id: Pfam:PF11860
pfam_id: PF11860
name: N-acetylmuramidase
short_name: Muramidase
seed_status: EX_DUF
characterization_status: UNSCORED
curation_status: SEEDED
source_url: https://www.ebi.ac.uk/interpro/api/entry/pfam/PF11860
counters:
  proteins: 1485
  matches: 1492
  proteomes: 1311
  taxa: 2361
  structures: 4
  alphafold_models: 794
  domain_architectures: 24
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:IPR024408
description: Endolysins are bacteriophage encoded proteins synthesized at the end of the lytic infection
  cycle. They degrade the peptidoglycan (PG) of the host bacterium to allow viral progeny release. This
  domain family is found in bacteria and viruses. It is also found associated with [pfam:PF01471]. One
  of the family members is the modular Gp110 endolysin found in the Salmonella phage. This domain represents
  the catalytic region found in the C-terminal of Gp110. It has been demonstrated to have N-acetylmuramidase
  (lysozyme) activity cleaving the beta-(1,4) glycosidic bond between N-acetylmuramic acid and N-acetylglucosamine
  residues in the sugar backbone of the PG. Furthermore, sequence alignments containing this domain show
  that the Gp110 E101 residue is conserved (suggesting that is is the catalytic residue), and followed
  by serine (a common feature in lysozymes). The structure of endolysins varies depending on their origin.
  In general, most of the endolysins from phages infecting Gram-positive bacteria have a modular structure
  consisting of one or two N-terminal enzymatic active domains (EADs) and a C-terminal cell wall binding
  domain (CBD) separated by a short linker. In silico analysis indicate that this endolysin has a modular
  structure harboring this EAD family at the C terminus and a PG_binding_1 CBD at the N terminus [[cite:PUB00081896]].