id: Pfam:PF03961
pfam_id: PF03961
name: Flagellar Assembly Protein A beta solenoid domain
short_name: FapA
seed_status: EX_DUF
characterization_status: UNSCORED
curation_status: SEEDED
source_url: https://www.ebi.ac.uk/interpro/api/entry/pfam/PF03961
counters:
  proteins: 3264
  matches: 3325
  proteomes: 2432
  taxa: 3856
  structures: 0
  alphafold_models: 2229
  domain_architectures: 17
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:IPR046865
description: This entry represents the C-terminal beta solenoid domain of FapA and its homologues. Members
  of this family include FapA (flagellar assembly protein A) [swissprot:Q7MBR0] found in Vibrio vulnificus.
  The synthesis of flagella allows bacteria to respond to chemotaxis by facilitating motility. Studies
  examining the role of FapA show that the loss or delocalization of FapA results in a complete failure
  of the flagellar biosynthesis and motility in response to glucose mediated chemotaxis. The polar localization
  of FapA is required for flagellar synthesis, and dephosphorylated EIIAGlc (Glucose-permease IIA component)
  inhibited the polar localization of FapA through direct interaction [[cite:PUB00085059]]. This entry
  shows similarity to [pfam:PF03775] suggesting a similar functional role.