id: Pfam:PF08353
pfam_id: PF08353
name: MurT ligase C-terminal
short_name: MurT_C
seed_status: EX_DUF
characterization_status: UNSCORED
curation_status: SEEDED
source_url: https://www.ebi.ac.uk/interpro/api/entry/pfam/PF08353
counters:
  proteins: 4479
  matches: 4479
  proteomes: 4418
  taxa: 6081
  structures: 6
  alphafold_models: 2758
  domain_architectures: 6
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:IPR013564
description: This entry represents the C-terminal domain of MurT ligase from Gram-positive bacteria. MurT
  is part of the bi-enzymatic complex MurT-GatD involved in the amidation of the alpha-carboxyl group
  of the D-isoglutamate residue in Lipid II in the peptidoglycan layer to produce D-isoglutamine. This
  domain contains an aspartate at position 349, the third residue in the catalytic triad GatD-C94, GatD-H189,
  MurT-D349. This C-terminal domain is built around a central six-stranded, predominantly parallel beta-sheet
  that is sandwiched between four alpha-helices on one side and two alpha-helices on the other. The MurT-GatD
  heterodimer adopts a boomerang-shaped conformation, with GatD packing against the C-terminal domain
  of MurT [[cite:PUB00094480]].