Homologous Superfamily

Salmonella invasion protein A, chaperone-binding (IPR023225)

Short name: SipA_chaperone-bd

Overlapping entries


Salmonella invasion protein A (SipA) is a virulence factor that is translocated into host cells by a type III secretion system. In the host cell it binds to actin, stimulates actin polymerisation and counteracts F-actin destabilising proteins. This contributes towards cytoskeletal rearrangements that allow the entry of the pathogen into the host cell [PMID: 11331579].

The chaperone-binding domain of SipA consists of a globular domain, represented by this entry, and an adjacent nonglobular polypeptide [PMID: 16507363]. Both of these elements are necessary for chaperone binding to occur. The globular domain is composed of eigth alpha helices arranged so that six amphipathic helices surround a predominantly hydrophobic helix in the middle.

Contributing signatures

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