CH60_KLEPN
ID CH60_KLEPN Reviewed; 547 AA.
AC O66026; O66208;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 94.
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 Klebsiella pneumoniae.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX NCBI_TaxID=573;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Cancino-Diaz M.E., Curiel-Quezada E., Cancino-Diaz J.C.,
RA Dominguez-Lopez M.L., Garcia-Latorre E.;
RL Submitted (DEC-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-539.
RC STRAIN=ATCC 13883 / DSM 30104 / JCM 1662 / NBRC 14940 / NCIMB 13281 / NCTC
RC 9633;
RX PubMed=12501307; DOI=10.2323/jgam.43.355;
RA Harada H., Ishikawa H.;
RT "Phylogenetical relationship based on groE genes among phenotypically
RT related Enterobacter, Pantoea, Klebsiella, Serratia, and Erwinia species.";
RL J. Gen. Appl. Microbiol. 43:355-361(1997).
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; U81143; AAC08714.1; -; Genomic_DNA.
DR EMBL; AB008146; BAA25225.1; -; Genomic_DNA.
DR AlphaFoldDB; O66026; -.
DR SMR; O66026; -.
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;
KW Stress response.
FT CHAIN 1..547
FT /note="Chaperonin GroEL"
FT /id="PRO_0000063396"
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 414
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00600"
FT BINDING 478..480
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"
FT CONFLICT 165
FT /note="V -> AM (in Ref. 2; BAA25225)"
FT /evidence="ECO:0000305"
FT CONFLICT 247
FT /note="V -> L (in Ref. 2; BAA25225)"
FT /evidence="ECO:0000305"
FT CONFLICT 371
FT /note="V -> L (in Ref. 2; BAA25225)"
FT /evidence="ECO:0000305"
FT CONFLICT 526
FT /note="S -> G (in Ref. 2; BAA25225)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 547 AA; 57038 MW; 7C11C457C55171A4 CRC64;
MAAKDVKFGN DARVKMLRGV NVLADAVKVT LGPKGRNVVL DKSFGAPTIT KDGVSVAREI
ELEDKFENMG AQMVKEVASK ANDAAGDGTT TATVLAQAIV NEGLKAVAAG MNPMDLKRGI
DKAVLAAVEE LKALSVPCSD SKAIAQVGTI SANSDETVGK LIAEVDKVGK EGVITVEDGT
GLEDELDVVE GMQFDRGYLS PYFINKPDTG AVELESPFIL LADKKISNIR EMLPVLEAVA
KAGKPLVIIA EDVEGEALAT LVVNTMRGIV KVAAVKAPGF GDRRKAMLQD IATLTGGTVI
SEEIGMELEK ATLEDLGQAK RVVINKDTTT IIDGVGEESA IQGRVAQIRK QIEEATSDYD
REKLQERVAK VAGGVAVIKV GAATEVEMKE KKARVDDALH ATRAAVEEGV VAGGGVALVR
VAAKLAGLTG QNEDQNVGIK VALRAMEAPL RQIVSNAGEE PSVVANNVKA GDGNYGYNAA
TEEYGNMIDF GILDPTKVTR SALQYAASVA GLMITTECMV TDLPKSDAPD LGAAGGMGGM
GGMGGMM
