ID   CH60_PECCC              Reviewed;         540 AA.
AC   O66220;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   03-AUG-2022, entry version 91.
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};
DE   Flags: Fragment;
GN   Name=groEL {ECO:0000255|HAMAP-Rule:MF_00600};
GN   Synonyms=groL {ECO:0000255|HAMAP-Rule:MF_00600}, mopA;
OS   Pectobacterium carotovorum subsp. carotovorum (Erwinia carotovora subsp.
OS   carotovora).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Pectobacteriaceae; Pectobacterium.
OX   NCBI_TaxID=555;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=JCM 20699 / NBRC 3380 / IAM 12633;
RX   PubMed=12501307; DOI=10.2323/jgam.43.355;
RA   Harada H., Ishikawa H.;
RT   "Phylogenetical relationship based on groE genes among phenotypically
RT   related Enterobacter, Pantoea, Klebsiella, Serratia, and Erwinia species.";
RL   J. Gen. Appl. Microbiol. 43:355-361(1997).
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; AB008152; BAA25237.1; -; Genomic_DNA.
DR   AlphaFoldDB; O66220; -.
DR   SMR; O66220; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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:0042026; P:protein refolding; IEA:InterPro.
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..>540
FT                   /note="Chaperonin GroEL"
FT                   /id="PRO_0000063375"
FT   BINDING         30..33
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00600"
FT   BINDING         51
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00600"
FT   BINDING         87..91
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00600"
FT   BINDING         415
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00600"
FT   BINDING         479..481
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00600"
FT   BINDING         495
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00600"
FT   NON_TER         540
SQ   SEQUENCE   540 AA;  56293 MW;  7E41FEA699566719 CRC64;
     MAAKDVKFGN DARVKMLRGV NVLADAVKVT LGPKGRNVVL DKSFGAPTIT KDGVSVAREI
     ELEDKFENMG AQMVKEVASK ANDAAGDGTT TATVLAQAII TEGLKAVAAG MNPMDLKRGI
     DKAVIAAVEE LKALSVPCSD SKAIAQVGTI SANSDETVGK MIAEAMDKVG KEGVITVEEG
     TGLQDELDVV EGMQFDRGYL SPYFINKPET GAVELESPFI LLADKKISNI REMLPVLEAV
     AKAGKPLVIV AEDVEGEALA TLVVNTMRGI VKVAAVKAPG FGDRRKAMLQ DIATLTGGTV
     ISEEIGLELE KATLEDLGQA KRVVINKDTT TIIDGTGEEA AIQGRVAQIR QQVEEATSDY
     DKEKLQERVA KLAGGVAVIK VGAATEVEMK EKKARVEDAL AATRAAVEEG VVAGGGVALV
     RVAAKLASLT AQNEDQNVGI KVALRAMEAP LRQIVSNAGE EPSVVANNVK AGDGNYGYNA
     ATEEYGNMID FGILDPTKVT RSALQFAASV AGLMITTECM VTDLPKGDAP DLGGAGGMGG