ID   CDSA_STAS1              Reviewed;         260 AA.
AC   Q49X46;
DT   07-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   16-JUN-2009, entry version 29.
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=SSP1507;
OS   Staphylococcus saprophyticus subsp. saprophyticus (strain ATCC 15305 /
OS   DSM 20229).
OC   Bacteria; Firmicutes; Bacillales; Staphylococcus.
OX   NCBI_TaxID=342451;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16135568; DOI=10.1073/pnas.0502950102;
RA   Kuroda M., Yamashita A., Hirakawa H., Kumano M., Morikawa K.,
RA   Higashide M., Maruyama A., Inose Y., Matoba K., Toh H., Kuhara S.,
RA   Hattori M., Ohta T.;
RT   "Whole genome sequence of Staphylococcus saprophyticus reveals the
RT   pathogenesis of uncomplicated urinary tract infection.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:13272-13277(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; AP008934; BAE18652.1; -; Genomic_DNA.
DR   RefSeq; YP_301597.1; -.
DR   GeneID; 3617249; -.
DR   GenomeReviews; AP008934_GR; SSP1507.
DR   KEGG; ssp:SSP1507; -.
DR   NMPDR; fig|342451.4.peg.1523; -.
DR   HOGENOM; Q49X46; -.
DR   OMA; Q49X46; YHIFFIF.
DR   BioCyc; SSAP342451:SSP1507-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_0000090756.
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;  29066 MW;  C95166CECD1011F0 CRC64;
     MKVRTLTAII ALIVFLPVLL KGGLILMLFS YLLAFIALKE LLNMNMIKFL SIPGIISALG
     ILIIMLPQDA GSWVNDLQLK SLIAMSFILL SYTVLSKNRF SFMDAAFCLM SIAYVGIGFM
     YLYETRSEGL HYILFAFLVV WLTDTGAYIF GRLMGKHKLW PVISPNKTVE GFVGGLICSL
     IVPLVMMIFV DFNIALWLLL IITIILSMFG QLGDLVESGF KRHFGVKDSG RILPGHGGIL
     DRFDSFMFVL PLLNILLIQI
//