TCID | Name | Domain | Kingdom/Phylum | Protein(s) |
---|---|---|---|---|
1.C.72.1.1 | Pertussis toxin | Bacteria |
Pseudomonadota | Pertussis toxin of Bordetella pertussis A (S1) + B (S2-S5) Subunit S1 (P04977) Subunit S2 (P04978) Subunit S3 (P04979) Subunit S4 (P0A3R5) Subunit S5 (P04981) |
1.C.72.2.1 | The ADP-ribosyltransferase toxin, ArtAB (Saitoh et al., 2005) (ArtA but not ArtB is demonsratively homologous to subunits in pertussis toxin) | Bacteria |
Pseudomonadota | ArtAB of Salmonella enterica serovar Typhimurium ArtA (Q404H4) ArbB (Q404H3) |
1.C.72.3.1 | The Subtilase cytotoxin, SubAB. Pentameric SubB, but not SubA, is homologous to ArtB of Salmonella enterica. SubA (AB5 subtilase) cytotoxin inactivates the endoplasmic reticulum chaperone, BiP (Paton et al., 2006; Beddoe et al., 2010). | Bacteria |
Pseudomonadota | Subtilase cytotoxin AB (SubAB) of E. coli Subtilase A (Q3ZTX7) Subtilase B (Q3ZTX8) |
1.C.72.4.1 | Heat labile enterotoxin AB, EltAB, ItpAB, ToxAB, LT-AB, cholera toxin (258 aas and 124 aas, respectively). The biological activity of the toxin is produced by the A chain, which activates intracellular adenyl cyclase. The A2 domain of LTA has cell penitration function (Liu et al. 2016). LT holotoxin can enter intestinal epithelial cells and cause diarrhea. The A2 domain might be useful as a transport vehicle for other proteins (Liu et al. 2016). A biotinylated cholera toxin becomes a fusogenic lectin upon cross-linking with streptavidin. This reengineered protein brings about hemifusion and fusion of vesicles as demonstrated by mixing of fluorescently labeled lipids between vesicles as well as content mixing of liposomes filled with fluorescently labeled dextran (Wehrum et al. 2022). | Bacteria |
Pseudomonadota | EltAB of E. coli 078:H11 |
1.C.72.4.2 | Heat labile enterotoxin IIB, A (α)-chain of 685 aas/B chain of | Bacteria |
Spirochaetota | Enterotoxin of Leptospira borgpetersenii |