CH60_TROWH
ID CH60_TROWH Reviewed; 540 AA.
AC P69204; Q9KJC0;
DT 15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 68.
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};
DE AltName: Full=Heat shock protein 65;
GN Name=groEL {ECO:0000255|HAMAP-Rule:MF_00600};
GN Synonyms=groL {ECO:0000255|HAMAP-Rule:MF_00600};
OS Tropheryma whipplei (Whipple's bacillus) (Tropheryma whippelii).
OC Bacteria; Actinobacteria; Micrococcales; Tropherymataceae; Tropheryma.
OX NCBI_TaxID=2039;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Morgenegg S., Drancourt M., Raoult D., Altwegg M.;
RT "Complete sequence of the 'Tropheryma whippelii' hsp65-gene and its use for
RT phylogeny.";
RL Submitted (MAR-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 65-271.
RX PubMed=10834984; DOI=10.1128/jcm.38.6.2248-2253.2000;
RA Morgenegg S., Dutly F., Altwegg M.;
RT "Cloning and sequencing of a part of the heat shock protein 65 gene (hsp65)
RT of 'Tropheryma whippelii' and its use for detection of 'T. whippelii' in
RT clinical specimens by PCR.";
RL J. Clin. Microbiol. 38:2248-2253(2000).
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; AF184091; AAF76292.2; -; Genomic_DNA.
DR RefSeq; WP_011102574.1; NZ_CAUR030000103.1.
DR AlphaFoldDB; P69204; -.
DR SMR; P69204; -.
DR PRIDE; P69204; -.
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..540
FT /note="Chaperonin GroEL"
FT /id="PRO_0000063588"
FT REGION 520..540
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 540 AA; 57014 MW; 58B7CF30699BB50C CRC64;
MAKKITFNED ARRGLERGLN TLADTVKVTL GPRGRNVVLE KKWGAPVITN DGVTIAKEIE
LDDPYEKIGA ELVKEVAKKT DDVAGDGTTT SVVLAQAMVR EGLKNVAAGA DPISLRRGIE
KSVAAVSKAL LTSAKEVETE AEIAACASIS AGDPQIGDII AQALEKVGKE GVVTVEESNT
FGTELEITEG MRFDKGYLSA YFVTDAERQE TVFENPYILI CDSKISSVKD LLPVVDKVIQ
SGKQLLIIAE DVDGEALATL VVNKIRGIFK SVAVKAPGFG DRRKMMLQDI AVLTGGQVIS
EEVGLKLENA TLDLLGRARK VVVSKDETTI VDGAGSSDQI AGRVSQIRKE LENSDSDYDR
EKLQERLAKL SGGVAVIRSG AATEVELKER KHRIEDAVRN AKAAVEEGIV AGGGAALLQS
GTSALKDLQL TSEEAVGRNI VRSAIEAPLR QISLNAGLEP GVVVGKVSSL PQGHGLDAST
GEYVDMLSRG ISDPVKVTRS ALENAASIAG LFLTTEAVVA EKPEPKPAPG PADPGAGMDF
