ID   CH60_ORITS              Reviewed;         555 AA.
AC   P16625;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1990, sequence version 1.
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=58 kDa antigen;
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   AltName: Full=Major antigen 58;
GN   Name=groEL {ECO:0000255|HAMAP-Rule:MF_00600};
GN   Synonyms=groL {ECO:0000255|HAMAP-Rule:MF_00600}, mopA, sta58;
OS   Orientia tsutsugamushi (Rickettsia tsutsugamushi).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Orientia.
OX   NCBI_TaxID=784;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Karp;
RX   PubMed=2108930; DOI=10.1128/iai.58.5.1360-1368.1990;
RA   Stover C.K., Marana D.P., Dasch G.A., Oaks E.V.;
RT   "Molecular cloning and sequence analysis of the Sta58 major antigen gene of
RT   Rickettsia tsutsugamushi: sequence homology and antigenic comparison of
RT   Sta58 to the 60-kilodalton family of stress proteins.";
RL   Infect. Immun. 58:1360-1368(1990).
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; M31887; AAA26393.1; -; Genomic_DNA.
DR   PIR; B41492; B41492.
DR   RefSeq; WP_045912467.1; NZ_LYMT01000068.1.
DR   AlphaFoldDB; P16625; -.
DR   SMR; P16625; -.
DR   STRING; 357244.OTBS_0917; -.
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..555
FT                   /note="Chaperonin GroEL"
FT                   /id="PRO_0000063518"
FT   REGION          528..555
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
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         418
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00600"
FT   BINDING         499
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00600"
SQ   SEQUENCE   555 AA;  59729 MW;  16400249D3FC03B4 CRC64;
     MSKQIVHGDQ CRKKIIEGIN VVANAVGITL GPKGRCVAIE QSYGPPKITK DGVSVAKAIQ
     LKDKSLNVGA QFVISVASKT ADVAGDGTTT ATVIADAAVR ELNKAEVAGI DIQEVRKGAE
     KAVEAVIADV RKNSSPVKNE EEIAQVATVS SNGDREIGEK IANAMKQVGQ EGVITVEDSK
     NFNFEVEVVK GMRFDRGYIS QYFATNREKM ITEFENPYIL LLDQKVSTVQ PLVPVLEAVA
     HTGKPLVLIA DDVDGEALTA LILNNLKGSI KVVAVKAPGF GDRKKEMLED IAILTNGEVI
     TEQLGIKLEK VNDTSKLGTA NRVIVTKDHT TIVHDKNNSD IEKKVNSRCE QIREAIKDTT
     SDYEKEKLQE RLAKLRNGVA VLKVGGATEV EQKERKDRVE DALHATRAAV EEGIVPGGGV
     ALFYASRVLD SLKFDNEDQR VGINIIKKVL EAPVRQIVKN AGGKEDVVVN ELSKSTDKNR
     GFDARTMQYV DMIKAGIVDP TKVVRTALQD AFSVASLVIA TSAMITDHEE DNNTGNRSGG
     GVGGGHHGGM GGMDF