ID   CH10_HELPY              Reviewed;         118 AA.
AC   P0A0R3; P48225;
DT   01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2005, sequence version 1.
DT   03-AUG-2022, entry version 92.
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}, hsp10, hspA, mopB;
GN   OrderedLocusNames=HP_0011;
OS   Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=85962;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=85P;
RX   PubMed=7715457; DOI=10.1111/j.1365-2958.1994.tb01331.x;
RA   Suerbaum S., Thiberge J.-M., Kansau I., Ferrero R.L., Labigne A.;
RT   "Helicobacter pylori hspA-hspB heat-shock gene cluster: nucleotide
RT   sequence, expression, putative function and immunogenicity.";
RL   Mol. Microbiol. 14:959-974(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700392 / 26695;
RX   PubMed=9252185; DOI=10.1038/41483;
RA   Tomb J.-F., White O., Kerlavage A.R., Clayton R.A., Sutton G.G.,
RA   Fleischmann R.D., Ketchum K.A., Klenk H.-P., Gill S.R., Dougherty B.A.,
RA   Nelson K.E., Quackenbush J., Zhou L., Kirkness E.F., Peterson S.N.,
RA   Loftus B.J., Richardson D.L., Dodson R.J., Khalak H.G., Glodek A.,
RA   McKenney K., FitzGerald L.M., Lee N., Adams M.D., Hickey E.K., Berg D.E.,
RA   Gocayne J.D., Utterback T.R., Peterson J.D., Kelley J.M., Cotton M.D.,
RA   Weidman J.F., Fujii C., Bowman C., Watthey L., Wallin E., Hayes W.S.,
RA   Borodovsky M., Karp P.D., Smith H.O., Fraser C.M., Venter J.C.;
RT   "The complete genome sequence of the gastric pathogen Helicobacter
RT   pylori.";
RL   Nature 388:539-547(1997).
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   -!- INTERACTION:
CC       P0A0R3; P0A0R3: groES; NbExp=3; IntAct=EBI-7508075, EBI-7508075;
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, ECO:0000305}.
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DR   EMBL; L23798; AAC41440.1; -; Genomic_DNA.
DR   EMBL; AE000511; AAD07081.1; -; Genomic_DNA.
DR   PIR; S61396; S61396.
DR   RefSeq; NP_206813.1; NC_000915.1.
DR   RefSeq; WP_000671934.1; NC_018939.1.
DR   AlphaFoldDB; P0A0R3; -.
DR   SMR; P0A0R3; -.
DR   IntAct; P0A0R3; 4.
DR   MINT; P0A0R3; -.
DR   STRING; 85962.C694_00050; -.
DR   PaxDb; P0A0R3; -.
DR   EnsemblBacteria; AAD07081; AAD07081; HP_0011.
DR   GeneID; 66521270; -.
DR   KEGG; hpy:HP_0011; -.
DR   PATRIC; fig|85962.47.peg.10; -.
DR   eggNOG; COG0234; Bacteria.
DR   OMA; EVKYSGE; -.
DR   PhylomeDB; P0A0R3; -.
DR   Proteomes; UP000000429; 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:0042802; F:identical protein binding; IPI:IntAct.
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   1: Evidence at protein level;
KW   Chaperone; Cytoplasm; Reference proteome; Stress response.
FT   CHAIN           1..118
FT                   /note="Co-chaperonin GroES"
FT                   /id="PRO_0000174764"
FT   VARIANT         75
FT                   /note="T -> V (in strain: 85P)"
SQ   SEQUENCE   118 AA;  12991 MW;  5A965CD4C2FF014A CRC64;
     MKFQPLGERV LVERLEEENK TSSGIIIPDN AKEKPLMGVV KAVSHKISEG CKCVKEGDVI
     AFGKYKGAEI VLDGTEYMVL ELEDILGIVG SGSCCHTGNH DHKHAKEHEA CCHDHKKH