ID   CH101_BRADU             Reviewed;         104 AA.
AC   P77828;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   03-AUG-2022, entry version 119.
DE   RecName: Full=Co-chaperonin GroES 1 {ECO:0000255|HAMAP-Rule:MF_00580};
DE   AltName: Full=10 kDa chaperonin 1 {ECO:0000255|HAMAP-Rule:MF_00580};
DE   AltName: Full=Chaperonin-10 1 {ECO:0000255|HAMAP-Rule:MF_00580};
DE            Short=Cpn10 1 {ECO:0000255|HAMAP-Rule:MF_00580};
GN   Name=groES1 {ECO:0000255|HAMAP-Rule:MF_00580};
GN   Synonyms=groS1 {ECO:0000255|HAMAP-Rule:MF_00580};
GN   OrderedLocusNames=blr5226;
OS   Bradyrhizobium diazoefficiens (strain JCM 10833 / BCRC 13528 / IAM 13628 /
OS   NBRC 14792 / USDA 110).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Bradyrhizobiaceae; Bradyrhizobium.
OX   NCBI_TaxID=224911;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8808920; DOI=10.1128/jb.178.18.5337-5346.1996;
RA   Narberhaus F., Weiglhofer W., Fischer H.-M., Hennecke H.;
RT   "The Bradyrhizobium japonicum rpoH1 gene encoding a sigma 32-like protein
RT   is part of a unique heat shock gene cluster together with groESL1 and three
RT   small heat shock genes.";
RL   J. Bacteriol. 178:5337-5346(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 10833 / BCRC 13528 / IAM 13628 / NBRC 14792 / USDA 110;
RX   PubMed=12597275; DOI=10.1093/dnares/9.6.189;
RA   Kaneko T., Nakamura Y., Sato S., Minamisawa K., Uchiumi T., Sasamoto S.,
RA   Watanabe A., Idesawa K., Iriguchi M., Kawashima K., Kohara M.,
RA   Matsumoto M., Shimpo S., Tsuruoka H., Wada T., Yamada M., Tabata S.;
RT   "Complete genomic sequence of nitrogen-fixing symbiotic bacterium
RT   Bradyrhizobium japonicum USDA110.";
RL   DNA Res. 9:189-197(2002).
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.
CC   -!- SIMILARITY: Belongs to the GroES chaperonin family. {ECO:0000255|HAMAP-
CC       Rule:MF_00580, ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC50491.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; U55047; AAC44752.1; -; Genomic_DNA.
DR   EMBL; BA000040; BAC50491.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; NP_771866.1; NC_004463.1.
DR   RefSeq; WP_028171493.1; NZ_CP011360.1.
DR   AlphaFoldDB; P77828; -.
DR   SMR; P77828; -.
DR   STRING; 224911.27353501; -.
DR   EnsemblBacteria; BAC50491; BAC50491; BAC50491.
DR   GeneID; 64024984; -.
DR   KEGG; bja:blr5226; -.
DR   PATRIC; fig|224911.44.peg.5112; -.
DR   eggNOG; COG0234; Bacteria.
DR   HOGENOM; CLU_132825_1_0_5; -.
DR   InParanoid; P77828; -.
DR   OMA; KGGIMPT; -.
DR   Proteomes; UP000002526; Chromosome.
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   GO; GO:0051087; F:chaperone binding; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IBA:GO_Central.
DR   GO; GO:0051082; F:unfolded protein binding; IBA:GO_Central.
DR   GO; GO:0051085; P:chaperone cofactor-dependent protein refolding; IBA:GO_Central.
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; Reference proteome; Stress response.
FT   CHAIN           1..104
FT                   /note="Co-chaperonin GroES 1"
FT                   /id="PRO_0000174705"
SQ   SEQUENCE   104 AA;  11307 MW;  DB55329D01AE4A6D CRC64;
     MHFRPLHDRV LVRRIDAEEK TAGGIIIPDT AKEKPQEGEI IAAGSGGRNE QGQLIPIDVK
     PGDRVLFGKW SGTEVKIDGQ DYLIMKESDL LGVVDKTGSV KKAA