ID   CH102_VIBPA             Reviewed;          96 AA.
AC   Q87JG7;
DT   25-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=Co-chaperonin GroES 2 {ECO:0000255|HAMAP-Rule:MF_00580};
DE   AltName: Full=10 kDa chaperonin 2 {ECO:0000255|HAMAP-Rule:MF_00580};
DE   AltName: Full=Chaperonin-10 2 {ECO:0000255|HAMAP-Rule:MF_00580};
DE            Short=Cpn10 2 {ECO:0000255|HAMAP-Rule:MF_00580};
GN   Name=groES2 {ECO:0000255|HAMAP-Rule:MF_00580};
GN   Synonyms=groS2 {ECO:0000255|HAMAP-Rule:MF_00580};
GN   OrderedLocusNames=VPA0286;
OS   Vibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=223926;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RIMD 2210633;
RX   PubMed=12620739; DOI=10.1016/s0140-6736(03)12659-1;
RA   Makino K., Oshima K., Kurokawa K., Yokoyama K., Uda T., Tagomori K.,
RA   Iijima Y., Najima M., Nakano M., Yamashita A., Kubota Y., Kimura S.,
RA   Yasunaga T., Honda T., Shinagawa H., Hattori M., Iida T.;
RT   "Genome sequence of Vibrio parahaemolyticus: a pathogenic mechanism
RT   distinct from that of V. cholerae.";
RL   Lancet 361:743-749(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, ECO:0000305}.
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DR   EMBL; BA000032; BAC61629.1; -; Genomic_DNA.
DR   RefSeq; NP_799796.1; NC_004605.1.
DR   RefSeq; WP_005481493.1; NC_004605.1.
DR   AlphaFoldDB; Q87JG7; -.
DR   SMR; Q87JG7; -.
DR   STRING; 223926.28808424; -.
DR   EnsemblBacteria; BAC61629; BAC61629; BAC61629.
DR   GeneID; 1190974; -.
DR   KEGG; vpa:VPA0286; -.
DR   PATRIC; fig|223926.6.peg.3238; -.
DR   eggNOG; COG0234; Bacteria.
DR   HOGENOM; CLU_132825_1_1_6; -.
DR   OMA; KGGIMPT; -.
DR   Proteomes; UP000002493; Chromosome 2.
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 2"
FT                   /id="PRO_0000174895"
SQ   SEQUENCE   96 AA;  10563 MW;  9A6A3ADB234DB7D5 CRC64;
     MKIRPLNDKL IVERQEVENK SEGGIVLTSQ SVKKSNRGKV IAVGLGKRFE NGERAAMEVK
     VGDQIIFNDG YGVKTEKIDG AEYLILSESD VLAIVE