ID   CH60_SCAIO              Reviewed;         538 AA.
AC   Q9EY76;
DT   11-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2001, sequence version 2.
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}, hsp60;
OS   Scardovia inopinata (Bifidobacterium inopinatum).
OC   Bacteria; Actinobacteria; Bifidobacteriales; Bifidobacteriaceae; Scardovia.
OX   NCBI_TaxID=78259;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=DSM 10107 / NCTC 12937 / CCUG 35729 / B3109;
RX   PubMed=12557349;
RA   Jian W., Dong X.;
RT   "Amplification of bacterial heat shock protein 60 gene using inverse PCR
RT   method.";
RL   Wei Sheng Wu Xue Bao 42:56-61(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; AY004281; AAF89506.2; -; Genomic_DNA.
DR   AlphaFoldDB; Q9EY76; -.
DR   SMR; Q9EY76; -.
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..538
FT                   /note="Chaperonin GroEL"
FT                   /id="PRO_0000063523"
FT   BINDING         29..32
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         413
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00600"
FT   BINDING         477..479
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00600"
FT   BINDING         493
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00600"
SQ   SEQUENCE   538 AA;  56613 MW;  48AFAF1DE86FD1D8 CRC64;
     MAKIIKYDEE ARQGMLEGLD ELANTVKVTL GPRGRNVVLD KTYGAPTITN DGVSIAKEID
     LEDPYARIGA ELVKEVAKKT DDVAGDGTTT ATVLAQSLVH EGLRNVTAGS NPIALRRGIE
     KASDAIVERL LSNAKPVETK EQIAATATIS AGDPEVGDKI AEALDKVGQD GVVTVEDNNK
     FGLDLEFTEG MRFDKGYISP YFVTNADEQT AVLEDPYILL TSGKVSSQQD IVHIAELVMK
     SGKPLLIVAE DVDGEALPTL VLNKIRGTFN TVAVKAPGFG DRRKAMLQDM AILTGAQVVS
     DELGLKLDSI DDTVFGHASK VIVSKDETTI VSGAGSKEDV AARVAQIRSE IEDSDSDYDR
     EKLQERLAKL AGGVAVIKVG AATEVEAKER KHRIEDAVRN AKAAIEEGLL PGGGVALVQA
     AADVQKNVKL EGDEATGAGI VFRAIEAPLK QIAQNAGFSG EVVIDKVRTL PAGSGLNAAT
     GEYEDLLSAG VTDPVKVTRS ALQNAASIAG LFLTTEAVVA NKPEPPAPAA APNPDMGY