(data stored in SCRATCH zone)

SWISSPROT: C8U1P3_ECO10

ID   C8U1P3_ECO10            Unreviewed;       275 AA.
AC   C8U1P3;
DT   03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   03-NOV-2009, sequence version 1.
DT   08-MAY-2019, entry version 48.
DE   RecName: Full=Phosphatidate cytidylyltransferase {ECO:0000256|RuleBase:RU003938};
DE            EC=2.7.7.41 {ECO:0000256|RuleBase:RU003938};
GN   Name=cdsA {ECO:0000313|EMBL:BAI29051.1};
GN   OrderedLocusNames=ECO103_0173 {ECO:0000313|EMBL:BAI29051.1};
OS   Escherichia coli O103:H2 (strain 12009 / EHEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=585395 {ECO:0000313|EMBL:BAI29051.1, ECO:0000313|Proteomes:UP000000959};
RN   [1] {ECO:0000313|EMBL:BAI29051.1, ECO:0000313|Proteomes:UP000000959}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=12009 / EHEC {ECO:0000313|Proteomes:UP000000959};
RX   PubMed=19815525; DOI=10.1073/pnas.0903585106;
RA   Ogura Y., Ooka T., Iguchi A., Toh H., Asadulghani M., Oshima K.,
RA   Kodama T., Abe H., Nakayama K., Kurokawa K., Tobe T., Hattori M.,
RA   Hayashi T.;
RT   "Comparative genomics reveal the mechanism of the parallel evolution
RT   of O157 and non-O157 enterohemorrhagic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:17939-17944(2009).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 1,2-diacyl-sn-glycero-3-phosphate + CTP + H(+) = a CDP-
CC         1,2-diacyl-sn-glycerol + diphosphate; Xref=Rhea:RHEA:16229,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:37563,
CC         ChEBI:CHEBI:58332, ChEBI:CHEBI:58608; EC=2.7.7.41;
CC         Evidence={ECO:0000256|RuleBase:RU003938};
CC   -!- PATHWAY: Phospholipid metabolism; CDP-diacylglycerol biosynthesis;
CC       CDP-diacylglycerol from sn-glycerol 3-phosphate: step 3/3.
CC       {ECO:0000256|RuleBase:RU003938}.
CC   -!- SIMILARITY: Belongs to the CDS family.
CC       {ECO:0000256|RuleBase:RU003938}.
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DR   EMBL; AP010958; BAI29051.1; -; Genomic_DNA.
DR   EnsemblBacteria; BAI29051; BAI29051; ECO103_0173.
DR   KEGG; eoh:ECO103_0173; -.
DR   HOGENOM; HOG000006168; -.
DR   KO; K00981; -.
DR   OMA; WEWGRLN; -.
DR   UniPathway; UPA00557; UER00614.
DR   Proteomes; UP000000959; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004605; F:phosphatidate cytidylyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016024; P:CDP-diacylglycerol biosynthetic process; IEA:UniProtKB-UniPathway.
DR   InterPro; IPR000374; PC_trans.
DR   PROSITE; PS01315; CDS; 1.
PE   3: Inferred from homology;
DR   PRODOM; C8U1P3.
DR   SWISS-2DPAGE; C8U1P3.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000959};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Nucleotidyltransferase {ECO:0000256|RuleBase:RU003938};
KW   Transferase {ECO:0000256|RuleBase:RU003938};
KW   Transmembrane {ECO:0000256|RuleBase:RU003938,
KW   ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM      6     34       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM     46     63       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM     83    103       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    110    131       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    143    161       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    182    200       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    206    224       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    254    272       Helical. {ECO:0000256|SAM:Phobius}.
SQ   SEQUENCE   275 AA;  30262 MW;  EEC88BF28F1F62D6 CRC64;
     MLIPVVIAAL FLLPPVGFAI VTLVVCMLAA WEWGQLSGFT TRSQRVWLAV LCGLLLALML
     FLLPEYHRNI HQPLVEISLW ASLGWWIVAL LLVLFYPGSA AIWRNSKTLR LIFGVLTIVP
     FFWGMLALRA WHYDENHYSG AIWLLYVMIL VWGADSGAYM FGKLFGKHKL APKVSPGKTW
     QGFIGGLATA AVISWGYGMW ANLDVAPVTL LICSIVAALA SVLGDLTESM FKREAGIKDS
     GHLIPGHGGI LDRIDSLTAA VPVFACLLLL VFRTL
//

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