ID   CH10_PELUB              Reviewed;          96 AA.
AC   Q4FPA6;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   30-AUG-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};
GN   OrderedLocusNames=SAR11_0161;
OS   Pelagibacter ubique (strain HTCC1062).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Pelagibacterales;
OC   Pelagibacteraceae; Candidatus Pelagibacter.
OX   NCBI_TaxID=335992;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HTCC1062;
RX   PubMed=16109880; DOI=10.1126/science.1114057;
RA   Giovannoni S.J., Tripp H.J., Givan S., Podar M., Vergin K.L., Baptista D.,
RA   Bibbs L., Eads J., Richardson T.H., Noordewier M., Rappe M.S., Short J.M.,
RA   Carrington J.C., Mathur E.J.;
RT   "Genome streamlining in a cosmopolitan oceanic bacterium.";
RL   Science 309:1242-1245(2005).
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; CP000084; AAZ20983.1; -; Genomic_DNA.
DR   RefSeq; WP_006997749.1; NC_007205.1.
DR   AlphaFoldDB; Q4FPA6; -.
DR   SMR; Q4FPA6; -.
DR   STRING; 335992.SAR11_0161; -.
DR   EnsemblBacteria; AAZ20983; AAZ20983; SAR11_0161.
DR   GeneID; 66294661; -.
DR   KEGG; pub:SAR11_0161; -.
DR   eggNOG; COG0234; Bacteria.
DR   HOGENOM; CLU_132825_1_0_5; -.
DR   OMA; EVKYSGE; -.
DR   OrthoDB; 1965002at2; -.
DR   Proteomes; UP000002528; 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..96
FT                   /note="Co-chaperonin GroES"
FT                   /id="PRO_1000025321"
SQ   SEQUENCE   96 AA;  10330 MW;  11E0B8697157CE27 CRC64;
     MKFKPLHDRV LIEVLDSSEK TAGGIIIPDT AQEKPQEGKV IAVGGGAKTE DGKLIPMDVK
     VGDKVLFGKW SGTEIKIDGK EYSIMKESDI MGISGK