ShET2 enterotoxin, N-terminal (IPR012927)

Short name: Toxin_15_N

Overlapping homologous superfamilies


Domain relationships



This domain is present in the N-terminal region of the ShET2 enterotoxin produced by Shigella flexneri (Q47635) and Escherichia coli (Q47634). This protein was found to confer toxigenicity in Ussing chamber assays, and the N-terminal region was found to be important for its enterotoxic effect. The N-terminal domain is a cysteine-type peptidase with a Cys/His/Asp catalytic triad that cleaves within the receptor-interacting protein homotypic interaction motifs found within host adaptor proteins such as receptor-interacting serine/threonine protein kinases RIPK1 and RIPK3, TIR-domain-containing adapter-inducing interferon beta and Z-DNA-binding protein 1, inactivating them and thus inhibiting necroptosis and inflammatory signalling [PMID: 28085133]. The toxin is injected into the host cell by the type III secretion system [PMID: 28085133].

Most proteins containing this domain are annotated as putative enterotoxins, but one member (Q8X606) is a regulator of acetyl CoA synthetase, and another two members (P76205 and P23325) are annotated as ankyrin-like regulatory proteins and contain Ank repeats (IPR002110).

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.