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VATD_CLOD6
ID   VATD_CLOD6              Reviewed;         222 AA.
AC   Q184E4;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   25-JUL-2006, sequence version 1.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=V-type ATP synthase subunit D {ECO:0000255|HAMAP-Rule:MF_00271};
DE   AltName: Full=V-ATPase subunit D {ECO:0000255|HAMAP-Rule:MF_00271};
GN   Name=atpD {ECO:0000255|HAMAP-Rule:MF_00271}; OrderedLocusNames=CD630_29540;
OS   Clostridioides difficile (strain 630) (Peptoclostridium difficile).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Peptostreptococcaceae;
OC   Clostridioides.
OX   NCBI_TaxID=272563;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=630;
RX   PubMed=16804543; DOI=10.1038/ng1830;
RA   Sebaihia M., Wren B.W., Mullany P., Fairweather N.F., Minton N.,
RA   Stabler R., Thomson N.R., Roberts A.P., Cerdeno-Tarraga A.M., Wang H.,
RA   Holden M.T.G., Wright A., Churcher C., Quail M.A., Baker S., Bason N.,
RA   Brooks K., Chillingworth T., Cronin A., Davis P., Dowd L., Fraser A.,
RA   Feltwell T., Hance Z., Holroyd S., Jagels K., Moule S., Mungall K.,
RA   Price C., Rabbinowitsch E., Sharp S., Simmonds M., Stevens K., Unwin L.,
RA   Whithead S., Dupuy B., Dougan G., Barrell B., Parkhill J.;
RT   "The multidrug-resistant human pathogen Clostridium difficile has a highly
RT   mobile, mosaic genome.";
RL   Nat. Genet. 38:779-786(2006).
CC   -!- FUNCTION: Produces ATP from ADP in the presence of a proton gradient
CC       across the membrane. {ECO:0000255|HAMAP-Rule:MF_00271}.
CC   -!- SIMILARITY: Belongs to the V-ATPase D subunit family.
CC       {ECO:0000255|HAMAP-Rule:MF_00271}.
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DR   EMBL; AM180355; CAJ69846.1; -; Genomic_DNA.
DR   RefSeq; WP_009891221.1; NZ_CP010905.2.
DR   RefSeq; YP_001089470.1; NC_009089.1.
DR   AlphaFoldDB; Q184E4; -.
DR   SMR; Q184E4; -.
DR   STRING; 272563.CD630_29540; -.
DR   EnsemblBacteria; CAJ69846; CAJ69846; CD630_29540.
DR   GeneID; 66355360; -.
DR   KEGG; cdf:CD630_29540; -.
DR   KEGG; pdc:CDIF630_03237; -.
DR   PATRIC; fig|272563.120.peg.3120; -.
DR   eggNOG; COG1394; Bacteria.
DR   OMA; SKNIMGV; -.
DR   PhylomeDB; Q184E4; -.
DR   BioCyc; PDIF272563:G12WB-3118-MON; -.
DR   Proteomes; UP000001978; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:UniProtKB-UniRule.
DR   GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:InterPro.
DR   GO; GO:0042777; P:proton motive force-driven plasma membrane ATP synthesis; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_00271; ATP_synth_D_arch; 1.
DR   InterPro; IPR002699; V_ATPase_D.
DR   PANTHER; PTHR11671; PTHR11671; 1.
DR   Pfam; PF01813; ATP-synt_D; 1.
DR   TIGRFAMs; TIGR00309; V_ATPase_subD; 1.
PE   3: Inferred from homology;
KW   ATP synthesis; Hydrogen ion transport; Ion transport; Reference proteome;
KW   Transport.
FT   CHAIN           1..222
FT                   /note="V-type ATP synthase subunit D"
FT                   /id="PRO_1000059153"
SQ   SEQUENCE   222 AA;  25585 MW;  967B13966B369FDC CRC64;
     MARLNINPTR MEMTRLKKLL KTATRGHKLL KDKLDELMKQ FLEIVRENKR LREEAENALD
     TAYKNFIIAR AVMSQEYLGS ALMMPKQSVS VDVSTRNIMS VDVPVFDFKT ENNQSDIYPY
     GLAFTSGELD SAMEAFSDAM QPLLRLAESE KSAQLLAQEI EKTRRRVNAL ENVMIPNYIE
     TIKYIAMKLE ENERASTTRL MKVKDMVLKK ALEEKKKNDL VV
 
 
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