id: Pfam:PF10090
pfam_id: PF10090
name: Histidine phosphotransferase C-terminal domain
short_name: HPTransfase
seed_status: EX_DUF
characterization_status: UNSCORED
curation_status: SEEDED
source_url: https://www.ebi.ac.uk/interpro/api/entry/pfam/PF10090
counters:
  proteins: 2320
  matches: 2320
  proteomes: 2317
  taxa: 3145
  structures: 4
  alphafold_models: 1567
  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:IPR018762
description: 'HPTransfase is a family of essential histidine phosphotransferases. It controls the activity
  of the master bacterial cell-cycle regulator CtrA through phosphorylation. It behaves as a homodimer
  by adopting the domain architecture of the intracellular part of class I histidine kinases. Each subunit
  consists of two distinct domains: an N-terminal helical hairpin domain and a C-terminal [alpha]/[beta]
  domain. The two N-terminal domains are adjacent within the dimer, forming a four-helix bundle. The C-terminal
  domain adopts an atypical Bergerat ATP-binding fold [[cite:PUB00075663]].'