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 03-OCT-2012, entry version 35. DE RecName: Full=60 kDa chaperonin; DE AltName: Full=GroEL protein; DE AltName: Full=Protein Cpn60; GN Name=groL; Synonyms=groEL; OrderedLocusNames=ACL_1247; OS Acholeplasma laidlawii (strain PG-8A). OC Bacteria; Tenericutes; 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., RA Akopian T.A., Vereshchagin V.V., Kostrjukova E.S., Kovaleva G.Y., RA Kazanov M.D., Malko D.B., Vitreschak A.G., Sernova N.V., Gelfand M.S., RA Demina I.A., Serebryakova M.V., Galyamina M.A., Vtyurin N.N., RA Rogov S.I., Alexeev D.G., Ladygina V.G., Govorun V.M.; RT "Complete genome and proteome of Acholeplasma laidlawii."; RL J. Bacteriol. 193:4943-4953(2011). 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; CP000896; ABX81846.1; -; Genomic_DNA. DR RefSeq; YP_001621222.1; NC_010163.1. DR ProteinModelPortal; A9NHL6; -. DR SMR; A9NHL6; 2-518. DR STRING; A9NHL6; -. DR GeneID; 5804462; -. DR GenomeReviews; CP000896_GR; ACL_1247. DR KEGG; acl:ACL_1247; -. DR PATRIC; 20639186; VBIAchLai134690_1199. DR eggNOG; COG0459; -. DR HOGENOM; HOG000076290; -. DR KO; K04077; -. DR OMA; ATSQANE; -. DR ProtClustDB; PRK00013; -. DR BioCyc; ALAI441768:ACL_1247-MONOMER; -. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0042026; P:protein refolding; IEA:InterPro. DR HAMAP; MF_00600; CH60; 1; -. DR InterPro; IPR001844; Chaprnin_Cpn60. DR InterPro; IPR002423; Cpn60/TCP-1. DR PANTHER; PTHR11353; PTHR11353; 1. DR Pfam; PF00118; Cpn60_TCP1; 1. DR PRINTS; PR00298; CHAPERONIN60. DR SUPFAM; SSF48592; GroEL-ATPase; 1. DR TIGRFAMs; TIGR02348; GroEL; 1. DR PROSITE; PS00296; CHAPERONINS_CPN60; FALSE_NEG. PE 3: Inferred from homology; KW ATP-binding; Chaperone; Complete proteome; Cytoplasm; KW Nucleotide-binding. FT CHAIN 1 536 60 kDa chaperonin. FT /FTId=PRO_1000082460. 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 //