CH60_BORBU
ID CH60_BORBU Reviewed; 545 AA.
AC P0C923; P27575;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 1.
DT 03-AUG-2022, entry version 72.
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;
GN OrderedLocusNames=BB_0649;
OS Borreliella burgdorferi (strain ATCC 35210 / DSM 4680 / CIP 102532 / B31)
OS (Borrelia burgdorferi).
OC Bacteria; Spirochaetes; Spirochaetales; Borreliaceae; Borreliella.
OX NCBI_TaxID=224326;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1709664;
RA Hindersson P., Hansen K.;
RT "T cell and antibody reactivity with the Borrelia burgdorferi 60-kDa heat
RT shock protein in Lyme arthritis.";
RL J. Immunol. 146:3985-3992(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35210 / DSM 4680 / CIP 102532 / B31;
RX PubMed=9403685; DOI=10.1038/37551;
RA Fraser C.M., Casjens S., Huang W.M., Sutton G.G., Clayton R.A.,
RA Lathigra R., White O., Ketchum K.A., Dodson R.J., Hickey E.K., Gwinn M.L.,
RA Dougherty B.A., Tomb J.-F., Fleischmann R.D., Richardson D.L.,
RA Peterson J.D., Kerlavage A.R., Quackenbush J., Salzberg S.L., Hanson M.,
RA van Vugt R., Palmer N., Adams M.D., Gocayne J.D., Weidman J.F.,
RA Utterback T.R., Watthey L., McDonald L.A., Artiach P., Bowman C.,
RA Garland S.A., Fujii C., Cotton M.D., Horst K., Roberts K.M., Hatch B.,
RA Smith H.O., Venter J.C.;
RT "Genomic sequence of a Lyme disease spirochaete, Borrelia burgdorferi.";
RL Nature 390:580-586(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; X54059; CAA37994.1; -; Genomic_DNA.
DR EMBL; AE000783; AAC66995.1; -; Genomic_DNA.
DR PIR; H70180; H70180.
DR RefSeq; NP_212783.1; NC_001318.1.
DR RefSeq; WP_002657108.1; NC_001318.1.
DR AlphaFoldDB; P0C923; -.
DR SMR; P0C923; -.
DR STRING; 224326.BB_0649; -.
DR EnsemblBacteria; AAC66995; AAC66995; BB_0649.
DR GeneID; 56567459; -.
DR KEGG; bbu:BB_0649; -.
DR PATRIC; fig|224326.49.peg.1040; -.
DR HOGENOM; CLU_016503_3_0_12; -.
DR OMA; TDTDKME; -.
DR Proteomes; UP000001807; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:CAFA.
DR GO; GO:0016020; C:membrane; IDA:CAFA.
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 Reference proteome.
FT CHAIN 1..545
FT /note="Chaperonin GroEL"
FT /id="PRO_0000063290"
FT BINDING 29..32
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00600"
FT BINDING 50
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 495
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00600"
FT CONFLICT 124
FT /note="N -> S (in Ref. 1; CAA37994)"
FT /evidence="ECO:0000305"
FT CONFLICT 213
FT /note="N -> S (in Ref. 1; CAA37994)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 545 AA; 58952 MW; 568BA8E5B4835719 CRC64;
MAKDIYFNED ARKSLLSGVE KLSNAVKVTL GPKGRNVLID KKFGSPTVTK DGVSVAREIE
LENPFENMGA QLLKEVAIKT NDVAGDGTTT ATVLAYAIAR EGLKNVSSGI NPIGIKKGID
HAVNLAAEKI RQSAKKITTK EEIAQVASIS ANNDSYIGEK IAEAMDKVGK DGVITVEESK
TFDTTISYVE GMQFDRGYLS PYFSTNKENM SVNFDDAFIL IYEKKISSIK ELLPVLEKVL
GTNKPLLIIA EDIEGDALAA LVLNSVRGAL KVCAIKSPGF GDRRKAMLED IAVLTGGVLI
SEELGLTLET VEIEQLGQAK TIKVDKDNTT IINTGNKEQI KERSELIKKQ IEDSTSEYDK
EKLQERLAKL VGGVAVINVG AVTEVELKEK KHRVEDALSA TRAAVEEGVV PGGGSTLIEV
AMYLDTIDTS KLSYEEKQGF EIVKRSLEEP MRQIISNAGF EGSIYIHQIK TEKKGLGFDA
SSFKWVNMIE SGIIDPAKVT RSALQNAASI AGLLLTTECA ITDIKEEKNT SGGGGYPMDP
GMGMM
