id: Pfam:PF08842
pfam_id: PF08842
name: Fimbrillin-A associated anchor proteins Mfa1 and Mfa2
short_name: Mfa2
seed_status: EX_DUF
characterization_status: UNSCORED
curation_status: SEEDED
source_url: https://www.ebi.ac.uk/interpro/api/entry/pfam/PF08842
counters:
  proteins: 835
  matches: 835
  proteomes: 217
  taxa: 389
  structures: 5
  alphafold_models: 553
  domain_architectures: 8
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:IPR014941
description: This family of proteins may be lipoproteins principally from bacilli. They are between 300
  and 400 residues. Many Bacteroides-like bacterial species, including Porphyromonas gingivalis, the causal
  agent of periodontal infection, carry at least two types of fimbriae, namely FimA and Mfa1 fimbriae,
  following the names of their major subunit proteins [[cite:PUB00055567]]. Normally, FimA fimbriae are
  long filaments that are easily detached from cells, whereas Mfa1 fimbriae are short filaments that are
  tightly bound to cells; however, in the absence of Mfa2 protein, the Mfa1 fimbriae are also very long
  and are not attached. Mfa2 and Mfa1 are associated with each other in whole P. gingivalis cells to the
  extent that Mfa2 is located on the cell surface and probably associated with Mfa1 fimbriae in such a
  way that it anchors the Mfa1 fimbriae to the cell surface and regulates Mfa1 filament length [[cite:PUB00055568]].