ID CH602_RHOPB Reviewed; 551 AA. AC Q20X88; DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot. DT 18-APR-2006, sequence version 1. DT 21-SEP-2011, entry version 36. DE RecName: Full=60 kDa chaperonin 2; DE AltName: Full=GroEL protein 2; DE AltName: Full=Protein Cpn60 2; GN Name=groL2; Synonyms=groEL2; OrderedLocusNames=RPC_4726; OS Rhodopseudomonas palustris (strain BisB18). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Bradyrhizobiaceae; Rhodopseudomonas. OX NCBI_TaxID=316056; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BisB18; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., RA Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., RA Larimer F., Land M., Hauser L., Pelletier D.A., Kyrpides N., RA Anderson I., Oda Y., Harwood C.S., Richardson P.; RT "Complete sequence of Rhodopseudomonas palustris BisB18."; RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Prevents misfolding and promotes the refolding and CC proper assembly of unfolded polypeptides generated under stress CC conditions (By similarity). CC -!- SUBUNIT: Oligomer of 14 subunits composed of two stacked rings of CC 7 subunits (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). CC -!- SIMILARITY: Belongs to the chaperonin (HSP60) family. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP000301; ABD90248.1; -; Genomic_DNA. DR RefSeq; YP_534567.1; NC_007925.1. DR HSSP; P0A6F5; 2CGT. DR ProteinModelPortal; Q20X88; -. DR SMR; Q20X88; 2-526. DR STRING; Q20X88; -. DR GeneID; 3972702; -. DR GenomeReviews; CP000301_GR; RPC_4726. DR KEGG; rpc:RPC_4726; -. DR eggNOG; COG0459; -. DR HOGENOM; HBG625289; -. DR OMA; SANGDEN; -. DR ProtClustDB; PRK12852; -. DR BioCyc; RPAL316056:RPC_4726-MON; -. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0042026; P:protein refolding; IEA:InterPro. DR HAMAP; MF_00600; CH60; 1; -. DR InterPro; IPR018370; Chaperonin_Cpn60_CS. DR InterPro; IPR001844; Chaprnin_Cpn60. DR InterPro; IPR002423; Cpn60/TCP-1. DR PANTHER; PTHR11353; Cpn60/TCP-1; 1. DR Pfam; PF00118; Cpn60_TCP1; 1. DR PRINTS; PR00298; CHAPERONIN60. DR SUPFAM; SSF48592; GroEL-ATPase; 1. DR TIGRFAMs; TIGR02348; GroEL; 1. DR PROSITE; PS00296; CHAPERONINS_CPN60; 1. PE 3: Inferred from homology; KW ATP-binding; Chaperone; Complete proteome; Cytoplasm; KW Nucleotide-binding. FT CHAIN 1 551 60 kDa chaperonin 2. FT /FTId=PRO_0000256971. SQ SEQUENCE 551 AA; 57861 MW; BF613FFE58F5F640 CRC64; MAAKDVKFAG DARDRMLRGV DILANAVKVT LGPKGRNVLI ERSFGAARIT KDGVTVAKEI ELEDKFENMG AQMLREVASK TNDLAGDGTT TATVLAQAIV REGAKSVAAG MNPMDLKRGI EIAVAAVIKD LVKRAKPVAS SAEIAQVGTI SSNGDAAIGK MIAQAMQKVG NEGVITVEEN KSLTTEVDIV EGMKFDRGYL SPYFVTNAEK MAVEFDDAYV LLHEKKVSGL QSMLPLLEAV VQSGKPLVII AEDVEGEALA TLVVNRLRGG LKVAAVKAPG FGDRRKAMLE DLAILTGGQL ISDDLGMKLE NVTLKMLGRA KKLVIDKENT TIVGGAGKKA DIETRVGQIK AQIEETTSDY DREKLQERLA KLAGGVAVIR VGGATEVEVK EKKDRVEDAL NATRAAVQEG IVPGGGVALL RAKKAVGRIS NDNPDVQAGI NIVLKALEAP IRQIAENAGV EGSIVVGKIL ENKSETFGFD AQTEEYVDML AKGIVDPAKV VRTALQDASS VAALLVTTEC MVAEMPRDAA PAMPGGGGGM GGMGGMGGMG F //