id: Pfam:PF09199
pfam_id: PF09199
name: Staphylococcal superantigen-like OB-fold domain
short_name: SSL_OB
seed_status: EX_DUF
characterization_status: UNSCORED
curation_status: SEEDED
source_url: https://www.ebi.ac.uk/interpro/api/entry/pfam/PF09199
counters:
  proteins: 88
  matches: 88
  proteomes: 15
  taxa: 31
  structures: 31
  alphafold_models: 76
  domain_architectures: 2
provenance:
  snapshot_id: interpro-pfam-duf-2026-10-10
  path: data/worklists/interpro-pfam-duf-2026-10-10.json
  sha256: 17fb625876c9326ed284263a47bcd84e0d7844a31c040dc06cd2260c36f1c383
  generated_at: '2026-10-10T07:44:21.614711Z'
  source_url: https://www.ebi.ac.uk/interpro/api/entry/pfam/
interpro_id: InterPro:IPR015282
description: This OB-fold domain folds into a five-stranded beta-barrel [[cite:PUB00018994]]. Members
  of this family 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, [pfam:PF02876]. 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 2,3,4,5,6,7,8]. 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 FcalphaR [[cite:PUB00065773]].