ID   CH60_ANAPH              Reviewed;         541 AA.
AC   O34191; O34337;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 89.
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   Anaplasma phagocytophilum (Ehrlichia phagocytophila).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Anaplasmataceae; Anaplasma; phagocytophilum group.
OX   NCBI_TaxID=948;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Equi, FG, and OS;
RX   PubMed=9230387; DOI=10.1128/jcm.35.8.2087-2092.1997;
RA   Sumner J.W., Nicholson W.L., Massung R.F.;
RT   "PCR amplification and comparison of nucleotide sequences from the groESL
RT   heat shock operon of Ehrlichia species.";
RL   J. Clin. Microbiol. 35:2087-2092(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; U96727; AAB65623.1; -; Genomic_DNA.
DR   EMBL; U96729; AAB65627.1; -; Genomic_DNA.
DR   EMBL; U96730; AAB65629.1; -; Genomic_DNA.
DR   EMBL; U96735; AAB65639.1; -; Genomic_DNA.
DR   AlphaFoldDB; O34191; -.
DR   SMR; O34191; -.
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..>541
FT                   /note="Chaperonin GroEL"
FT                   /id="PRO_0000063260"
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         416
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00600"
FT   BINDING         498
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00600"
FT   NON_TER         541
SQ   SEQUENCE   541 AA;  57548 MW;  1EA51FB835083C46 CRC64;
     MSNTVVTGEV LDKSIREVVR ILEDAVGCTA GPKGLTVAIS KPYGSPEITK DGYKVMKSIK
     PEEPLAAAIA SIITQSASQC NDKVGDGTTT CSILTAKVIE EVSKAKAAGS DIVSIKNGIL
     KAKEAVLTAL MSMRREVEED EIAQVATLSA NGDKNIGSKI AQCVKEVGKD GVITVEESKG
     FKDLEVEKTD GMQFDRGYLS PYFVTNAEKM LVEFENPYIF LTEKKINLVQ SILPILENVA
     RSGRPLLIIA EDVEGEALST LVLNKLRGGL QVAAVKAPGF GDRRKDMLGD IAVIVGAKYV
     VNDELAVKME DIALSDLGTA KSVRITKDAT TIIGSVDSSS ESIASRTNQI KAQIENSSSD
     YDKEKLRERL AKLSGGVAVL KVGGSSEVEV KERKDRVEDA LHATRAAVEE GVVPGGGAAL
     LYALSSLDGL KGKNDDEQWG IDIIRRAACA PIKRIIKNSG SEEAPCVIQH LLKQNDKELI
     YNVDTMNYAN AFTSGVMDPL KVVRIAFDLA VSLAAVFMTL NAVVVDVPSK NDAAGAGAGG
     M