ID   CH60_FUSNP              Reviewed;         539 AA.
AC   Q8GJ00;
DT   11-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 82.
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}, hsp60;
OS   Fusobacterium nucleatum subsp. polymorphum.
OC   Bacteria; Fusobacteria; Fusobacteriales; Fusobacteriaceae; Fusobacterium.
OX   NCBI_TaxID=76857;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 10953 / DSM 20482 / CCUG 9126 / JCM 12990 / NCTC 10562 / 555A;
RA   Skar C.K., Bolstad A., Bakken V.;
RT   "Genes encoding heat shock proteins 10 and 60 from Fusobacterium nucleatum
RT   ATCC 10953.";
RL   Submitted (JUL-2001) 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: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; AJ320160; CAC86118.1; -; Genomic_DNA.
DR   RefSeq; WP_005897776.1; NZ_LN831027.1.
DR   AlphaFoldDB; Q8GJ00; -.
DR   SMR; Q8GJ00; -.
DR   STRING; 76857.RO02_02155; -.
DR   GeneID; 45635341; -.
DR   PATRIC; fig|76857.9.peg.1532; -.
DR   OrthoDB; 265347at2; -.
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..539
FT                   /note="Chaperonin GroEL"
FT                   /id="PRO_0000063379"
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   539 AA;  57552 MW;  E300F0AD2CAC8960 CRC64;
     MAKIINFNDE ARKKLEIGVN TLADAVKVTL GPRGRNVVLE KSYGAPLITN DGVTIAKEIE
     LEDPFENMGA ALVKEVAIKS NDVAGDGTTT ATILAQAIVK EGLKMLSAGA NPIFLKKGIE
     LAAKEAIDVL KDKAKKIESN EEISQVASIS AGDEEIGKLI AQAMAKVGET GVITVEEAKS
     LETTLETVEG MQFDKGYVSP YMVTDSERMT AELDNPLILL TDKKISSMKE LLPLLEQTVQ
     MSKPVLIVAD DIEGEALTTL VINKLRGTLN VVAVKAPAFG DRRKAILEDI AILTGGEVIS
     EEKGMKLEEA TIQQLGKAKT VKVTKDLTVI VDGGGEQKDI SARVNSIKAQ IEETTSDYDK
     EKLQERLAKL SGGVAVIKVG AATEVEMKDK KLRIEDALNA TRAAVEEGIV AGGGTILLDI
     IESMKDFNET GEIAMGIEIV KRALEAPIKQ IAENCGLNGG VVLEKVRMSP KGFGFDAKNE
     KYVNMIECGI IDPAKVTRAA IQNSTSVASL LLTTEVVIAN KKEEEKAPMG AGGMMPGMM