id: Pfam:PF06251
pfam_id: PF06251
name: Capsule biosynthesis GfcC C-terminal
short_name: Caps_syn_GfcC_C
seed_status: EX_DUF
characterization_status: UNSCORED
curation_status: SEEDED
source_url: https://www.ebi.ac.uk/interpro/api/entry/pfam/PF06251
counters:
  proteins: 940
  matches: 941
  proteomes: 900
  taxa: 1356
  structures: 1
  alphafold_models: 549
  domain_architectures: 25
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:IPR010425
description: Many bacteria are covered in a layer of surface-associated polysaccharide called the capsule.
  These capsules can be divided into four groups depending upon the organisation of genes responsible
  for capsule assembly, the assembly pathway and regulation [[cite:PUB00062058]]. This family plays a
  role in group 4 capsule biosynthesis [[cite:PUB00066719]]. These proteins have a beta-grasp fold [[cite:PUB00044948]].
  Two beta-grasp domains, D2 and D3, are arranged in tandem. There is a C-terminal amphipathic helix which
  packs against D3. A helical hairpin insert in D2 binds to D3 and constrains its position, a conserved
  arginine residue at the end of this hairpin is essential for structural integrity [[cite:PUB00099551]].
  This is the C-terminal domain which covers D3 and D4 domains [[cite:PUB00099551]].