{"metadata":{"accession":"A0AB33HPC3","id":"A0AB33HPC3_MYCPM","source_organism":{"taxId":"1112856","scientificName":"Mycoplasmoides pneumoniae 309","fullName":"Mycoplasmoides pneumoniae 309"},"name":"Chaperonin GroEL","description":["Together with its co-chaperonin GroES, 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"],"length":543,"sequence":"MAKELVFGKNARNKLLAGINKLADAVKVTVGPKGQNVILGRKFSNPLITNDGVTIAKEIELTDPLENIGAKVISVAAVSTNDIAGDGTTTATILAQEMTNRGVEAVNNGANPVNVRRGIEDASQLIITELDKRSKKINTNEEIEQVAAISSGSKEIGKLIAQAMALVGKNGVITTDDAKTINTTLETTEGIEFKGTYASPYMVSDQEKMEVVLDQPKILVSAMKINTIKEILPLLEGSMENGNPLLIVAPDFAEEVVTTLAVNKLRGTINVVAVKCNEYGERQKAALEDLAISTGTLAYNNELGGGFKDVTVNHLGEARRVQVAKEKTTVIGGKGSKETIQKHLDLLNGRLKQTTEKYDTDLLKERIAHLSQGVAVVRVGGATELAQKELKLRIEDALNSTKAAVEEGIISGGGIALLNVSTILNDSKLADKYKAETSAENLKEILVGYEIVRKSLEAPVRQIIENSGVNPVKVFAELRSEADGVGFDAETKKKVDMIRSGIIDPTKVTKTALEKAASVASSLITTSVAVYDIKENKEGSFQE","proteome":null,"gene":"groEL","go_terms":[{"identifier":"GO:0140662","name":"ATP-dependent protein folding chaperone","category":{"code":"F","name":"molecular_function"}},{"identifier":"GO:0042026","name":"protein refolding","category":{"code":"P","name":"biological_process"}},{"identifier":"GO:0005524","name":"ATP binding","category":{"code":"F","name":"molecular_function"}},{"identifier":"GO:0006457","name":"protein folding","category":{"code":"P","name":"biological_process"}}],"protein_evidence":3,"source_database":"unreviewed","is_fragment":false,"in_alphafold":true,"in_bfvd":false,"ida_accession":"bef8793fffa344cae7b4310cccda4040a454c532","counters":{"domain_architectures":111908,"entries":23,"isoforms":0,"proteomes":0,"sets":1,"structures":0,"taxa":1,"dbEntries":{"ssf":3,"cdd":1,"cathgene3d":3,"ncbifam":5,"hamap":1,"panther":1,"pfam":1,"prosite":1,"prints":1,"interpro":6},"proteome":0,"taxonomy":1,"similar_proteins":111908}}}