{"metadata":{"accession":"PF09994","entry_id":null,"type":"domain","go_terms":null,"source_database":"pfam","member_databases":null,"integrated":"IPR018712","hierarchy":null,"name":{"name":"T6SS, Phospholipase effector Tle1-like, catalytic domain","short":"T6SS_Tle1-like_cat"},"description":[{"text":"<p>This domain is found in the type VI secretion system (T6SS) protein Phospholipase effector Tle1 from Pseudomonas aeruginosa ([swissprot:Q9HYV3]), which hydrolyse membrane phospholipids. Tle1 is organised into two distinct parts, the phospholipase catalytic module (this entry) and the putative membrane-anchoring module ([pfam:PF22137]). This domain adopts a compact conformation with a classical mixed alpha/beta-hydrolase fold that shows of seven central parallel beta-sheets and 13 alpha-helices [[cite:PUB00154252]].</p>","llm":false,"checked":false,"updated":false}],"wikipedia":null,"literature":{"PUB00154252":{"PMID":25084336,"ISBN":null,"volume":"70","issue":"Pt 8","year":2014,"title":"Structure of the type VI secretion phospholipase effector Tle1 provides insight into its hydrolysis and membrane targeting.","URL":null,"raw_pages":"2175-85","medline_journal":"Acta Crystallogr D Biol Crystallogr","ISO_journal":"Acta Crystallogr D Biol Crystallogr","authors":["Hu H","Zhang H","Gao Z","Wang D","Liu G","Xu J","Lan K","Dong Y."],"DOI_URL":"https://doi.org/10.1107/S1399004714012899"}},"set_info":{"accession":"CL0028","name":"AB_hydrolase"},"overlaps_with":null,"counters":{"subfamilies":0,"domain_architectures":286,"interactions":0,"matches":13510,"pathways":0,"proteins":12473,"proteomes":4775,"sets":1,"structural_models":{"alphafold":9172},"structures":4,"taxa":7945},"entry_annotations":{"hmm":0,"logo":0,"alignment:seed":279,"alignment:full":8862},"cross_references":{},"is_llm":false,"is_reviewed_llm":false,"is_updated_llm":false,"representative_structure":null}}