v5.1.0.3
Cicer data from the Legume Information System
| Type | Homologous_superfamily |
| Description | 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 [ ]. The chaperone-binding domain of SipA consists of a globular domain, represented by this entry, and an adjacent nonglobular polypeptide [ ]. 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. |
| Short Name | SipA_chaperone-bd |