ID   CH60_TREPR              Reviewed;         542 AA.
AC   Q8KTS0;
DT   25-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   03-AUG-2022, entry version 80.
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};
OS   Tremblaya princeps.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Candidatus Tremblaya.
OX   NCBI_TaxID=189385;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=12088995; DOI=10.1128/aem.68.7.3198-3205.2002;
RA   Baumann L., Thao M.L., Hess J.M., Johnson M.W., Baumann P.;
RT   "The genetic properties of the primary endosymbionts of mealybugs differ
RT   from those of other endosymbionts of plant sap-sucking insects.";
RL   Appl. Environ. Microbiol. 68:3198-3205(2002).
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; AF481102; AAM75978.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8KTS0; -.
DR   SMR; Q8KTS0; -.
DR   STRING; 1053648.TCP_023; -.
DR   PRIDE; Q8KTS0; -.
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..542
FT                   /note="Chaperonin GroEL"
FT                   /id="PRO_0000063325"
FT   BINDING         30..33
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00600"
FT   BINDING         51
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00600"
FT   BINDING         87..91
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         480..482
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00600"
FT   BINDING         496
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00600"
SQ   SEQUENCE   542 AA;  57269 MW;  89FA39F2B8C35BE5 CRC64;
     MPAKDVIFGD CARLRLMEGV NTLTDAVKVT LGPKGRNVVL ERSYGSPAVT KDGVTVAKDI
     ELRDRLQNMG AQMVKEVAAK TSDNAGDGTT TATVLAQSIV REGMRYVASG VNPMDIKRGI
     DQAVSSAVME LKKISRPCTT GKEIAQVGSV SANNDRTVGE MIAEAMNKVG KEGVITVEDG
     KSLADELEVV EGMQFDRGYL SPYFINNPDR QVAVLDSPFV LLCEKKVASI RDLLPIMERV
     AKAGRPLLIV AEDVEGEALA TLVVNNARGI LKAAAVKAPG FGDRRKAMLQ DIAILTGGHV
     VSEETGLSLE KVSLPELGQA KRAEVAKDTT TIIDGAGDAK AINARIKHIR LQIEEAASDY
     DKEKLQERVA KLAGGVAVIR VGAATEVEMK EKKARVEDAL HATRAAVEEG IVPGGGVALI
     RARNAISNLR CDNPDQDAGI RIVLRAMEEP LRQIVANGGE EASVVASSVA SGKSISYGYN
     AAMRVYGDLM DAGVVDPTKV TRSALQNAAS VAGLMLTTDV AVCDSPKREE AAPTQPVHGG
     VG