ID CH60_PARPJ Reviewed; 546 AA. AC B2T0I0; DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-2008, sequence version 1. DT 11-DEC-2019, entry version 69. DE RecName: Full=60 kDa chaperonin {ECO:0000255|HAMAP-Rule:MF_00600}; DE AltName: Full=GroEL protein {ECO:0000255|HAMAP-Rule:MF_00600}; DE AltName: Full=Protein Cpn60 {ECO:0000255|HAMAP-Rule:MF_00600}; GN Name=groL {ECO:0000255|HAMAP-Rule:MF_00600}; GN Synonyms=groEL {ECO:0000255|HAMAP-Rule:MF_00600}; GN OrderedLocusNames=Bphyt_0864; OS Paraburkholderia phytofirmans (strain DSM 17436 / LMG 22146 / PsJN) OS (Burkholderia phytofirmans). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Paraburkholderia. OX NCBI_TaxID=398527; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 17436 / LMG 22146 / PsJN; RX PubMed=21551308; DOI=10.1128/jb.05055-11; RA Weilharter A., Mitter B., Shin M.V., Chain P.S., Nowak J., Sessitsch A.; RT "Complete genome sequence of the plant growth-promoting endophyte RT Burkholderia phytofirmans strain PsJN."; RL J. Bacteriol. 193:3383-3384(2011). CC -!- FUNCTION: Prevents misfolding and promotes the refolding and proper CC assembly of unfolded polypeptides generated under stress conditions. CC {ECO:0000255|HAMAP-Rule:MF_00600}. CC -!- SUBUNIT: Oligomer of 14 subunits composed of two stacked rings of 7 CC subunits. {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; CP001052; ACD15285.1; -; Genomic_DNA. DR RefSeq; WP_012431919.1; NC_010681.1. DR SMR; B2T0I0; -. DR STRING; 398527.Bphyt_0864; -. DR EnsemblBacteria; ACD15285; ACD15285; Bphyt_0864. DR KEGG; bpy:Bphyt_0864; -. DR eggNOG; ENOG4105CJ9; Bacteria. DR eggNOG; COG0459; LUCA. DR HOGENOM; HOG000076290; -. DR KO; K04077; -. DR OMA; TDTDKME; -. DR OrthoDB; 265347at2; -. DR Proteomes; UP000001739; Chromosome 1. 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; Nucleotide-binding. FT CHAIN 1..546 FT /note="60 kDa chaperonin" FT /id="PRO_1000129984" SQ SEQUENCE 546 AA; 57136 MW; 1624DA136AF66038 CRC64; MAAKDVVFGD SARAKMVEGV NILANAVKVT LGPKGRNVVL ERSFGGPTVT KDGVSVAKEI ELKDKLQNMG AQMVKEVASK TSDNAGDGTT TATVLAQSIV REGMKYVASG MNPMDLKRGI DKAVTAAIEE LRKISKPCTT NKEIAQVGAI SANSDSSIGD RIAEAMDKVG KEGVITVEDG KSLQDELDVV EGMQFDRGYL SPYFINNPDK QVAVLDNPFV LLHDKKVSNI RDLLPVLEQV AKAGRPLLII AEDVEGEALA TLVVNNIRGI LKTVAVKAPG FGDRRKAMLE DIAILTGGQV IAEETGLTLE KATLAELGQA KRIEVGKENT TIIDGAGEAA NIEARVKQVR TQIEEATSDY DREKLQERVA KLAGGVAVIK VGAATEVEMK EKKARVEDAL HATRAAVEEG IVAGGGVALI RARTAIAGLK GANADQDAGI KIVLRAMEEP LRQIVTNGGE EASVVVAAVA AGQGNYGYNA ATGEYVDLVD AGVVDPTKVT RTALQNAASV AGLLLTTDAA VCELPKEDAP MAGGMPGGMG GMGMDM //