ID   CH60_HOLOB              Reviewed;         554 AA.
AC   P94820;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   03-AUG-2022, entry version 90.
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}, mopA;
OS   Holospora obtusa.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Holosporales; Holosporaceae;
OC   Holospora.
OX   NCBI_TaxID=49893;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9495035; DOI=10.1111/j.1550-7408.1998.tb05072.x;
RA   Dohra H., Fujishima M., Ishikawa H.;
RT   "Structure and expression of a GroE-homologous operon of a macronucleus-
RT   specific symbiont Holospora obtusa of the ciliate Paramecium caudatum.";
RL   J. Eukaryot. Microbiol. 45:71-79(1998).
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; D89970; BAA14046.1; -; Genomic_DNA.
DR   AlphaFoldDB; P94820; -.
DR   SMR; P94820; -.
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..554
FT                   /note="Chaperonin GroEL"
FT                   /id="PRO_0000063391"
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         416
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00600"
FT   BINDING         503
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00600"
SQ   SEQUENCE   554 AA;  59159 MW;  5CCB9866F5AA2F08 CRC64;
     MSVKQIAFGS KVGESLLNGV IKLANCVQVT LGPNGRNVLI EQSFGDPRVT KDGVTVAKHV
     ELEDRYENLA AQLVKSVASK TADMVGDGTT TATVLARSIY SEAFKGTSAG MNSMELRAGI
     DHAVEIVVEK LKELSIPVKG DYQKISQVAT VSANGDTEIG DMIAQAMEKV GSDGVITVEE
     AKSFKTELDV VPGMQFDRGY ISPYFITRQD KGIAELERSY ILLYDGKISS AQSLLPVLEK
     CAKESASLLI IAEDVEGEAL RMLVVNKLRG VLKVAAVKSP GFGDRRKAML GDIAVLTNGY
     VVSSEVGMRL EDVRIEDLGR ADTIVIEKDN TTVIVNGPAR SSVKERCDKI RSEIQEATSD
     YDKEKLQERL AKLSGGVAVI RVGGATEVEL KERKDRVEDA MHATKAAVEE GIIPGGGTAF
     LRCVKPLEEV IKSAKVQERG RDFICGIDAV RKALSSPCYQ IASNAGKEGG VVVAEVLKAS
     DVNVGYDARH DQYVDMIKSG IIDPTKVART ALQNAGSVAG LLNTTEVIIA QVPEKEKPNM
     GGGMGGGMGG GMDF