(data stored in ACNUC7421 zone)

SWISSPROT: CH10_DESOH

ID   CH10_DESOH              Reviewed;          95 AA.
AC   A8ZU47;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 1.
DT   11-DEC-2019, entry version 65.
DE   RecName: Full=10 kDa chaperonin {ECO:0000255|HAMAP-Rule:MF_00580};
DE   AltName: Full=GroES protein {ECO:0000255|HAMAP-Rule:MF_00580};
DE   AltName: Full=Protein Cpn10 {ECO:0000255|HAMAP-Rule:MF_00580};
GN   Name=groS {ECO:0000255|HAMAP-Rule:MF_00580};
GN   Synonyms=groES {ECO:0000255|HAMAP-Rule:MF_00580};
GN   OrderedLocusNames=Dole_0549;
OS   Desulfococcus oleovorans (strain DSM 6200 / Hxd3).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfobacterales;
OC   Desulfobacteraceae; Desulfococcus.
OX   NCBI_TaxID=96561;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 6200 / Hxd3;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Kiss H., Brettin T., Bruce D., Detter J.C., Han C.,
RA   Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Wawrik B.,
RA   Richardson P.;
RT   "Complete sequence of Desulfococcus oleovorans Hxd3.";
RL   Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Binds to Cpn60 in the presence of Mg-ATP and suppresses the
CC       ATPase activity of the latter. {ECO:0000255|HAMAP-Rule:MF_00580}.
CC   -!- SUBUNIT: Heptamer of 7 subunits arranged in a ring. {ECO:0000255|HAMAP-
CC       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}.
DR   EMBL; CP000859; ABW66359.1; -; Genomic_DNA.
DR   RefSeq; WP_012173978.1; NC_009943.1.
DR   SMR; A8ZU47; -.
DR   STRING; 96561.Dole_0549; -.
DR   EnsemblBacteria; ABW66359; ABW66359; Dole_0549.
DR   KEGG; dol:Dole_0549; -.
DR   eggNOG; ENOG4105K5Y; Bacteria.
DR   eggNOG; COG0234; LUCA.
DR   HOGENOM; HOG000133897; -.
DR   KO; K04078; -.
DR   OMA; PGRIDDN; -.
DR   OrthoDB; 1965002at2; -.
DR   BioCyc; DOLE96561:G1GAC-569-MONOMER; -.
DR   Proteomes; UP000008561; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0006457; P:protein folding; IEA:UniProtKB-UniRule.
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;
DR   PRODOM; A8ZU47.
DR   SWISS-2DPAGE; A8ZU47.
KW   Chaperone; Cytoplasm; Reference proteome.
FT   CHAIN           1..95
FT                   /note="10 kDa chaperonin"
FT                   /id="PRO_1000129649"
SQ   SEQUENCE   95 AA;  10651 MW;  AD506100364E372C CRC64;
     MKFRPLHDRI LVKRVEEETK TKGGIIIPDT AKEKPIEGKV MAVGNGRLGE DGKLIPLEVK
     KGDRVLFGKY GGTEVKMDGQ EYLIMREDDI LGILE
//

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