ID   CH10_CAUVN              Reviewed;          96 AA.
AC   B8H164; P48222;
DT   16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 76.
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}, mopB;
GN   OrderedLocusNames=CCNA_00722;
OS   Caulobacter vibrioides (strain NA1000 / CB15N) (Caulobacter crescentus).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Caulobacterales;
OC   Caulobacteraceae; Caulobacter.
OX   NCBI_TaxID=565050;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], OPERON STRUCTURE, AND INDUCTION.
RX   PubMed=8821938; DOI=10.1046/j.1365-2958.1996.347879.x;
RA   Avedissian M., Gomes S.L.;
RT   "Expression of the groESL operon is cell-cycle controlled in Caulobacter
RT   crescentus.";
RL   Mol. Microbiol. 19:79-89(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NA1000 / CB15N;
RX   PubMed=20472802; DOI=10.1128/jb.00255-10;
RA   Marks M.E., Castro-Rojas C.M., Teiling C., Du L., Kapatral V.,
RA   Walunas T.L., Crosson S.;
RT   "The genetic basis of laboratory adaptation in Caulobacter crescentus.";
RL   J. Bacteriol. 192:3678-3688(2010).
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   -!- INDUCTION: By heat shock. {ECO:0000269|PubMed:8821938}.
CC   -!- SIMILARITY: Belongs to the GroES chaperonin family. {ECO:0000255|HAMAP-
CC       Rule:MF_00580, ECO:0000305}.
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DR   EMBL; L41394; AAB18634.1; -; Genomic_DNA.
DR   EMBL; CP001340; ACL94187.1; -; Genomic_DNA.
DR   PIR; S70668; S70668.
DR   RefSeq; WP_010918572.1; NC_011916.1.
DR   RefSeq; YP_002516095.1; NC_011916.1.
DR   AlphaFoldDB; B8H164; -.
DR   SMR; B8H164; -.
DR   PRIDE; B8H164; -.
DR   EnsemblBacteria; ACL94187; ACL94187; CCNA_00722.
DR   GeneID; 7330531; -.
DR   KEGG; ccs:CCNA_00722; -.
DR   PATRIC; fig|565050.3.peg.712; -.
DR   HOGENOM; CLU_132825_1_0_5; -.
DR   OMA; RSINMTI; -.
DR   OrthoDB; 1965002at2; -.
DR   PhylomeDB; B8H164; -.
DR   Proteomes; UP000001364; 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   2: Evidence at transcript level;
KW   Chaperone; Cytoplasm; Reference proteome.
FT   CHAIN           1..96
FT                   /note="Co-chaperonin GroES"
FT                   /id="PRO_0000378280"
FT   CONFLICT        42..43
FT                   /note="AV -> RS (in Ref. 1; AAB18634)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        50..56
FT                   /note="DKGDVVA -> EHTSSP (in Ref. 1; AAB18634)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        74
FT                   /note="E -> ASEGTK (in Ref. 1)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        78..80
FT                   /note="DGQ -> TS (in Ref. 1; AAB18634)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   96 AA;  10344 MW;  28DE4E283A248796 CRC64;
     MKFRPLGDRV LVKRVEEETK TKGGIIIPDT AKEKPQEGEV VAVGPGARND KGDVVALDVK
     AGDRILFGKW SGTEVKVDGQ DLLIMKESDV LGVVEA