsiella pneumoniae |
|
1.B.22.4.5 | Outer membrane porin of 382 aas and 1 or 2 N-terminal TMSs. | Bacteria |
Firmicutes | OMP of Megasphaera sp. |
|
1.B.22.5.1 | Gene IV protein secretin | Viruses |
Inoviridae | Gene IV protein of bacteriophage f1 |
|
1.B.22.5.2 | Putative pilus assembly transmembrane protein of 509 aas, PilQ. | Bacteria |
Proteobacteria | PilQ of Bdellovibrio bacteriovorus |
|
1.B.22.6.1 | NolW secretin | Bacteria |
Proteobacteria | NolW of Rhizobium spp. |
|
1.B.22.7.1 | Bundle-forming pilus-B (BfpB) secretin (catalyzes export of pilins and EPEC proteins; uptake of vancomycin). (BfpB complex formation requires BfpG, 113 aas; gbBAA84839). While the N-terminus is periplasmic, the C-terminus is extracelllular. BfpB may form a beta barrel with 16 transmembrane beta strands with a C-terminal segment passing through the center of each monomer (Lieberman et al. 2015). | Bacteria |
Proteobacteria | BfpB of enteropathogenic E. coli |