id: Pfam:PF07314
pfam_id: PF07314
name: Lipoprotein intramolecular transacylase Lit
short_name: Lit
seed_status: EX_DUF
characterization_status: UNSCORED
curation_status: SEEDED
source_url: https://www.ebi.ac.uk/interpro/api/entry/pfam/PF07314
counters:
  proteins: 1709
  matches: 1709
  proteomes: 1655
  taxa: 2669
  structures: 4
  alphafold_models: 1127
  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:IPR010178
description: This entry represents the lipoprotein intramolecular transacylase, Lit [[cite:PUB00158976],[cite:PUB00158977]].
  Lit creates a lipoprotein that is less immunogenic, possibly enabling the bacteria to gain a foothold
  in the host by stealth. The crystal structure of the Lit enzyme from Bacillus cereus ([swissprot:Q813T3])
  revealed that it consists of consists of four transmembrane helices with an extracellular cap [[cite:PUB00158977]].
  The conserved residues map to the cap-membrane interface and they include two catalytic histidines that
  function to effect unimolecular transacylation. The reaction involves acyl transfer from the sn-2 position
  of the glyceryl moiety to the amino group on the N-terminal cysteine of the substrate via an 8-membered
  ring intermediate.