TCDB is operated by the Saier Lab Bioinformatics Group
TCIDNameDomainKingdom/PhylumProtein(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 (Korotkov et al. 2013).

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.22.5.1









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