{"metadata":{"accession":"PF11962","entry_id":null,"type":"domain","go_terms":null,"source_database":"pfam","member_databases":null,"integrated":"IPR021865","hierarchy":null,"name":{"name":"Peptidase_G2, IMC autoproteolytic cleavage domain","short":"Peptidase_G2"},"description":[{"text":"<p>This domain is found at the very C-terminus of bacteriophage parallel beta-helical tailspike proteins. It carries the enzymic residues that induce autoproteolytic cleavage to bring about maturation of the folding process of the helix in a chaperone-like manner. The domain thus mediates the assembly of a large tailspike protein and then releases itself after maturation. These C-terminal regions that autoproteolytically release themselves after maturation are exchangeable between functionally unrelated N-terminal proteins and have been identified in a number of bacteriophage tailspike proteins [[cite:PUB00057232]].</p>","llm":false,"checked":false,"updated":false}],"wikipedia":null,"literature":{"PUB00057232":{"PMID":21330133,"ISBN":null,"volume":"21","issue":"2","year":2011,"title":"Knitting and snipping: chaperones in β-helix folding.","URL":null,"raw_pages":"232-9","medline_journal":"Curr Opin Struct Biol","ISO_journal":"Curr. Opin. Struct. Biol.","authors":["Schulz EC","Ficner R."],"DOI_URL":"http://dx.doi.org/10.1016/j.sbi.2011.01.009"}},"set_info":null,"overlaps_with":null,"counters":{"subfamilies":0,"domain_architectures":31,"interactions":0,"matches":340,"pathways":0,"proteins":321,"proteomes":241,"sets":0,"structural_models":{"alphafold":163},"structures":11,"taxa":502},"entry_annotations":{"hmm":0,"logo":0,"alignment:seed":6,"alignment:full":183},"cross_references":{},"is_llm":false,"is_reviewed_llm":false,"is_updated_llm":false,"representative_structure":{"accession":"3gqh","name":"Crystal Structure of the Bacteriophage phi29 gene product 12 C-terminal fragment"}}}