ID   CDSA_STAHJ              Reviewed;         260 AA.
AC   Q4L5W3;
DT   07-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT   02-AUG-2005, sequence version 1.
DT   16-JUN-2009, entry version 31.
DE   RecName: Full=Phosphatidate cytidylyltransferase;
DE            EC=2.7.7.41;
DE   AltName: Full=CDP-diglyceride pyrophosphorylase;
DE   AltName: Full=CDP-diglyceride synthetase;
DE   AltName: Full=CDP-diacylglycerol synthase;
DE            Short=CDS;
DE   AltName: Full=CTP:phosphatidate cytidylyltransferase;
DE   AltName: Full=CDP-DG synthetase;
DE   AltName: Full=CDP-DAG synthase;
GN   Name=cdsA; OrderedLocusNames=SH1653;
OS   Staphylococcus haemolyticus (strain JCSC1435).
OC   Bacteria; Firmicutes; Bacillales; Staphylococcus.
OX   NCBI_TaxID=279808;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16237012; DOI=10.1128/JB.187.21.7292-7308.2005;
RA   Takeuchi F., Watanabe S., Baba T., Yuzawa H., Ito T., Morimoto Y.,
RA   Kuroda M., Cui L., Takahashi M., Ankai A., Baba S., Fukui S.,
RA   Lee J.C., Hiramatsu K.;
RT   "Whole-genome sequencing of Staphylococcus haemolyticus uncovers the
RT   extreme plasticity of its genome and the evolution of human-colonizing
RT   staphylococcal species.";
RL   J. Bacteriol. 187:7292-7308(2005).
CC   -!- CATALYTIC ACTIVITY: CTP + phosphatidate = diphosphate + CDP-
CC       diacylglycerol.
CC   -!- PATHWAY: Phospholipid metabolism; CDP-diacylglycerol biosynthesis;
CC       CDP-diacylglycerol from sn-glycerol 3-phosphate: step 3/3.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein
CC       (By similarity).
CC   -!- SIMILARITY: Belongs to the CDS family.
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DR   EMBL; AP006716; BAE04962.1; -; Genomic_DNA.
DR   RefSeq; YP_253568.1; -.
DR   GeneID; 3482336; -.
DR   GenomeReviews; AP006716_GR; SH1653.
DR   KEGG; sha:SH1653; -.
DR   NMPDR; fig|279808.3.peg.1025; -.
DR   HOGENOM; Q4L5W3; -.
DR   OMA; Q4L5W3; HITEMEV.
DR   BioCyc; SHAE279808:SH1653-MON; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004605; F:phosphatidate cytidylyltransferase activity; IEA:EC.
DR   GO; GO:0008654; P:phospholipid biosynthetic process; IEA:UniProtKB-KW.
DR   InterPro; IPR000374; PC_trans.
DR   Pfam; PF01148; CTP_transf_1; 1.
DR   PROSITE; PS01315; CDS; 1.
PE   3: Inferred from homology;
KW   Cell membrane; Complete proteome; Membrane; Nucleotidyltransferase;
KW   Phospholipid biosynthesis; Transferase; Transmembrane.
FT   CHAIN         1    260       Phosphatidate cytidylyltransferase.
FT                                /FTId=PRO_0000090755.
FT   TRANSMEM      9     29       Potential.
FT   TRANSMEM     46     66       Potential.
FT   TRANSMEM     70     90       Potential.
FT   TRANSMEM    102    122       Potential.
FT   TRANSMEM    130    150       Potential.
FT   TRANSMEM    172    192       Potential.
FT   TRANSMEM    196    216       Potential.
SQ   SEQUENCE   260 AA;  29032 MW;  4758A210219C26A8 CRC64;
     MKVRTLTAII ALLIFLPILL MGGTTLMLFA YLLALIALKE LLNMNMIKLI SVPGIFSALA
     LIIIMLPQSA GDWVSNIQLK SLIAMSFILL SYTVLSKNRF SFMDAAFCLM SVAYVGIGFM
     YFYATRSDGL HYILYAFLVV WLTDTGAYIF GRLMGKHKLW PVISPNKTIE GFIGGLICSL
     IVPIVMLFFV DFNLNIWLLL LVTIILSIFG QLGDLVESGF KRHFGVKDSG RILPGHGGIL
     DRFDSFMFVL PLLNILLIQM
//