{"metadata":{"accession":"PF24574","entry_id":null,"type":"domain","go_terms":null,"source_database":"pfam","member_databases":null,"integrated":"IPR056025","hierarchy":null,"name":{"name":"ACP-like domain","short":"Nm-ACP"},"description":[{"text":"<p>This domain, previously known as DUF7606, is found in Neisseria Adhesin Complex Protein (ACP) and in a group of uncharacterised sequences from proteobacteria. It folds into an eight-stranded beta-barrel, stabilised by a disulphide bond between the first and last beta-strands [[cite:PUB00147614]]. Nm-ACP is structurally similar to members of the MliC/PliC protein family of lysozyme inhibitors. Despite it does not share any conserved MliC/PliC sequence motifs associated with lysozyme recognition, ACP is capable of inhibiting lysozyme.</p>","llm":false,"checked":false,"updated":false}],"wikipedia":null,"literature":{"PUB00147614":{"PMID":28662181,"ISBN":null,"volume":"13","issue":"6","year":2017,"title":"Structure of the Neisseria Adhesin Complex Protein (ACP) and its role as a novel lysozyme inhibitor.","URL":null,"raw_pages":"e1006448","medline_journal":"PLoS Pathog","ISO_journal":"PLoS Pathog","authors":["Humbert MV","Awanye AM","Lian LY","Derrick JP","Christodoulides M."],"DOI_URL":null}},"set_info":{"accession":"CL0887","name":"MliC_ACP-like"},"overlaps_with":null,"counters":{"subfamilies":0,"domain_architectures":2,"interactions":0,"matches":293,"pathways":0,"proteins":283,"proteomes":194,"sets":1,"structural_models":{"alphafold":213},"structures":2,"taxa":317},"entry_annotations":{"hmm":0,"logo":0,"alignment:seed":88,"alignment:full":129},"cross_references":{},"is_llm":false,"is_reviewed_llm":false,"is_updated_llm":false,"representative_structure":{"accession":"6gq4","name":"Neisseria gonorrhoeae Adhesin Complex Protein"}}}