id: Pfam:PF05618
pfam_id: PF05618
name: Retropepsin-like aspartic endopeptidase RimB
short_name: RimB-like
seed_status: EX_DUF
characterization_status: UNSCORED
curation_status: SEEDED
source_url: https://www.ebi.ac.uk/interpro/api/entry/pfam/PF05618
counters:
  proteins: 7079
  matches: 7218
  proteomes: 4665
  taxa: 6703
  structures: 3
  alphafold_models: 4590
  domain_architectures: 9
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:IPR008503
description: This entry represents a domain found in retropepsin-like bacterial proteases such as RimB
  from Pseudomonas fluorescens and the related retropepsin-like osmotic stress tolerance peptidases (Rlo)
  from Pseudomonas aeruginosa [[cite:PUB00161732],[cite:PUB00161733]]. RimB is involved in rhizosphere
  colonisation and plant infection. It is a bifunctional retropepsin-like aspartic endopeptidase that
  uniquely recognises and removes glutamate residues from polyglutamated RpsF and stimulates poly-alpha-L-glutamate
  synthesis by RimK. While Rlo proteases are homologous to RimB, they contain N-terminal signal peptides
  and perform distinct biological functions. Mutants lacking all three secreted Rlo peptidases show defects
  in antibiotic resistance, biofilm formation, and cell morphology. Rlo peptidases have been structurally
  characterised, showing structural features characteristic of retroviral pepsins (PDB:9G59, PDB:9G58)
  [[cite:PUB00161733]]. Similar to RimB, RloA proteins cleave substrates that become polyglutamated post-translationally.