ID   CH101_VIBVY             Reviewed;          96 AA.
AC   Q7M7I6;
DT   19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2003, sequence version 1.
DT   03-AUG-2022, entry version 104.
DE   RecName: Full=Co-chaperonin GroES 1 {ECO:0000255|HAMAP-Rule:MF_00580};
DE   AltName: Full=10 kDa chaperonin 1 {ECO:0000255|HAMAP-Rule:MF_00580};
DE   AltName: Full=Chaperonin-10 1 {ECO:0000255|HAMAP-Rule:MF_00580};
DE            Short=Cpn10 1 {ECO:0000255|HAMAP-Rule:MF_00580};
GN   Name=groES1 {ECO:0000255|HAMAP-Rule:MF_00580};
GN   Synonyms=groS1 {ECO:0000255|HAMAP-Rule:MF_00580}; OrderedLocusNames=VV3107;
OS   Vibrio vulnificus (strain YJ016).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=196600;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YJ016;
RX   PubMed=14656965; DOI=10.1101/gr.1295503;
RA   Chen C.-Y., Wu K.-M., Chang Y.-C., Chang C.-H., Tsai H.-C., Liao T.-L.,
RA   Liu Y.-M., Chen H.-J., Shen A.B.-T., Li J.-C., Su T.-L., Shao C.-P.,
RA   Lee C.-T., Hor L.-I., Tsai S.-F.;
RT   "Comparative genome analysis of Vibrio vulnificus, a marine pathogen.";
RL   Genome Res. 13:2577-2587(2003).
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; BA000037; BAC95871.1; -; Genomic_DNA.
DR   RefSeq; WP_011079244.1; NC_005139.1.
DR   AlphaFoldDB; Q7M7I6; -.
DR   SMR; Q7M7I6; -.
DR   STRING; 672.VV93_v1c28300; -.
DR   EnsemblBacteria; BAC95871; BAC95871; BAC95871.
DR   GeneID; 66966301; -.
DR   KEGG; vvy:VV3107; -.
DR   eggNOG; COG0234; Bacteria.
DR   HOGENOM; CLU_132825_1_1_6; -.
DR   OMA; KVFYRQW; -.
DR   OrthoDB; 1965002at2; -.
DR   Proteomes; UP000002675; Chromosome I.
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 1"
FT                   /id="PRO_0000174898"
SQ   SEQUENCE   96 AA;  10295 MW;  587751C6BB9E455A CRC64;
     MNIRPLHDRV IVERQEVESK SAGGIVLTGS AAEKSTRGVV LAVGKGRILE NGTVQPLDVK
     VGDTVIFAES YGTKTEKIDG KEVLIMSEND IMAIVD