ID   CH60_ELUMP              Reviewed;         542 AA.
AC   B2KD81;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-JUN-2008, sequence version 1.
DT   03-AUG-2022, entry version 73.
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};
GN   OrderedLocusNames=Emin_0924;
OS   Elusimicrobium minutum (strain Pei191).
OC   Bacteria; Elusimicrobia; Elusimicrobia; Elusimicrobiales;
OC   Elusimicrobiaceae; Elusimicrobium.
OX   NCBI_TaxID=445932;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pei191;
RX   PubMed=19270133; DOI=10.1128/aem.02698-08;
RA   Herlemann D.P.R., Geissinger O., Ikeda-Ohtsubo W., Kunin V., Sun H.,
RA   Lapidus A., Hugenholtz P., Brune A.;
RT   "Genomic analysis of 'Elusimicrobium minutum,' the first cultivated
RT   representative of the phylum 'Elusimicrobia' (formerly termite group 1).";
RL   Appl. Environ. Microbiol. 75:2841-2849(2009).
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; CP001055; ACC98477.1; -; Genomic_DNA.
DR   RefSeq; WP_012415092.1; NC_010644.1.
DR   AlphaFoldDB; B2KD81; -.
DR   SMR; B2KD81; -.
DR   STRING; 445932.Emin_0924; -.
DR   PRIDE; B2KD81; -.
DR   EnsemblBacteria; ACC98477; ACC98477; Emin_0924.
DR   KEGG; emi:Emin_0924; -.
DR   HOGENOM; CLU_016503_3_0_0; -.
DR   OMA; TDTDKME; -.
DR   OrthoDB; 265347at2; -.
DR   Proteomes; UP000001029; Chromosome.
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; 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.
PE   3: Inferred from homology;
KW   ATP-binding; Chaperone; Cytoplasm; Isomerase; Nucleotide-binding;
KW   Reference proteome.
FT   CHAIN           1..542
FT                   /note="Chaperonin GroEL"
FT                   /id="PRO_1000130014"
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         493
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00600"
SQ   SEQUENCE   542 AA;  57622 MW;  35BA619E28FE9870 CRC64;
     MAKQIVYGDE ARAKMKAGIE KVAKAVSVTL GPKGRSVVLE KKFGSPLIID DGVTIAKDIE
     LEDKFENMGA QLIREVASKT NDIAGDGTTT ATVLTHAILT EGIKNITAGA NPTLVKKGIE
     MAVETVKEEL KKMQRPVETK EEKAQIATIS ANDRMVGELI AEAMEKVGHE GVITVEEGKT
     ATTELQVVEG MQFDRGYISP YFVTDSERME CVLEDCQIIL ADKKVSSMNE LLPLLEGIVK
     NGRNFLIIAE DVDGEALATL VVNRLRGTLK GCAVKAPGFG DRRKEMLEDI AILTGGQVIA
     EERGMKLETA TLDMLGSAKR VVIDKENATI VSGEGDKKKI EARAEQIRKQ IENSTSDYDK
     EKLQERLAKL SGGVAVISVG AATETEMKAK KAKVEDAKNA TKAGVEEGLI PGGGVALTRC
     EGAVGKLKAD NEDVQTGINI VKKALTAPLY QIAFNAGLDG SVVVENVRNA KGNQGFDADT
     GEYVDMIKAG VVDAVKVVRI GLENAASIAA TVLLTEALVA DIPEEKGAAP MGHPGMGGMG
     MM