CH60_ENTFA
ID CH60_ENTFA Reviewed; 541 AA.
AC Q93EU6;
DT 25-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 23-APR-2003, sequence version 2.
DT 03-AUG-2022, entry version 118.
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}; OrderedLocusNames=EF_2633;
OS Enterococcus faecalis (strain ATCC 700802 / V583).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae;
OC Enterococcus.
OX NCBI_TaxID=226185;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 29212 / DSM 2570;
RX PubMed=11526171; DOI=10.1128/jcm.39.9.3326-3331.2001;
RA Teng L.-J., Hsueh P.R., Wang Y.H., Lin H.M., Luh K.T., Ho S.W.;
RT "Determination of Enterococcus faecalis groESL full-length sequence and
RT application for species identification.";
RL J. Clin. Microbiol. 39:3326-3331(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700802 / V583;
RX PubMed=12663927; DOI=10.1126/science.1080613;
RA Paulsen I.T., Banerjei L., Myers G.S.A., Nelson K.E., Seshadri R.,
RA Read T.D., Fouts D.E., Eisen J.A., Gill S.R., Heidelberg J.F., Tettelin H.,
RA Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J., Daugherty S.C.,
RA DeBoy R.T., Durkin S.A., Kolonay J.F., Madupu R., Nelson W.C.,
RA Vamathevan J.J., Tran B., Upton J., Hansen T., Shetty J., Khouri H.M.,
RA Utterback T.R., Radune D., Ketchum K.A., Dougherty B.A., Fraser C.M.;
RT "Role of mobile DNA in the evolution of vancomycin-resistant Enterococcus
RT faecalis.";
RL Science 299:2071-2074(2003).
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}.
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DR EMBL; AF335185; AAL04033.1; -; Genomic_DNA.
DR EMBL; AE016830; AAO82342.1; -; Genomic_DNA.
DR RefSeq; NP_816272.1; NC_004668.1.
DR RefSeq; WP_002362559.1; NZ_KE136528.1.
DR AlphaFoldDB; Q93EU6; -.
DR SMR; Q93EU6; -.
DR STRING; 226185.EF_2633; -.
DR PRIDE; Q93EU6; -.
DR EnsemblBacteria; AAO82342; AAO82342; EF_2633.
DR GeneID; 60894630; -.
DR KEGG; efa:EF2633; -.
DR PATRIC; fig|226185.45.peg.926; -.
DR eggNOG; COG0459; Bacteria.
DR HOGENOM; CLU_016503_3_0_9; -.
DR OMA; TDTDKME; -.
DR Proteomes; UP000001415; 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; 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; Chaperone; Cytoplasm; Isomerase; Nucleotide-binding;
KW Reference proteome.
FT CHAIN 1..541
FT /note="Chaperonin GroEL"
FT /id="PRO_0000063371"
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 476..478
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00600"
FT BINDING 492
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00600"
FT CONFLICT 176
FT /note="E -> A (in Ref. 1; AAL04033)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 541 AA; 57110 MW; 4BEACA614ADF9D9A CRC64;
MAKEIKFAED ARAAMLRGVD VLADTVKVTL GPKGRNVVLE KSFGSPLITN DGVTIAKEIE
LEDHFENMGA KLVSEVASKT NDIAGDGTTT ATVLTQAIVR EGLKNVTAGA NPLGIRRGIE
LATKTAVEEL HNISSVVDSK EAIAQVAAVS SGSEKVGQLI ADAMEKVGND GVITIEESKG
IETELDVVEG MQFDRGYLSQ YMVTDNDKME AVLENPYILI TDKKISNIQD ILPLLEQILQ
QSRPLLIIAD DVDGEALPTL VLNKIRGTFN VVAVKAPGFG DRRKAMLEDI AILTGGTVIT
DDLGLELKDT TIENLGNASK VVVDKDNTTI VEGAGSKEAI DARVHLIKNQ IGETTSDFDR
EKLQERLAKL AGGVAVVKVG AATETELKEL KLRIEDALNA TRAAVEEGMV SGGGTALVNV
IGKVAALEAE GDVATGIKIV VRALEEPIRQ IAENAGYEGS VIVDKLKNVD LGIGFNAANG
EWVNMVEAGI VDPTKVTRSA LQNAASVSAL LLTTEAVVAD KPEPAAPAPM MDPSMGMGGM
M
