{"metadata":{"accession":"I3V6P1","id":"I3V6P1_ACILW","source_organism":{"taxId":"28090","scientificName":"Acinetobacter lwoffii","fullName":"Acinetobacter lwoffii"},"name":"Co-chaperonin GroES","description":["Together with the chaperonin GroEL, plays an essential role in assisting protein folding. The GroEL-GroES system forms a nano-cage that allows encapsulation of the non-native substrate proteins and provides a physical environment optimized to promote and accelerate protein folding. GroES binds to the apical surface of the GroEL ring, thereby capping the opening of the GroEL channel"],"length":133,"sequence":"MACRVRPVLLSAVWHSLRATAKIAGFFHVNQPFTEVAMSNIKPLHDRVVIKRMEEEKLSAGGIVIPDSATEKPIKGEVVAVGTGKVLDNGQVRAPQVKVGDKVLFGKYSGTEVKLDGVELLVVKEDDLFAILG","proteome":null,"gene":"groES","go_terms":[{"identifier":"GO:0006457","name":"protein folding","category":{"code":"P","name":"biological_process"}},{"identifier":"GO:0005524","name":"ATP binding","category":{"code":"F","name":"molecular_function"}},{"identifier":"GO:0044183","name":"protein folding chaperone","category":{"code":"F","name":"molecular_function"}}],"protein_evidence":3,"source_database":"unreviewed","is_fragment":false,"in_alphafold":true,"in_bfvd":false,"ida_accession":"96ac8ba8a540be879c6c062e6821e3878208f354","counters":{"domain_architectures":38603,"entries":17,"isoforms":0,"proteomes":0,"sets":2,"structures":0,"taxa":1,"dbEntries":{"cathgene3d":1,"ssf":1,"pfam":1,"smart":1,"cdd":1,"panther":1,"ncbifam":4,"hamap":1,"prosite":1,"prints":1,"interpro":4},"proteome":0,"taxonomy":1,"similar_proteins":38603}}}