| Primary Identifier | IPR012927 | Type | Domain |
| Short Name | Toxin_15_N |
| description | This domain is present in the N-terminal region of the ShET2 enterotoxin produced by Shigella flexneri () and Escherichia coli (). 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 []. The toxin is injected into the host cell by the type III secretion system [].Most proteins containing this domain are annotated as putative enterotoxins, but one member () is a regulator of acetyl CoA synthetase, and another two members (and ) are annotated as ankyrin-like regulatory proteins and contain Ank repeats (). |
