ID   CH10_GEMAT              Reviewed;          97 AA.
AC   C1A8L7;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   26-MAY-2009, sequence version 1.
DT   03-AUG-2022, entry version 58.
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=GAU_1535;
OS   Gemmatimonas aurantiaca (strain T-27 / DSM 14586 / JCM 11422 / NBRC
OS   100505).
OC   Bacteria; Gemmatimonadetes; Gemmatimonadales; Gemmatimonadaceae;
OC   Gemmatimonas.
OX   NCBI_TaxID=379066;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=T-27 / DSM 14586 / JCM 11422 / NBRC 100505;
RA   Takasaki K., Ichikawa N., Miura H., Matsushita S., Watanabe Y., Oguchi A.,
RA   Ankai A., Yashiro I., Takahashi M., Terui Y., Fukui S., Yokoyama H.,
RA   Tanikawa S., Hanada S., Kamagata Y., Fujita N.;
RT   "Complete genome sequence of Gemmatimonas aurantiaca T-27 that represents a
RT   novel phylum Gemmatimonadetes.";
RL   Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
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   -!- SIMILARITY: Belongs to the GroES chaperonin family. {ECO:0000255|HAMAP-
CC       Rule:MF_00580}.
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DR   EMBL; AP009153; BAH38577.1; -; Genomic_DNA.
DR   RefSeq; WP_012683024.1; NC_012489.1.
DR   AlphaFoldDB; C1A8L7; -.
DR   SMR; C1A8L7; -.
DR   STRING; 379066.GAU_1535; -.
DR   EnsemblBacteria; BAH38577; BAH38577; GAU_1535.
DR   KEGG; gau:GAU_1535; -.
DR   eggNOG; COG0234; Bacteria.
DR   HOGENOM; CLU_132825_2_0_0; -.
DR   OMA; RSINMTI; -.
DR   OrthoDB; 1965002at2; -.
DR   Proteomes; UP000002209; 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   3: Inferred from homology;
KW   Chaperone; Cytoplasm; Reference proteome.
FT   CHAIN           1..97
FT                   /note="Co-chaperonin GroES"
FT                   /id="PRO_1000212115"
SQ   SEQUENCE   97 AA;  10566 MW;  A91F0345AA91616D CRC64;
     MANQKVAPLA DRVVVKPLEE AEQMRGGLYI PDTAKEKPQQ GTVVAVGPGR FEKETRVPMD
     VKVGDKILYG KYSGTEVTIE GEALLILRES DVLAVIN