Staphylococcal superantigen-like OB-fold domain (IPR015282)

Short name: SSL_OB

Overlapping homologous superfamilies

Domain relationships



This OB-fold domain folds into a five-stranded beta-barrel [PMID: 12082105]. Proteins containing this domain are found in various staphylococcal toxins described as staphylococcal superantigen-like (SSL) proteins that are related to the staphylococcal enterotoxins (SEs) or superantigens. These SSL proteins of which 11 have so far been characterised have a typical SE tertiary structure consisting of a distinct oligonucleotide/oligosaccharide binding (OB-fold), this domain, linked to a beta-grasp domain, family Stap_Strp_tox_C (IPR006123 ). SSLs do not bind to T-cell receptors or major histocompatibility complex class II molecules and do not stimulate T cells. SSLs target components of innate immunity, such as complement, Fc receptors, and myeloid cells [PMID: 15213171, PMID: 17848512, PMID: 17996251, PMID: 18045383, PMID: 20133685, PMID: 2121764, PMID: 22949551]. SSL protein 7 (SSL7) is the best characterised of the SSLs and binds complement factor C5 and IgA with high affinity and inhibits the end stage of complement activation and IgA binding to FcgammaR [PMID: 22949551].

Contributing signatures

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