TCDB is operated by the Saier Lab Bioinformatics Group
TCIDNameDomainKingdom/PhylumProtein(s)
1.C.107.1.1









Insecticidal toxin complex (TC) component, TcaA (1095 aas) (may mediate toxin-C internalization)(Landsberg et al., 2011).  The TcdA1 prepore assembles as a pentamer forming an α-helical, vuvuzela-shaped channel less than 1.5 nanometres in diameter surrounded by a large outer shell (Gatsogiannis et al. 2013). Membrane insertion is triggered not only at low pH as expected, but also at high pH, explaining Tc action directly through the midgut of insects. Comparisons with structures of the TcdA1 pore inserted into a membrane and in complex with TcdB2 and TccC3 reveal large conformational changes during membrane insertion, suggesting a novel syringe-like mechanism of protein translocation (Gatsogiannis et al. 2013).  P. luminescens is a nematode symbiont and an insect pathogen.  The toxin, TcC, of the tripartite toxin complex, is an ADP ribosyl transferase causing actin clustering, defects in phagocytosis and cell dealth.

Bacteria
Proteobacteria
TcaA of Photorhabdus luminescens (Q66PW7)
1.C.107.1.2









Insecticidal toxin complex (TC) component, XptA1 or TccA (1156 aas) (may mediate toxin-C internalization) (Landsberg et al., 2011).

Bacteria
Proteobacteria
XptA1 of Xenorhabdus nematophila (D3VHH3)
1.C.107.1.3









Insecticidal toxin complex (TC) component, Yen-Tc (may mediate toxin-C internalization) (Landsberg et al., 2011).

Bacteria
Proteobacteria
Yen-Tc of Yersinia enterocolitica (Q693A5)
1.C.107.1.4









The trimeric Tc toxin complex consisting of three subunits, TcdA, TcdB and TccC (TcA, B and C, respectively) of 2525, 1476 and 1043 aas, respectively. Several 3-d structures and their modes of action and secretion have been described (see the family description) (Gatsogiannis et al. 2013; Yang and Waterfield 2013; Moriya et al. 2017).

Bacteria
Proteobacteria
Tc toxin complex of Photorhabdus luminescens
TcdA, 2525 aas
TcdB, 1476 aas
TccC, 1043 aas
1.C.107.1.5









Pore-forming component, SepA of the tripartite toxin, SepA (Q9F9Z3; 2376 aas)/SepB (Q9F9Z2; 1428 aas)/SepC (Q9F9Z0; 973 aas), that causes amber disease in the grass grub, Costelytra zealandica (Hurst et al. 2000).

Bacteria
Proteobacteria
SepA of Serratia entomophila