id: Pfam:PF14092
pfam_id: PF14092
name: BamH
short_name: BamH
seed_status: EX_DUF
characterization_status: UNSCORED
curation_status: SEEDED
source_url: https://www.ebi.ac.uk/interpro/api/entry/pfam/PF14092
counters:
  proteins: 2444
  matches: 2444
  proteomes: 2014
  taxa: 2671
  structures: 4
  alphafold_models: 1580
  domain_architectures: 1
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:IPR025366
description: This entry, previously known as DUF4270, represents BamH subunit of the beta-barrel-assembly
  machinery so-called BAM. BamH along with BamG are involved in forming the extracellular canopy and are
  both required for BAM function. They are conserved across the Bacteroidota, suggesting that they form
  an essential extension to the canonical BAM core in this phylum. BamH interacts with BamM to form a
  long canopy structure on the extracellular side of the outer membrane that extends from the rear of
  BamA across the BamA barrel [[cite:PUB00163537]]. BamH consists of two homologous beta-sandwich domains
  with a Nucleoplasmin-like jelly roll topology. One of the domains is inserted into the other resulting
  in a circular permutation. The N-terminal strand of one of the domains occupies the position of the
  C-terminal strand of the other.