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 24-JAN-2024, entry version 84. DE RecName: Full=Chaperonin GroEL {ECO:0000255|HAMAP-Rule:MF_00600}; DE EC=5.6.1.7 {ECO:0000255|HAMAP-Rule:MF_00600}; DE AltName: Full=60 kDa chaperonin {ECO:0000255|HAMAP-Rule:MF_00600}; DE AltName: Full=Chaperonin-60 {ECO:0000255|HAMAP-Rule:MF_00600}; DE Short=Cpn60 {ECO:0000255|HAMAP-Rule:MF_00600}; GN Name=groEL {ECO:0000255|HAMAP-Rule:MF_00600}; GN Synonyms=groL {ECO:0000255|HAMAP-Rule:MF_00600}; GN OrderedLocusNames=Bphyt_0864; OS Paraburkholderia phytofirmans (strain DSM 17436 / LMG 22146 / PsJN) OS (Burkholderia phytofirmans). OC Bacteria; Pseudomonadota; 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: 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 + H2O + 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; CP001052; ACD15285.1; -; Genomic_DNA. DR RefSeq; WP_012431919.1; NC_010681.1. DR AlphaFoldDB; B2T0I0; -. DR SMR; B2T0I0; -. DR STRING; 398527.Bphyt_0864; -. DR KEGG; bpy:Bphyt_0864; -. DR eggNOG; COG0459; Bacteria. DR HOGENOM; CLU_016503_3_0_4; -. DR OMA; TDTDKME; -. DR OrthoDB; 9766614at2; -. 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:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro. DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW. 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; 3.50.7.10; GroEL; 1. DR Gene3D; 1.10.560.10; GroEL-like equatorial domain; 1. DR Gene3D; 3.30.260.10; TCP-1-like chaperonin intermediate domain; 1. DR HAMAP; MF_00600; CH60; 1. DR InterPro; IPR018370; Chaperonin_Cpn60_CS. DR InterPro; IPR001844; Cpn60/GroEL. DR InterPro; IPR002423; Cpn60/GroEL/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 NCBIfam; TIGR02348; GroEL; 1. DR PANTHER; PTHR45633; 60 KDA HEAT SHOCK PROTEIN, MITOCHONDRIAL; 1. DR PANTHER; PTHR45633:SF3; 60 KDA HEAT SHOCK PROTEIN, MITOCHONDRIAL; 1. DR Pfam; PF00118; Cpn60_TCP1; 1. DR PRINTS; PR00298; CHAPERONIN60. DR SUPFAM; SSF52029; GroEL apical domain-like; 1. DR SUPFAM; SSF48592; GroEL equatorial domain-like; 1. DR SUPFAM; SSF54849; GroEL-intermediate domain like; 1. DR PROSITE; PS00296; CHAPERONINS_CPN60; 1. PE 3: Inferred from homology; KW ATP-binding; Chaperone; Cytoplasm; Isomerase; Nucleotide-binding. FT CHAIN 1..546 FT /note="Chaperonin GroEL" FT /id="PRO_1000129984" FT BINDING 30..33 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00600" FT BINDING 51 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00600" FT BINDING 87..91 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00600" FT BINDING 415 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00600" FT BINDING 479..481 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00600" FT BINDING 495 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00600" 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 //