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









Type III protein secretion complex. Assembly of the YscR,S,T,U,V complex occurs independently of other structural components and involves the formation of a YscV oligomer (Diepold et al., 2011). A C-terminal region of Yersinia pestis YscD binds the outer membrane secretin YscC (Ross and Plano, 2011). YopBD-mediated translocation of T3SS cargo, but not YopBD pore formation, leads to activation of host pathways influencing inflammation, cell death, and response to stress (Kwuan et al. 2013).

Bacteria
Proteobacteria
Type IIISP system of Yersinia enterocolitica species (22 subunits) LcrD + YscA - R:
LcrD - P0C2V3
YscA - A1JU92
YscB - A1JU93
YscC - Q93KT1
YscD - Q93KT0
YscE - Q93KS9
YscF - Q93KS8
YscG - Q93KS7
YscH - Q93KS6
YscI - Q93KS5
YscJ - Q7BFA4
YscK - Q93KS4
YscL - Q93KS3
YscM - A1JUA4
YscN - P40290
YscO - Q93KT7
YscP - Q93KT6
YscQ - Q9ZA78
YscR - Q9ZA77
YscS - Q7BFA7
YscT - Q93KT5
YscU - Q93KT4
*3.A.6.1.2









Type III secretion system, SpaLMNOPQRS.  Required for surface presentation of invasion plasmid antigens. Required for invasion and for secretion of the three IPA proteins.

Bacteria
Proteobacteria
Type III secretion system of Shigella flexneri
*3.A.6.1.3









Type III secretion system, SpaLMNOPQRS-PrgHIJK.  SpaP forms a pentameric 15 Å wide pore.  It interacts with SpaQ, R and S as well as the inner rod protein, PrgJ (Dietsche et al. 2016). The small hydrophobic export apparatus components, SpaP and SpaR, nucleate assembly of the needle complex and form the central "cup" substructure of this secretion system.

Bacteria
Proteobacteria
Type III secretion system, SpaLMNOPQRS-PrgHIJK of Samonella enterica Typhimurium
SpaL, ATPase also called InvC or SpaI; 431 aas
SpaM, 147 aas
SpaN, 336 aas (also called InvJ
SpaO, 303 aas, 0 TMSs
SpaP, 224 aas
SpaQ, 86 aas, 2 TMSs
SpaR, 263 aas, 6 TMSs
SpaS, 256 aas, 6 TMSs
PrgI, 80 aas
PrgJ, 101 aas, inner rod protein
PrgK, 252 aas, lipoprotein
*3.A.6.2.1









Flagellar protein export system.  Infrequent ATP hydrolysis by the FliI6FliJ ring is sufficient for gate activation, allowing processive translocation of export flagellar protein substrates for efficient flagellar assembly (Minamino et al. 2014). FliO have been identified as a flagellar basal body chaparone protein (Fabiani et al. 2017).

Bacteria
Proteobacteria
Flagellar subunit export system of Salmonella typhimurium (10 subunits)
*3.A.6.3.1









Chlamydial type III secretion complex, CdsCDJLNQRSTUV, FliF, FliI, FlhA (Peters et al., 2007).  Genome analyses have indicated which proteins are substrates (Dehoux et al. 2011).

Bacteria
Chlamydiae/Verrucomicrobia group
Type III SP of Chlamydia trachomatis:
CdsC - O84681
CdsD - O84671
CdsJ - O84563
CdsL - O84565
CdsN - O84676
CdsQ - O84679
CdsR - O84566
CdsS - O84567
CdsT - O84568
CdsU - O84093
DsdV - O84092
FliF - O84724
FliI - O84722
FlhA - O84063