(data stored in ACNUC7421 zone)

SWISSPROT: D6XY30_BACIE

ID   D6XY30_BACIE            Unreviewed;        94 AA.
AC   D6XY30;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   08-MAY-2019, entry version 62.
DE   RecName: Full=10 kDa chaperonin {ECO:0000256|HAMAP-Rule:MF_00580, ECO:0000256|RuleBase:RU000535};
DE   AltName: Full=GroES protein {ECO:0000256|HAMAP-Rule:MF_00580};
DE   AltName: Full=Protein Cpn10 {ECO:0000256|HAMAP-Rule:MF_00580};
GN   Name=groS {ECO:0000256|HAMAP-Rule:MF_00580};
GN   Synonyms=groES {ECO:0000256|HAMAP-Rule:MF_00580};
GN   OrderedLocusNames=Bsel_0567 {ECO:0000313|EMBL:ADH98103.1};
OS   Bacillus selenitireducens (strain ATCC 700615 / DSM 15326 / MLS10).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Sporolactobacillaceae;
OC   unclassified Sporolactobacillaceae.
OX   NCBI_TaxID=439292 {ECO:0000313|EMBL:ADH98103.1, ECO:0000313|Proteomes:UP000000271};
RN   [1] {ECO:0000313|EMBL:ADH98103.1, ECO:0000313|Proteomes:UP000000271}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700615 / DSM 15326 / MLS10
RC   {ECO:0000313|Proteomes:UP000000271};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T.,
RA   Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Ovchinnikova G., Stolz J.;
RT   "Complete sequence of Bacillus selenitireducens MLS10.";
RL   Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Binds to Cpn60 in the presence of Mg-ATP and suppresses
CC       the ATPase activity of the latter. {ECO:0000256|HAMAP-
CC       Rule:MF_00580, ECO:0000256|RuleBase:RU000535,
CC       ECO:0000256|SAAS:SAAS00735107}.
CC   -!- SUBUNIT: Heptamer of 7 subunits arranged in a ring.
CC       {ECO:0000256|HAMAP-Rule:MF_00580, ECO:0000256|RuleBase:RU000535,
CC       ECO:0000256|SAAS:SAAS00735104}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00580,
CC       ECO:0000256|SAAS:SAAS00735165}.
CC   -!- SIMILARITY: Belongs to the GroES chaperonin family.
CC       {ECO:0000256|HAMAP-Rule:MF_00580, ECO:0000256|RuleBase:RU000535,
CC       ECO:0000256|SAAS:SAAS00735109}.
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DR   EMBL; CP001791; ADH98103.1; -; Genomic_DNA.
DR   RefSeq; WP_013171532.1; NC_014219.1.
DR   STRING; 439292.Bsel_0567; -.
DR   EnsemblBacteria; ADH98103; ADH98103; Bsel_0567.
DR   KEGG; bse:Bsel_0567; -.
DR   eggNOG; ENOG4105K5Y; Bacteria.
DR   eggNOG; COG0234; LUCA.
DR   HOGENOM; HOG000133897; -.
DR   KO; K04078; -.
DR   OMA; PGRIDDN; -.
DR   OrthoDB; 1965002at2; -.
DR   BioCyc; BSEL439292:G1GLR-610-MONOMER; -.
DR   Proteomes; UP000000271; 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; D6XY30.
DR   SWISS-2DPAGE; D6XY30.
KW   Chaperone {ECO:0000256|HAMAP-Rule:MF_00580,
KW   ECO:0000256|RuleBase:RU000535, ECO:0000256|SAAS:SAAS00735148};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000271};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00580,
KW   ECO:0000256|SAAS:SAAS00735098};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000271}.
SQ   SEQUENCE   94 AA;  10263 MW;  492B7556634225C0 CRC64;
     MLKPLGDRIV IELVEQEEKT ASGIVLPDSA KEKPQEGKVV AVGKGRVTEN GETVTPELKE
     GDKIVFSKYA GSEVKFEGKE YMILRESDVL AVIS
//

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