ID CH60_BURPP Reviewed; 546 AA. AC B2T0I0; DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-2008, sequence version 1. DT 15-DEC-2009, entry version 13. DE RecName: Full=60 kDa chaperonin; DE AltName: Full=Protein Cpn60; DE AltName: Full=groEL protein; GN Name=groL; Synonyms=groEL; OrderedLocusNames=Bphyt_0864; OS Burkholderia phytofirmans (strain DSM 17436 / PsJN). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia. OX NCBI_TaxID=398527; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., RA Lang D., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., RA Mikhailova N., Nowak J., Sessitsch A., Lazarovits G., Compant S., RA Barka E., Tiedje J.; RT "Complete sequence of chromosome 1 of Burkholderia phytofirmans RT PsJN."; RL Submitted (MAY-2008) 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; CP001052; ACD15285.1; -; Genomic_DNA. DR RefSeq; YP_001894509.1; -. DR GeneID; 6284451; -. DR GenomeReviews; CP001052_GR; Bphyt_0864. DR KEGG; bpy:Bphyt_0864; -. DR HOGENOM; HBG625289; -. DR OMA; TANAGDE; -. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:HAMAP. DR GO; GO:0051082; F:unfolded protein binding; IEA:HAMAP. DR GO; GO:0042026; P:protein refolding; IEA:HAMAP. DR HAMAP; MF_00600; -; 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 PROSITE; PS00296; CHAPERONINS_CPN60; 1. PE 3: Inferred from homology; KW ATP-binding; Chaperone; Complete proteome; Cytoplasm; KW Nucleotide-binding. FT CHAIN 1 546 60 kDa chaperonin. FT /FTId=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 //