ID CH60_ACHLI Reviewed; 536 AA. AC A9NHL6; DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot. DT 05-FEB-2008, sequence version 1. DT 24-JAN-2024, entry version 88. 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=ACL_1247; OS Acholeplasma laidlawii (strain PG-8A). OC Bacteria; Mycoplasmatota; Mollicutes; Acholeplasmatales; OC Acholeplasmataceae; Acholeplasma. OX NCBI_TaxID=441768; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PG-8A; RX PubMed=21784942; DOI=10.1128/jb.05059-11; RA Lazarev V.N., Levitskii S.A., Basovskii Y.I., Chukin M.M., Akopian T.A., RA Vereshchagin V.V., Kostrjukova E.S., Kovaleva G.Y., Kazanov M.D., RA Malko D.B., Vitreschak A.G., Sernova N.V., Gelfand M.S., Demina I.A., RA Serebryakova M.V., Galyamina M.A., Vtyurin N.N., Rogov S.I., Alexeev D.G., RA Ladygina V.G., Govorun V.M.; RT "Complete genome and proteome of Acholeplasma laidlawii."; RL J. Bacteriol. 193:4943-4953(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; CP000896; ABX81846.1; -; Genomic_DNA. DR RefSeq; WP_012243177.1; NC_010163.1. DR AlphaFoldDB; A9NHL6; -. DR SMR; A9NHL6; -. DR STRING; 441768.ACL_1247; -. DR GeneID; 66294375; -. DR KEGG; acl:ACL_1247; -. DR eggNOG; COG0459; Bacteria. DR HOGENOM; CLU_016503_3_0_14; -. DR OMA; TDTDKME; -. DR OrthoDB; 9766614at2; -. DR Proteomes; UP000008558; Chromosome. 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; 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; 2. PE 3: Inferred from homology; KW ATP-binding; Chaperone; Cytoplasm; Isomerase; Nucleotide-binding; KW Reference proteome. FT CHAIN 1..536 FT /note="Chaperonin GroEL" FT /id="PRO_1000082460" FT BINDING 29..32 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00600" FT BINDING 86..90 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00600" FT BINDING 413 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00600" FT BINDING 494 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00600" SQ SEQUENCE 536 AA; 58267 MW; 23ED94C2EAA69C52 CRC64; MSKEIRYGKD AKQSLLKGVD LLANTVKITL GPKGRNVVLD KGYGSPLITN DGVSIAKEIE LKDPYENMGA KLLYEVASKT NDVAGDGTTT ATLLAQSIIH KGFKAVDNGA NPVLVREGIL RAGKEVSQKL LEKSRPVETS EDIENVASIS ASSREIGKII AEAMDKVSKN GVISVDESKG FETELEVVEG MQYDKGYISP YFVSDRETMT VELENPHVLV TDQKISTIQD ILPILEQVVK ANKPLLIIAD DIENEVTSTL ILNKLRGTFN VVATKAPGFG DNQKDMLNDI AILTGATFYA KDLQMKLQEI KLEDLGLVQK AVVKKDTTTL IGGHGTKDAI DKRILEIEAQ INSSTSDYDK KRLQERLAKL AGGVAIIKVG AATEAELKEK KLRIEDALNA TKAAILEGIV AGGGSVLVDI QTELKETLKD SHIDIYKGIL AVLDSLSEPL YQIAENAGFD GQDILTEQRK QNKNYGFDAK EGKWVNMLKE GIIDPTKVTR NAILNASSIG ALMITSEAAV VEIKDKDQNI PTQPMY //