ID   CH60_OLEAN              Reviewed;         548 AA.
AC   Q8KM30;
DT   25-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   03-AUG-2022, entry version 78.
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=cpn60, groL {ECO:0000255|HAMAP-Rule:MF_00600};
OS   Oleispira antarctica.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC   Oceanospirillaceae; Oleispira.
OX   NCBI_TaxID=188908;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=DSM 14852 / LMG 21398 / RB-8;
RA   Ferrer M., Lunsdorf H., Chernikova T.N., Yakimov M.M., Golyshin P.N.,
RA   Timmis K.N.;
RT   "Cold-adapted chaperonins, Cpn60 and Cpn10 from the hydrocarbonoclastic
RT   psychrophile, Oleispira antarctica RB8, and their ability to interact with
RT   a non-native 102 kDa carboxylesterase.";
RL   Submitted (AUG-2002) 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; AJ505131; CAD43724.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8KM30; -.
DR   SMR; Q8KM30; -.
DR   PRIDE; Q8KM30; -.
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..548
FT                   /note="Chaperonin GroEL"
FT                   /id="PRO_0000063466"
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         494
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00600"
SQ   SEQUENCE   548 AA;  56872 MW;  7AE998CC84E47AE2 CRC64;
     MAAKDVLFGD SARAKMLVGV NILADAVRVT LGPKGRNVVI EKSFGAPIIT KDGVSVAREI
     ELKDKFENMG AQMVKEVASQ ANDQAGDGTT TATVLAQAII SEGLKSVAAG MNPMDLKRGI
     DKATAAVVAA IKEQAQPCLD TKAIAQVGTI SANADETVGR LIAEAMEKVG KEGVITVEEG
     KGLEDELDVV EGMQFDRGYL SPYFINNQEK MTVEMENPLI LLVDKKIDNL QELLPILENV
     AKSGRPLLIV AEDVEGQALA TLVVNNLRGT FKVAAVKAPG FGDRRKAMLQ DLAILTGGQV
     ISEELGMSLE TADPSSLGTA SKVVIDKENT VIVDGAGTEA SVNTRVDQIR AEIESSTSDY
     DIEKLQERVA KLAGGVAVIK VGAGSEMEMK EKKDRVDDAL HATRAAVEEG VVAGGGVALI
     RALSSVTVVG DNEDQNVGIA LALRAMEAPI RQIAGNAGAE GSVVVDKVKS GTGSFGFNAS
     TGEYGDMIAM GILDPAKVTR SSLQAAASIA GLMITTEAMV ADAPVEEGAG GMPDMGGMGG
     MGGMPGMM