ID   CH10_PARTM              Reviewed;          94 AA.
AC   Q8VV85;
DT   10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 81.
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};
OS   Parageobacillus thermoglucosidasius (Geobacillus thermoglucosidasius).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Parageobacillus.
OX   NCBI_TaxID=1426;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 43742 / DSM 2542 / NCIMB 11955 / NRRL B-14516 / KP 1006;
RX   PubMed=11834128; DOI=10.1042/ba20010064;
RA   Watanabe K., Fujiwara H., Inui K., Suzuki Y.;
RT   "Oligo-1,6-glucosidase from a thermophile, Bacillus thermoglucosidasius
RT   KP1006, was efficiently produced by combinatorial expression of GroEL in
RT   Escherichia coli.";
RL   Biotechnol. Appl. Biochem. 35:35-43(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   -!- SIMILARITY: Belongs to the GroES chaperonin family. {ECO:0000255|HAMAP-
CC       Rule:MF_00580}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AB025944; BAB83939.1; -; Genomic_DNA.
DR   RefSeq; WP_003253377.1; NZ_LUCT01000019.1.
DR   AlphaFoldDB; Q8VV85; -.
DR   SMR; Q8VV85; -.
DR   STRING; 1426.AOT13_04585; -.
DR   GeneID; 56924742; -.
DR   eggNOG; COG0234; Bacteria.
DR   OMA; EVKYSGE; -.
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.
FT   CHAIN           1..94
FT                   /note="Co-chaperonin GroES"
FT                   /id="PRO_0000174699"
SQ   SEQUENCE   94 AA;  10239 MW;  F771FC4EBC0C0918 CRC64;
     MIKPLGDRVV IEIVETEEKT ASGIVLPDTA KEKPQEGKVV AVGKGRVLDN GQRVAPEVEV
     GDRIIFSKYA GTEVKYDGKE YLILRESDIL AVIG