{"cross_mech":[],"family":{"alphafold_models":1127,"candidate_reasons":["pfam_previous_unknown_name"],"characterization_status":"","context_evidence_count":null,"cross_mech":{"example_proteins":0,"protein_traits_record":false,"records_by_mech":{},"scanned":false},"curation_status":"SEEDED","demotion_reasons":[],"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.","domain_architectures":4,"interpro_id":"IPR010178","known_evidence_count":null,"matches":1709,"name":"Lipoprotein intramolecular transacylase Lit","partial_evidence_count":null,"pfam_id":"PF07314","proteins":1709,"proteomes":1655,"short_name":"Lit","source_url":"https://www.ebi.ac.uk/interpro/api/entry/pfam/PF07314","structures":4,"taxa":2669,"unknown_status":"EX_DUF"},"inputs":{"cross_mech":"cross-mech-duf-examples-2026-10-10","members":"pfam-uniprot-uniref90-2026-10-07","protein_examples":"duf-protein-examples-2026-10-13","worklist":"interpro-pfam-duf-2026-10-10"},"members":[],"metadata":{"curation_status":"SEEDED","local_source":"source/data/families/PF07314.yaml","record":{"characterization_status":"UNSCORED","counters":{"alphafold_models":1127,"domain_architectures":4,"matches":1709,"proteins":1709,"proteomes":1655,"structures":4,"taxa":2669},"curation_status":"SEEDED","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.","id":"Pfam:PF07314","interpro_id":"InterPro:IPR010178","name":"Lipoprotein intramolecular transacylase Lit","pfam_id":"PF07314","provenance":{"generated_at":"2026-10-10T07:44:21.614711Z","path":"data/worklists/interpro-pfam-duf-2026-10-10.json","sha256":"17fb625876c9326ed284263a47bcd84e0d7844a31c040dc06cd2260c36f1c383","snapshot_id":"interpro-pfam-duf-2026-10-10","source_url":"https://www.ebi.ac.uk/interpro/api/entry/pfam/"},"seed_status":"EX_DUF","short_name":"Lit","source_url":"https://www.ebi.ac.uk/interpro/api/entry/pfam/PF07314"},"source":{"commit":"c8155abfcf881ad8662936343deb81e604e3a194","path":"data/families/PF07314.yaml","repository":"https://github.com/CultureBotAI/DUFMech","sha256":"0d9a43e621259333272fcd194d073bc1c51f0c66864c92383f6773bf29c0889d"}},"protein_examples":{"candidate_count":0,"discovery_scanned":true,"example_count":0,"examples":[],"pfam_id":"PF07314","short_name":"Lit","status":"NO_SIBLING_CANDIDATE","unresolved":[]}}
