id: Pfam:PF10093
pfam_id: PF10093
name: Elongation-Factor P (EF-P) rhamnosyltransferase EarP
short_name: EarP
seed_status: EX_DUF
characterization_status: UNSCORED
curation_status: SEEDED
source_url: https://www.ebi.ac.uk/interpro/api/entry/pfam/PF10093
counters:
  proteins: 1864
  matches: 1898
  proteomes: 1846
  taxa: 2406
  structures: 12
  alphafold_models: 1101
  domain_architectures: 4
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:IPR016633
description: This entry includes family members such as EarP enzymes which are essential for post-translational
  activation of elongation factor P(EF-P). It was identified as EF-P arginine R32 specific rhamnosyl transferase
  in Shewanella oneidensis using dTDP-beta-L-rhamnose as donor substrate [[cite:PUB00091040]]. This was
  further confirmed for Pseudomonas aeruginosa [[cite:PUB00091041]], Pseudomonas putida [[cite:PUB00091042]]
  and Neisseria meningitidis [[cite:PUB00091043]]. As for S. oneidensis [[cite:PUB00091044]] and P. aeruginosa
  [[cite:PUB00091045]], EarP enzyme acts as an inverting glycosyltransferase, thus mediating the formation
  of an alpha-L-rhamnosidic linkage. Structural analysis show that EarP is composed of two opposing domains
  with Rossmann folds, thus constituting a B pattern-type glycosyltransferase (GT-B) and provide basis
  for arginine glycosylation by EarP [[cite:PUB00091042]]. Mutational analysis of efp and earP genes,
  resulted in a substantial decrease in the production of rhamnolipids and pyocyanin (important factors
  for colonization and invasion during infection) of P. aeruginosa. Collectively this indicates that EarP
  and EF-P are essential for P. aeruginosa pathogenicity [[cite:PUB00091040]].The protein family is also
  annotated in the CaZy Database as GT104.