ID A0A0G3HIX5_9CORY Unreviewed; 544 AA. AC A0A0G3HIX5; DT 16-SEP-2015, integrated into UniProtKB/TrEMBL. DT 16-SEP-2015, sequence version 1. DT 12-OCT-2022, entry version 28. DE RecName: Full=Chaperonin GroEL {ECO:0000256|HAMAP-Rule:MF_00600}; DE EC=5.6.1.7 {ECO:0000256|HAMAP-Rule:MF_00600}; DE AltName: Full=60 kDa chaperonin {ECO:0000256|HAMAP-Rule:MF_00600}; DE AltName: Full=Chaperonin-60 {ECO:0000256|HAMAP-Rule:MF_00600}; DE Short=Cpn60 {ECO:0000256|HAMAP-Rule:MF_00600}; GN Name=groL2 {ECO:0000313|EMBL:AKK11893.1}; GN Synonyms=groEL {ECO:0000256|HAMAP-Rule:MF_00600}, groL GN {ECO:0000256|HAMAP-Rule:MF_00600}; GN ORFNames=CUTER_09625 {ECO:0000313|EMBL:AKK11893.1}; OS Corynebacterium uterequi. OC Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae; OC Corynebacterium. OX NCBI_TaxID=1072256 {ECO:0000313|EMBL:AKK11893.1, ECO:0000313|Proteomes:UP000035548}; RN [1] {ECO:0000313|EMBL:AKK11893.1, ECO:0000313|Proteomes:UP000035548} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 45634 {ECO:0000313|EMBL:AKK11893.1, RC ECO:0000313|Proteomes:UP000035548}; RX PubMed=26227590; RA Ruckert C., Kriete M., Jaenicke S., Winkler A., Tauch A.; RT "Virulence Factor Genes Detected in the Complete Genome Sequence of RT Corynebacterium uterequi DSM 45634, Isolated from the Uterus of a Maiden RT Mare."; RL Genome Announc. 3:e00783-15(2015). RN [2] {ECO:0000313|Proteomes:UP000035548} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 45634 {ECO:0000313|Proteomes:UP000035548}; RA Ruckert C., Albersmeier A., Winkler A., Tauch A.; RT "Complete genome sequence of Corynebacterium uterequi DSM 45634, isolated RT from the uterus of a maiden mare."; RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases. 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:0000256|HAMAP-Rule:MF_00600, CC ECO:0000256|RuleBase:RU000419}. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + H2O + a folded polypeptide = ADP + phosphate + an CC unfolded polypeptide.; EC=5.6.1.7; Evidence={ECO:0000256|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:0000256|HAMAP-Rule:MF_00600, ECO:0000256|RuleBase:RU000419}. CC -!- SUBCELLULAR LOCATION: Cell surface {ECO:0000256|ARBA:ARBA00004241}. CC Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00600}. Secreted, capsule CC {ECO:0000256|ARBA:ARBA00025702}. Secreted, cell wall CC {ECO:0000256|ARBA:ARBA00004191}. CC -!- SIMILARITY: Belongs to the chaperonin (HSP60) family. CC {ECO:0000256|ARBA:ARBA00006607, ECO:0000256|HAMAP-Rule:MF_00600, CC ECO:0000256|RuleBase:RU000418}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC feature annotation. {ECO:0000256|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; CP011546; AKK11893.1; -; Genomic_DNA. DR RefSeq; WP_047260211.1; NZ_CP011546.1. DR STRING; 1072256.CUTER_09625; -. DR EnsemblBacteria; AKK11893; AKK11893; CUTER_09625. DR KEGG; cut:CUTER_09625; -. DR PATRIC; fig|1072256.5.peg.1896; -. DR OrthoDB; 265347at2; -. DR Proteomes; UP000035548; Chromosome. DR GO; GO:0042603; C:capsule; IEA:UniProtKB-SubCell. DR GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell. 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; 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; 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 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 {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP- KW Rule:MF_00600}; KW Chaperone {ECO:0000256|ARBA:ARBA00023186, ECO:0000256|HAMAP-Rule:MF_00600}; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00600}; KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|HAMAP-Rule:MF_00600}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP- KW Rule:MF_00600}; Reference proteome {ECO:0000313|Proteomes:UP000035548}. FT REGION 525..544 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 349..412 FT /evidence="ECO:0000256|SAM:Coils" FT BINDING 29..32 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00600" FT BINDING 86..90 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00600" FT BINDING 418 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00600" FT BINDING 481..483 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00600" FT BINDING 497 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00600" SQ SEQUENCE 544 AA; 57153 MW; 5B3124EA78DA6C25 CRC64; MSKIIAFDEE ARRGLERGLN TLADAVKVTL GPKGRNVVLE KSWGAPTITN DGVTIAKEIE LEDPYEKIGA ELVKEVAKKT DDVAGDGTTT ATVLAQALVS EGLRNVAAGS NPMGIKRGIE AAVAKVNDEI LATAKEVETE EEIAQTAGIS AADPEIGKQI ARAMYAVGNG AVNKDSVITV EESNTFGVDL EVTEGMRFDK GYISGYFATD MERQEAVLED PYILLVSAKI SNIKDLLPLL EQVMQSGKPL LIIAEDVEGE ALSTLVVNKI RGTFKSVAVK APGFGDRRKA QLQDMAILTG GQVISEEVGL SLETATVDLL GTARKVVVTK DETTIVQGAG SPEQIEGRVK QIRAEIENSD SEYDREKLQE RLAKLAGGVA VIKVGAATEV ELKERKLRIE DAVRNAKAAV EEGIVAGGGV ALLQAASVLD SLELEGDEAT GVKIVRDSLS APLKQIAFNA GLEPGVVADK VAHLPTGEGL NAATGEYVDM MKAGINDPAK VTRSALQNAA SIAALFLTTE AVVADKPQPA GSGPSPEDMA GMGM //