ID CH60_BIFAS Reviewed; 537 AA.
AC Q93M78; C6AHY9;
DT 11-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 22-SEP-2009, sequence version 2.
DT 27-MAR-2024, entry version 107.
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=Balat_0656;
OS Bifidobacterium animalis subsp. lactis (strain DSM 10140 / JCM 10602 / LMG
OS 18314).
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=555970;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=12557349;
RA Jian W., Dong X.;
RT "Amplification of bacterial heat shock protein 60 gene using inverse PCR
RT method.";
RL Wei Sheng Wu Xue Bao 42:56-61(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10140 / JCM 10602 / LMG 18314;
RX PubMed=19376856; DOI=10.1128/jb.00155-09;
RA Barrangou R., Briczinski E.P., Traeger L.L., Loquasto J.R., Richards M.,
RA Horvath P., Coute-Monvoisin A.-C., Leyer G., Rendulic S., Steele J.L.,
RA Broadbent J.R., Oberg T., Dudley E.G., Schuster S., Romero D.A.,
RA Roberts R.F.;
RT "Comparison of the complete genome sequences of Bifidobacterium animalis
RT subsp. lactis DSM 10140 and Bl-04.";
RL J. Bacteriol. 191:4144-4151(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; AY004282; AAF89507.2; -; Genomic_DNA.
DR EMBL; CP001606; ACS47596.1; -; Genomic_DNA.
DR RefSeq; WP_004218937.1; NC_012815.1.
DR AlphaFoldDB; Q93M78; -.
DR SMR; Q93M78; -.
DR GeneID; 66533009; -.
DR KEGG; blt:Balat_0656; -.
DR HOGENOM; CLU_016503_3_0_11; -.
DR BioCyc; BANI555970:G1GVE-677-MONOMER; -.
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; 3.50.7.10; GroEL; 1.
DR Gene3D; 1.10.560.10; GroEL-like equatorial domain; 1.
DR Gene3D; 3.30.260.10; TCP-1-like chaperonin intermediate domain; 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 NCBIfam; TIGR02348; GroEL; 1.
DR PANTHER; PTHR45633; 60 KDA HEAT SHOCK PROTEIN, MITOCHONDRIAL; 1.
DR PANTHER; PTHR45633:SF3; 60 KDA HEAT SHOCK PROTEIN, MITOCHONDRIAL; 1.
DR Pfam; PF00118; Cpn60_TCP1; 1.
DR PRINTS; PR00298; CHAPERONIN60.
DR SUPFAM; SSF52029; GroEL apical domain-like; 1.
DR SUPFAM; SSF48592; GroEL equatorial domain-like; 1.
DR SUPFAM; SSF54849; GroEL-intermediate domain like; 1.
DR PROSITE; PS00296; CHAPERONINS_CPN60; 1.
PE 3: Inferred from homology;
KW ATP-binding; Chaperone; Cytoplasm; Isomerase; Nucleotide-binding.
FT CHAIN 1..537
FT /note="Chaperonin GroEL"
FT /id="PRO_0000063287"
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 394
FT /note="I -> T (in Ref. 1; AAF89507)"
FT /evidence="ECO:0000305"
FT CONFLICT 533..534
FT /note="QD -> HN (in Ref. 1; AAF89507)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 537 AA; 56438 MW; 784D06124C05A9D3 CRC64;
MAKIIEYDEE ARQGMLAGLD KLADTVKVTL GPKGRNVVLD KTYGAPTITN DGVSIAKEID
LEDPFERIGA ELVKEVAKRT DDVAGDGTTT ATVLAQSLVH EGLKNVVAGS NPIALRRGIE
KASDALVKQL VASAKPVETK EQIAATATIS AGDPEVGEKI AEALDKVGQD GVVTVEDNNR
FGLDLDFTEG MRFDKGYISP YFVTNAEDQT AVLDDPYILL TSSKVSSQQD VVHIAELVMK
TGKPLLIVAE DVDGEALPTL ILNNIRGTFK SCAVKAPGFG DRRKAMLQDM AILTGGQVVS
EDLGLKLDSI DLSVFGTAKK VIVSKDETTI VSGGGSKEDV AARVAQIRAE IEKTDSDYDR
EKLQERLAKL AGGVAVIKVG AATEVEAKER KHRIEDAVRN AKAAIEEGLV PGGGVALVQA
AEKVEKDFNL EGDEATGAAI VFSGIEAPIK QIAENAGLSG AVVIDKVRSL PEGEGFNAAT
DTYEDLMAAG VTDPVKVTRS ALQNAASIAG LFLTTEAVVA NKPEPAAAPA AGQDMGY
//
