ID   CH60_DEHMC              Reviewed;         537 AA.
AC   Q3ZYW8;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   27-SEP-2005, sequence version 1.
DT   03-AUG-2022, entry version 99.
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=cbdbA1393;
OS   Dehalococcoides mccartyi (strain CBDB1).
OC   Bacteria; Chloroflexi; Dehalococcoidia; Dehalococcoidales;
OC   Dehalococcoidaceae; Dehalococcoides.
OX   NCBI_TaxID=255470;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBDB1;
RX   PubMed=16116419; DOI=10.1038/nbt1131;
RA   Kube M., Beck A., Zinder S.H., Kuhl H., Reinhardt R., Adrian L.;
RT   "Genome sequence of the chlorinated compound-respiring bacterium
RT   Dehalococcoides species strain CBDB1.";
RL   Nat. Biotechnol. 23:1269-1273(2005).
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; AJ965256; CAI83436.1; -; Genomic_DNA.
DR   RefSeq; WP_011309787.1; NC_007356.1.
DR   AlphaFoldDB; Q3ZYW8; -.
DR   SMR; Q3ZYW8; -.
DR   KEGG; deh:cbdbA1393; -.
DR   HOGENOM; CLU_016503_3_0_0; -.
DR   OMA; PYILINQ; -.
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.
FT   CHAIN           1..537
FT                   /note="Chaperonin GroEL"
FT                   /id="PRO_0000256903"
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         492
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00600"
SQ   SEQUENCE   537 AA;  57125 MW;  9A9EC7F7F1970EB2 CRC64;
     MAKQIIFGEK VRVSLKKGVD TLANTVRVTL GPKGHPVALE RKWGAPTVID DGVTIARDIE
     LPDAFENMGA QLVKEAATRT SDAAGDGTTT SIVLAQAIIN EAFKNIAAGA EPINLKRGIE
     KAVAALKAQL RKNSTPVKGK QQIVQVATIT GKDPEIGNLI ADVMDKVGKD GVITIEESRG
     LRYETSYVEG MQFDRGYISA YFVTDPGRME SVMEDATILM TDRKIETVAE LLPALEKILQ
     ISKNLVIVAE NVEAEALATL VVNKLRGNLN ILAVKAPGYG DRQKAMLEDM AILTGGHVIS
     KEAGRKLDSV TEADLGHARR IVSNKDKTTI IDGEGSAEAI KDRIKQIKAQ IEETESAFDR
     EKLQERQAAL VGGVAVIAVG AATETEMKER KARVEDALAA TRAAIEEGIL PGGGTGLLNA
     LPCLDALKLE GDEATGVNIV RKALIEPVRW IATNAGKDGN VIVDKVKNSP VGHGYNAEND
     VFGDMAEMGI IDPTMVVRSA LENAASIANM VLITDSLVAD IQEKAPAAPG PEAAGMY