id: Pfam:PF03777
pfam_id: PF03777
name: ChpA-C
short_name: ChpA-C
seed_status: EX_DUF
characterization_status: UNSCORED
curation_status: SEEDED
source_url: https://www.ebi.ac.uk/interpro/api/entry/pfam/PF03777
counters:
  proteins: 6476
  matches: 9507
  proteomes: 1356
  taxa: 1624
  structures: 0
  alphafold_models: 2903
  domain_architectures: 23
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:IPR005528
description: Small domain found in a family of secreted streptomyces proteins. It occurs singly or as
  a pair. Many of the domains have two cysteines that may form a disulphide bridge. This domain is found
  in chaplins ChpA-C (coelicolor hydrophobic aerial) proteins. ChpA-C contain a canonical C-terminal sortase
  signal, which is recognized by sortase enzymes that covalently couple their substrates to the peptidoglycan
  present in the cell wall. Indeed, direct evidence for sortase-mediated coupling of ChpC has been demonstrated,
  and it is expected that ChpA and ChpB are also anchored to the cell wall [[cite:PUB00091046]].