TCDB is operated by the Saier Lab Bioinformatics Group
TCIDNameDomainKingdom/PhylumProtein(s)
*1.C.36.1.1









IIITCP protein complex EspB/EspD. The topology of and EspD interaction sites in EspB have been defined (Luo and Donnenberg, 2011).  EspD inserts into the membrane with its two helical hairpins traversing the membrane with the N- and C-termini on the extraluminal surface, forming 2.5 diameter pores (Chatterjee et al. 2015).

Bacteria
Proteobacteria
EspB/EspD of E. coli
EspB (NP_290254)
EspD (NP_290255)
*1.C.36.2.1









IIITCP protein complex, YopB/YopD (Olsson et al., 2004). Forms a multimeric integral membrane complex (Montagner et al., 2011).  Mutants have been isoated which show defects in effector translocation and pore formation, and many of these are in a C-terminal domain (Solomon et al. 2015).

Bacteria
Proteobacteria
YopB/YopD of Yersinia pseudotuberculosis
YopB (Q06114)
YopD (Q06131)
*1.C.36.2.2









IIITCP protein complex, PopB/PopD. Purified PopB and PopD form pores in model membranes (Romano et al., 2011).  PopB in isolation forms a biimodal distribution of two complexes with 6 and 12 subunits while PopD forms a hexameric complex.  However when present together, the form a hexadecameric transmembrane complex (Romano et al. 2016).

Bacteria
Proteobacteria
PopB/PopD of Pseudomonas aeruginosa
PopB (AAO91773)
PopD (AAO91774)
*1.C.36.2.3









Translocator complex AopB/AopD of 347 and 299 aas, respectively.  AopB has been crystalized and the structure determined for this protein in complex with the AcrH chaperone protein (Nguyen et al. 2015). The structure revealed unique interactions between the various interfaces of AopB and AcrH, with the N-terminal "molecular anchor" of AopB crossing into the "N-terminal arm" of AcrH. AopB adopts a novel fold, and its transmembrane regions form two pairs of helical hairpins.

Bacteria
Proteobacteria
AopBD of Aeromonas hydrophila
*1.C.36.3.1









IIITCP protein complex, IpaB/IpaC/IpaD. Physical contact with host cells initiates secretion and leads to assembly of a pore, IpaB/IpaC, in the host cell membrane. The active needle tip complex of S. flexneri is composed of a tip protein, IpaD, and the two pore-forming proteins, IpaB and IpaC. The atomic structures of IpaD and a protease-stable coiled-coil fragment in the N-terminal regions of IpaB from S. flexneri and the homologous SipB from Salmonella enterica have been determined (Barta et al. 2012).  Structural comparisons revealed similarity to the coiled-coil regions of pore-forming proteins such as colicin Ia (TC# 1.C.1.1.1).  Interaction between IpaB and IpaD at the needle tip is key to host cell sensing, orchestration of IpaC secretion and its subsequent assembly at needle tips (Veenendaal et al. 2007).

Bacteria
Proteobacteria
IpaB/IpaD of Shigella dysenteriae
IpaB (P18011)
IpaD (P18013)
IpaC (P18012)
*1.C.36.3.2









IIITCP protein complex, SipB/SipD of pathogenicity island 1 (SPI1)
Bacteria
Proteobacteria
SipB/SipD of Salmonella typhimurium
SipB (AAL21765)
SipD (AAL21763)
*1.C.36.3.3









IIITCP complex, BipB/BipD (BipB, 620aas; BipD, 310aas)

Bacteria
Proteobacteria
BipB/BipD of Burkholderia pseudomallei
BipB (Q3JL23)
BipD (Q3JL26)
*1.C.36.3.4









IIITCP complex, BipB/BipD (Cell invasion protein complex).

Bacteria
Proteobacteria
BipB/D of Protens mirablis
BipB (B4EYC8)
BipD (B4EYC6)
*1.C.36.3.5









IIITCP complex protein, CopB of 852aas; 4TMSs

Bacteria
Chlamydiae/Verrucomicrobia group
CopB of Parachlamydia acathamoebae (F8KWQ0)
*1.C.36.4.1









IIITCP protein complex, BopB/BopD (Nogawa et al., 2004)
Bacteria
Proteobacteria
BopB/BopD of Bordetella bronchiseptica
BopB (NP_888166)
BopD (NP_888165)
*1.C.36.5.1









IIICP protein complex SseB/SseC/SseD; SseB: translocon sheath protein; SseC and SseD: translocon pore subunits of the Salmonella pathogenicity island 2 (SPI2)

Bacteria
Proteobacteria
SseB/SseC/SseD of Salmonella typhimurium
SseB (CAA12185)
SseC (CAA12187)
SseD (CAA12188)
*1.C.36.6.1









EspA/D

Bacteria
Proteobacteria
EspA/D of E. coli O157:H7