ID   CH102_BRADU             Reviewed;         104 AA.
AC   P35863;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   03-AUG-2022, entry version 122.
DE   RecName: Full=Co-chaperonin GroES 2 {ECO:0000255|HAMAP-Rule:MF_00580};
DE   AltName: Full=10 kDa chaperonin 2 {ECO:0000255|HAMAP-Rule:MF_00580};
DE   AltName: Full=Chaperonin-10 2 {ECO:0000255|HAMAP-Rule:MF_00580};
DE            Short=Cpn10 2 {ECO:0000255|HAMAP-Rule:MF_00580};
GN   Name=groES2 {ECO:0000255|HAMAP-Rule:MF_00580};
GN   Synonyms=groS2 {ECO:0000255|HAMAP-Rule:MF_00580};
GN   OrderedLocusNames=blr6978;
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].
RC   STRAIN=USDA 110spc4;
RX   PubMed=8101485; DOI=10.1002/j.1460-2075.1993.tb05952.x;
RA   Fischer H.-M., Babst M., Kaspar T., Acuna G., Arigoni F., Hennecke H.;
RT   "One member of a gro-ESL-like chaperonin multigene family in Bradyrhizobium
RT   japonicum is co-regulated with symbiotic nitrogen fixation genes.";
RL   EMBO J. 12:2901-2912(1993).
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: Not induced by heat shock.
CC   -!- SIMILARITY: Belongs to the GroES chaperonin family. {ECO:0000255|HAMAP-
CC       Rule:MF_00580, ECO:0000305}.
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DR   EMBL; Z22604; CAA80317.1; -; Genomic_DNA.
DR   EMBL; BA000040; BAC52243.1; -; Genomic_DNA.
DR   PIR; S35308; S35308.
DR   RefSeq; NP_773618.1; NC_004463.1.
DR   RefSeq; WP_011089716.1; NZ_CP011360.1.
DR   AlphaFoldDB; P35863; -.
DR   SMR; P35863; -.
DR   STRING; 224911.27355259; -.
DR   EnsemblBacteria; BAC52243; BAC52243; BAC52243.
DR   GeneID; 64026732; -.
DR   KEGG; bja:blr6978; -.
DR   PATRIC; fig|224911.44.peg.7012; -.
DR   eggNOG; COG0234; Bacteria.
DR   HOGENOM; CLU_132825_1_0_5; -.
DR   InParanoid; P35863; -.
DR   OMA; LGIFEND; -.
DR   PhylomeDB; P35863; -.
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.
FT   CHAIN           1..104
FT                   /note="Co-chaperonin GroES 2"
FT                   /id="PRO_0000174706"
SQ   SEQUENCE   104 AA;  11296 MW;  345A5658EB577579 CRC64;
     MKFRPLHDRV VVKRIDAEEK TAGGIIIPDT VKEKPSQGEV IAVGPGGRDE SGKLIPIDVR
     VGDRVLFGKW SGTEVKIDTQ ELLIMKESDI MGVLADVSSK KKAA