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 29-SEP-2021, entry version 90. DE RecName: Full=Chaperonin GroEL 2 {ECO:0000255|HAMAP-Rule:MF_00600}; DE EC=5.6.1.7 {ECO:0000255|HAMAP-Rule:MF_00600}; DE AltName: Full=60 kDa chaperonin 2 {ECO:0000255|HAMAP-Rule:MF_00600}; DE AltName: Full=Chaperonin-60 2 {ECO:0000255|HAMAP-Rule:MF_00600}; DE Short=Cpn60 2 {ECO:0000255|HAMAP-Rule:MF_00600}; GN Name=groEL2 {ECO:0000255|HAMAP-Rule:MF_00600}; GN Synonyms=groL2 {ECO:0000255|HAMAP-Rule:MF_00600}; GN OrderedLocusNames=RPC_4726; OS Rhodopseudomonas palustris (strain BisB18). OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales; OC Bradyrhizobiaceae; Rhodopseudomonas. OX NCBI_TaxID=316056; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BisB18; RG US DOE Joint Genome Institute; 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., Pitluck S., RA Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., RA Hauser L., Pelletier D.A., Kyrpides N., Anderson I., Oda Y., Harwood C.S., RA Richardson P.; RT "Complete sequence of Rhodopseudomonas palustris BisB18."; RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Together with its co-chaperonin GroES, plays an essential CC role in assisting protein folding. The GroEL-GroES system forms a nano- CC cage that allows encapsulation of the non-native substrate proteins and CC provides a physical environment optimized to promote and accelerate CC protein folding. {ECO:0000255|HAMAP-Rule:MF_00600}. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + H(2)O + a folded polypeptide = ADP + phosphate + an CC unfolded polypeptide.; EC=5.6.1.7; Evidence={ECO:0000255|HAMAP- CC Rule:MF_00600}; CC -!- SUBUNIT: Forms a cylinder of 14 subunits composed of two heptameric CC rings stacked back-to-back. Interacts with the co-chaperonin GroES. CC {ECO:0000255|HAMAP-Rule:MF_00600}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00600}. CC -!- SIMILARITY: Belongs to the chaperonin (HSP60) family. CC {ECO:0000255|HAMAP-Rule:MF_00600}. 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; WP_011475125.1; NC_007925.1. DR SMR; Q20X88; -. DR STRING; 316056.RPC_4726; -. DR EnsemblBacteria; ABD90248; ABD90248; RPC_4726. DR KEGG; rpc:RPC_4726; -. DR eggNOG; COG0459; Bacteria. DR HOGENOM; CLU_016503_3_0_5; -. DR OMA; TDTDKME; -. DR OrthoDB; 265347at2; -. DR BioCyc; RPAL316056:G1G6B-4776-MONOMER; -. DR Proteomes; UP000001948; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0051082; F:unfolded protein binding; IEA:UniProtKB-UniRule. DR GO; GO:0042026; P:protein refolding; IEA:UniProtKB-UniRule. DR CDD; cd03344; GroEL; 1. DR Gene3D; 1.10.560.10; -; 1. DR Gene3D; 3.30.260.10; -; 1. DR Gene3D; 3.50.7.10; -; 1. DR HAMAP; MF_00600; CH60; 1. DR InterPro; IPR018370; Chaperonin_Cpn60_CS. DR InterPro; IPR001844; Chaprnin_Cpn60. DR InterPro; IPR002423; Cpn60/TCP-1. DR InterPro; IPR027409; GroEL-like_apical_dom_sf. DR InterPro; IPR027413; GROEL-like_equatorial_sf. DR InterPro; IPR027410; TCP-1-like_intermed_sf. DR Pfam; PF00118; Cpn60_TCP1; 1. DR PRINTS; PR00298; CHAPERONIN60. DR SUPFAM; SSF48592; SSF48592; 1. DR SUPFAM; SSF52029; SSF52029; 1. DR SUPFAM; SSF54849; SSF54849; 1. DR TIGRFAMs; TIGR02348; GroEL; 1. DR PROSITE; PS00296; CHAPERONINS_CPN60; 1. PE 3: Inferred from homology; KW ATP-binding; Chaperone; Cytoplasm; Isomerase; Nucleotide-binding; KW Reference proteome. FT CHAIN 1..551 FT /note="Chaperonin GroEL 2" FT /id="PRO_0000256971" FT NP_BIND 30..33 FT /note="ATP" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00600" FT NP_BIND 87..91 FT /note="ATP" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00600" FT BINDING 51 FT /note="ATP" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00600" FT BINDING 415 FT /note="ATP; via amide nitrogen" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00600" FT BINDING 496 FT /note="ATP" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00600" 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 //