CH60_BIFAA
ID CH60_BIFAA Reviewed; 538 AA.
AC Q9REU4; A1A0W3;
DT 11-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 20-FEB-2007, sequence version 3.
DT 03-AUG-2022, entry version 118.
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}, hsp60;
GN OrderedLocusNames=BAD_0565;
OS Bifidobacterium adolescentis (strain ATCC 15703 / DSM 20083 / NCTC 11814 /
OS E194a).
OC Bacteria; Actinobacteria; Bifidobacteriales; Bifidobacteriaceae;
OC Bifidobacterium.
OX NCBI_TaxID=367928;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Jian W., Dong X.;
RT "Phylogenetic development research of Bifidobacteria through the hsp60
RT gene.";
RL Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15703 / DSM 20083 / NCTC 11814 / E194a;
RA Suzuki T., Tsuda Y., Kanou N., Inoue T., Kumazaki K., Nagano S., Hirai S.,
RA Tanaka K., Watanabe K.;
RT "Bifidobacterium adolescentis complete genome sequence.";
RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
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; AF210319; AAF18475.2; -; Genomic_DNA.
DR EMBL; AP009256; BAF39346.1; -; Genomic_DNA.
DR RefSeq; WP_011743003.1; NC_008618.1.
DR AlphaFoldDB; Q9REU4; -.
DR SMR; Q9REU4; -.
DR STRING; 1680.BADO_0578; -.
DR PRIDE; Q9REU4; -.
DR EnsemblBacteria; BAF39346; BAF39346; BAD_0565.
DR GeneID; 56674649; -.
DR KEGG; bad:BAD_0565; -.
DR HOGENOM; CLU_016503_3_0_11; -.
DR OMA; TDTDKME; -.
DR Proteomes; UP000008702; 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; 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..538
FT /note="Chaperonin GroEL"
FT /id="PRO_0000063286"
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 477..479
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"
FT CONFLICT 533..538
FT /note="GADMGY -> VFPLRRNAGTRRFPAPSSTTRAWLTSNGLMVATSMSTIGCVL
FT AIMRMALK (in Ref. 1; AAF18475)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 538 AA; 56248 MW; 14E866085CB9A77E CRC64;
MAKMIAYDDE ARQGMLAGLD KLADTVKVTL GPKGRNVVLD KTYGAPTITN DGVSIAKEID
LDDPYERIGA ELVKEVAKKT DDVAGDGTTT ATVLAQSLVH EGLKNVTAGS NPIALRRGIE
KAADAIVKEL VAAAKDVETK DQIAATATIS AADPEVGEKI AEALDKVGQD GVVTVEDNNR
FGLDLDFTEG MRFDKGYIAP YFVTNAEDQT AVLEDPYILL TSGKLSSQQD VVHIAELVMK
TGKPLLIIAE DVDGEALPTL ILNNIRGTFK SCAVKAPGFG DRRKAMLQDM AILTGAQVVS
DELGLKLDSV DMSVLGTAKK VIVSKDETTI VSGGGSKEDV AARVAQIRGE IANTDSDYDR
EKLQERLAKL AGGVAVIKVG AATEVEAKER KHRIEDAVRN AKAAIEEGLL PGGGVALIQA
AAKAKDDVKL EGDEATGAAI VFRAVEAPIK QIAENAGLSG DVVIDKVRSL PDGQGLNAAT
NEYEDLLAAG VTDPVKVTRS ALQNAASIAG LFLTTEAVVA NKPEPPAAAP AAGADMGY
