ID   CH10_ALKHC              Reviewed;          94 AA.
AC   O50304;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2000, sequence version 2.
DT   03-AUG-2022, entry version 125.
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}, mopB;
GN   OrderedLocusNames=BH0561;
OS   Alkalihalobacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344
OS   / JCM 9153 / C-125) (Bacillus halodurans).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Alkalihalobacillus.
OX   NCBI_TaxID=272558;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125;
RX   PubMed=11058132; DOI=10.1093/nar/28.21.4317;
RA   Takami H., Nakasone K., Takaki Y., Maeno G., Sasaki R., Masui N., Fuji F.,
RA   Hirama C., Nakamura Y., Ogasawara N., Kuhara S., Horikoshi K.;
RT   "Complete genome sequence of the alkaliphilic bacterium Bacillus halodurans
RT   and genomic sequence comparison with Bacillus subtilis.";
RL   Nucleic Acids Res. 28:4317-4331(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 7-94.
RC   STRAIN=ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125;
RX   PubMed=8987660; DOI=10.1271/bbb.60.1633;
RA   Xu Y., Kobayashi T., Kudo T.;
RT   "Molecular cloning and nucleotide sequence of the groEL gene from the
RT   alkaliphilic Bacillus sp. strain C-125 and reactivation of thermally
RT   inactivated alpha-glucosidase by recombinant GroEL.";
RL   Biosci. Biotechnol. Biochem. 60:1633-1636(1996).
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}.
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DR   EMBL; BA000004; BAB04280.1; -; Genomic_DNA.
DR   EMBL; D55630; BAA09493.1; -; Genomic_DNA.
DR   PIR; A83720; A83720.
DR   PIR; PC4238; PC4238.
DR   RefSeq; WP_010896738.1; NC_002570.2.
DR   AlphaFoldDB; O50304; -.
DR   SMR; O50304; -.
DR   STRING; 272558.10173174; -.
DR   EnsemblBacteria; BAB04280; BAB04280; BAB04280.
DR   KEGG; bha:BH0561; -.
DR   eggNOG; COG0234; Bacteria.
DR   HOGENOM; CLU_132825_2_0_9; -.
DR   OMA; EVKYSGE; -.
DR   OrthoDB; 1965002at2; -.
DR   Proteomes; UP000001258; 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   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..94
FT                   /note="Co-chaperonin GroES"
FT                   /id="PRO_0000174693"
SQ   SEQUENCE   94 AA;  10220 MW;  5BC8D3EAD0D851A6 CRC64;
     MLKPLGDRVV IEQVETEEKT ASGIVLPDTA KEKPQEGRVV AVGTGRVTEN GEKIALEVKE
     GDSVIFSKYA GTEVKYDGKE YLILRESDIL AIIG