ID   CH60_MYCXE              Reviewed;         120 AA.
AC   Q50852;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   03-AUG-2022, entry version 76.
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=65 kDa heat shock protein;
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   Mycobacterium xenopi.
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=1789;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=263;
RX   PubMed=7848059;
RA   Kapur V., Li L.L., Hamrick M.R., Plikaytis B.B., Shinnick T.M., Telenti A.,
RA   Jacobs W.R. Jr., Banerjee A., Cole S., Yuen K.Y., Clarridge J.E.,
RA   Kreiswirth B.N., Musser J.M.;
RT   "Rapid Mycobacterium species assignment and unambiguous identification of
RT   mutations associated with antimicrobial resistance in Mycobacterium
RT   tuberculosis by automated DNA sequencing.";
RL   Arch. Pathol. Lab. Med. 119:131-138(1995).
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, ECO:0000305}.
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DR   EMBL; U17959; AAB39078.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q50852; -.
DR   SMR; Q50852; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.560.10; -; 1.
DR   Gene3D; 3.30.260.10; -; 1.
DR   InterPro; IPR002423; Cpn60/GroEL/TCP-1.
DR   InterPro; IPR027413; GROEL-like_equatorial_sf.
DR   InterPro; IPR027410; TCP-1-like_intermed_sf.
DR   Pfam; PF00118; Cpn60_TCP1; 1.
DR   SUPFAM; SSF48592; SSF48592; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Chaperone; Cytoplasm; Isomerase; Nucleotide-binding;
KW   Stress response.
FT   CHAIN           <1..>120
FT                   /note="Chaperonin GroEL"
FT                   /id="PRO_0000063455"
FT   BINDING         23..27
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00600"
FT   NON_TER         1
FT   NON_TER         120
SQ   SEQUENCE   120 AA;  12393 MW;  5FB79564E7CBE0DC CRC64;
     PYEKIGAELV KEVAKKTDDV AGDGTTTATV LAQALVKEGL RNVAAGANPL ALKRGIEKAV
     EKVTETLLKT AKEVETKEQI AATAAISAGD QAIGDLIAEA MDKVGNEGVI TVEESNTFGL