ID   CH60_TANFO              Reviewed;         544 AA.
AC   P81284; Q9X6Y3;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 102.
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}, mopA;
OS   Tannerella forsythia (Bacteroides forsythus).
OC   Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Tannerellaceae;
OC   Tannerella.
OX   NCBI_TaxID=28112;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 43037 / JCM 10827 / FDC 338 / CIP 105219;
RX   PubMed=10524765; DOI=10.3109/10425179809008477;
RA   Reid H.I., Riggio M.P.;
RT   "Identification and nucleotide sequence of the heat shock protein 60
RT   (GroEL) gene of Bacteroides forsythus.";
RL   DNA Seq. 9:359-364(1998).
RN   [2]
RP   PROTEIN SEQUENCE OF 2-40.
RC   STRAIN=ATCC 43037 / JCM 10827 / FDC 338 / CIP 105219;
RA   Sojar H.T., Glurich I.E., Genco R.J.;
RL   Submitted (APR-1998) to UniProtKB.
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; AJ006516; CAB43992.1; -; Genomic_DNA.
DR   AlphaFoldDB; P81284; -.
DR   SMR; P81284; -.
DR   PRIDE; P81284; -.
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   1: Evidence at protein level;
KW   ATP-binding; Chaperone; Cytoplasm; Direct protein sequencing; Isomerase;
KW   Nucleotide-binding.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|Ref.2"
FT   CHAIN           2..544
FT                   /note="Chaperonin GroEL"
FT                   /id="PRO_0000063271"
FT   BINDING         29..32
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00600"
FT   BINDING         50
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         415
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   CONFLICT        4..24
FT                   /note="EIKFDMNARDLLKKGVDELAN -> DVKFGNDARVKMLRGVNVLAD (in
FT                   Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        38..40
FT                   /note="ILE -> VLD (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   544 AA;  57972 MW;  4712157E0349494C CRC64;
     MAKEIKFDMN ARDLLKKGVD ELANAVKVTL GPKGRNVILE KKFGAPQITK DGVTVAKEIE
     LACPYENMGA QLVKEVASKT NDKAGDGTTT ATVLAQAIIG VGLKNVTAGA NPMDLKRGID
     KAVSKVVESI ASQSEAVGTN MDRIEHVAKI SANGDEGIGK LIAEAMQKVK KEGVITVEEA
     KGTETTVEVV EGMQFDRGYI SAYFVTDTEK METQFENPYI LIYDKKISVL KDLLPILEQM
     VQSGRALLII AEDIDSEALA TLVVNRLRGG LKVCAVKAPG FGDRRKAMLE DIAILTGGTV
     ITEEKGMKLE DAKMDMLGSA DKVTVNKDNT TIVKGNGDKA AIESRIGQIK AQIETTTSDY
     DKEKLQERLA KLAGGVAVLY VGAPSEVEMK EKKDRVDDAL HATRAAIEEG TVPGGGVAYL
     RAIPALEGLK GENEDETTGI EIVKRAIEEP LRQIVNNAGK EGAVVVQKVK EGTGAFGYNA
     RTDVYEDLSE AGVVDPAKVT RIALENAASI AGMFLTTECV VADKKEEAPA PPMNPGMGGM
     GGMM