CH60_BRUA1
ID CH60_BRUA1 Reviewed; 546 AA.
AC B2SCZ4; P25967; Q579Q0;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-2008, sequence version 1.
DT 03-AUG-2022, entry version 78.
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};
GN OrderedLocusNames=BAbS19_II01790;
OS Brucella abortus (strain S19).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX NCBI_TaxID=430066;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1347461; DOI=10.1016/0167-4781(92)90476-g;
RA Gor D., Mayfield J.E.;
RT "Cloning and nucleotide sequence of the Brucella abortus groE operon.";
RL Biochim. Biophys. Acta 1130:120-122(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION.
RX PubMed=1350274; DOI=10.1128/iai.60.6.2425-2431.1992;
RA Lin J., Adams L.G., Ficht T.A.;
RT "Characterization of the heat shock response in Brucella abortus and
RT isolation of the genes encoding the GroE heat shock proteins.";
RL Infect. Immun. 60:2425-2431(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S19;
RX PubMed=18478107; DOI=10.1371/journal.pone.0002193;
RA Crasta O.R., Folkerts O., Fei Z., Mane S.P., Evans C., Martino-Catt S.,
RA Bricker B., Yu G., Du L., Sobral B.W.;
RT "Genome sequence of Brucella abortus vaccine strain S19 compared to
RT virulent strains yields candidate virulence genes.";
RL PLoS ONE 3:E2193-E2193(2008).
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 -!- INDUCTION: By heat shock. {ECO:0000269|PubMed:1350274}.
CC -!- SIMILARITY: Belongs to the chaperonin (HSP60) family.
CC {ECO:0000255|HAMAP-Rule:MF_00600}.
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DR EMBL; M82975; AAA22997.1; -; Genomic_DNA.
DR EMBL; M83930; AAA22995.1; -; Genomic_DNA.
DR EMBL; CP000888; ACD73698.1; -; Genomic_DNA.
DR PIR; B43827; B43827.
DR PIR; S22347; S22347.
DR RefSeq; WP_002966387.1; NC_010740.1.
DR AlphaFoldDB; B2SCZ4; -.
DR SMR; B2SCZ4; -.
DR EnsemblBacteria; ACD73698; ACD73698; BAbS19_II01790.
DR GeneID; 3828243; -.
DR KEGG; bmc:BAbS19_II01790; -.
DR HOGENOM; CLU_016503_3_0_5; -.
DR OMA; TDTDKME; -.
DR Proteomes; UP000002565; Chromosome 2.
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 2: Evidence at transcript level;
KW ATP-binding; Chaperone; Cytoplasm; Isomerase; Nucleotide-binding.
FT CHAIN 1..546
FT /note="Chaperonin GroEL"
FT /id="PRO_1000129982"
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 415
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 35..36
FT /note="GR -> A (in Ref. 2; AAA22995)"
FT /evidence="ECO:0000305"
FT CONFLICT 154
FT /note="G -> A (in Ref. 1; AAA22997 and 2; AAA22995)"
FT /evidence="ECO:0000305"
FT CONFLICT 155..157
FT /note="EAE -> KQ (in Ref. 2; AAA22995)"
FT /evidence="ECO:0000305"
FT CONFLICT 258
FT /note="A -> R (in Ref. 2; AAA22995)"
FT /evidence="ECO:0000305"
FT CONFLICT 278
FT /note="A -> R (in Ref. 2; AAA22995)"
FT /evidence="ECO:0000305"
FT CONFLICT 287
FT /note="A -> R (in Ref. 2; AAA22995)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 546 AA; 57515 MW; 2E403D8CC121A30A CRC64;
MAAKDVKFGR TAREKMLRGV DILADAVKVT LGPKGRNVVI EKSFGAPRIT KDGVSVAKEV
ELEDKFENMG AQMLREVASK TNDTAGDGTT TATVLGQAIV QEGAKAVAAG MNPMDLKRGI
DLAVNEVVAE LLKKAKKINT SEEVAQVGTI SANGEAEIGK MIAEAMQKVG NEGVITVEEA
KTAETELEVV EGMQFDRGYL SPYFVTNPEK MVADLEDAYI LLHEKKLSNL QALLPVLEAV
VQTSKPLLII AEDVEGEALA TLVVNKLRGG LKIAAVKAPG FGDRRKAMLE DIAILTGGQV
ISEDLGIKLE SVTLDMLGRA KKVSISKENT TIVDGAGQKA EIDARVGQIK QQIEETTSDY
DREKLQERLA KLAGGVAVIR VGGATEVEVK EKKDRVDDAL NATRAAVEEG IVAGGGTALL
RASTKITAKG VNADQEAGIN IVRRAIQAPA RQITTNAGEE ASVIVGKILE NTSETFGYNT
ANGEYGDLIS LGIVDPVKVV RTALQNAASV AGLLITTEAM IAELPKKDAA PAGMPGGMGG
MGGMDF
