ID   CH10_BRUA1              Reviewed;          98 AA.
AC   B2SCZ5; P0A344; P25968; Q579P9;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-2008, sequence version 1.
DT   03-AUG-2022, entry version 73.
DE   RecName: Full=Co-chaperonin GroES {ECO:0000255|HAMAP-Rule:MF_00580};
DE   AltName: Full=10 kDa chaperonin {ECO:0000255|HAMAP-Rule:MF_00580};
DE   AltName: Full=Chaperonin-10 {ECO:0000255|HAMAP-Rule:MF_00580};
DE            Short=Cpn10 {ECO:0000255|HAMAP-Rule:MF_00580};
GN   Name=groES {ECO:0000255|HAMAP-Rule:MF_00580};
GN   Synonyms=groS {ECO:0000255|HAMAP-Rule:MF_00580};
GN   OrderedLocusNames=BAbS19_II01800;
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 the chaperonin GroEL, plays an essential role
CC       in assisting protein folding. The GroEL-GroES system forms a nano-cage
CC       that allows encapsulation of the non-native substrate proteins and
CC       provides a physical environment optimized to promote and accelerate
CC       protein folding. GroES binds to the apical surface of the GroEL ring,
CC       thereby capping the opening of the GroEL channel. {ECO:0000255|HAMAP-
CC       Rule:MF_00580}.
CC   -!- SUBUNIT: Heptamer of 7 subunits arranged in a ring. Interacts with the
CC       chaperonin GroEL. {ECO:0000255|HAMAP-Rule:MF_00580}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00580}.
CC   -!- INDUCTION: By heat shock. {ECO:0000269|PubMed:1350274}.
CC   -!- SIMILARITY: Belongs to the GroES chaperonin family. {ECO:0000255|HAMAP-
CC       Rule:MF_00580}.
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DR   EMBL; M82975; AAA22996.1; -; Genomic_DNA.
DR   EMBL; M83930; AAA22994.1; -; Genomic_DNA.
DR   EMBL; CP000888; ACD73699.1; -; Genomic_DNA.
DR   PIR; A43827; A43827.
DR   RefSeq; WP_002966386.1; NC_010740.1.
DR   AlphaFoldDB; B2SCZ5; -.
DR   SMR; B2SCZ5; -.
DR   EnsemblBacteria; ACD73699; ACD73699; BAbS19_II01800.
DR   GeneID; 45053273; -.
DR   GeneID; 55591911; -.
DR   KEGG; bmc:BAbS19_II01800; -.
DR   HOGENOM; CLU_132825_1_0_5; -.
DR   OMA; EVKYSGE; -.
DR   Proteomes; UP000002565; Chromosome 2.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR   CDD; cd00320; cpn10; 1.
DR   Gene3D; 2.30.33.40; -; 1.
DR   HAMAP; MF_00580; CH10; 1.
DR   InterPro; IPR020818; Chaperonin_GroES.
DR   InterPro; IPR037124; Chaperonin_GroES_sf.
DR   InterPro; IPR018369; Chaprnonin_Cpn10_CS.
DR   InterPro; IPR011032; GroES-like_sf.
DR   PANTHER; PTHR10772; PTHR10772; 1.
DR   Pfam; PF00166; Cpn10; 1.
DR   PRINTS; PR00297; CHAPERONIN10.
DR   SMART; SM00883; Cpn10; 1.
DR   SUPFAM; SSF50129; SSF50129; 1.
DR   PROSITE; PS00681; CHAPERONINS_CPN10; 1.
PE   2: Evidence at transcript level;
KW   Chaperone; Cytoplasm; Stress response.
FT   CHAIN           1..98
FT                   /note="Co-chaperonin GroES"
FT                   /id="PRO_1000129631"
SQ   SEQUENCE   98 AA;  10393 MW;  77BCA37410612716 CRC64;
     MADIKFRPLH DRVVVRRVES EAKTAGGIII PDTAKEKPQE GEVVAAGAGA RDEAGKLVPL
     DVKAGDRVLF GKWSGTEVKI GGEDLLIMKE SDILGIVG