ID   CDSA_RICFE              Reviewed;         227 AA.
AC   Q4ULR7;
DT   20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-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=RF_0655;
OS   Rickettsia felis (Rickettsia azadi).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
OX   NCBI_TaxID=42862;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC VR-1525 / URRWXCal2;
RX   PubMed=15984913; DOI=10.1371/journal.pbio.0030248;
RA   Ogata H., Renesto P., Audic S., Robert C., Blanc G., Fournier P.-E.,
RA   Parinello H., Claverie J.-M., Raoult D.;
RT   "The genome sequence of Rickettsia felis identifies the first putative
RT   conjugative plasmid in an obligate intracellular parasite.";
RL   PLoS Biol. 3:1-12(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.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; CP000053; AAY61506.1; -; Genomic_DNA.
DR   RefSeq; YP_246671.1; -.
DR   GeneID; 3400663; -.
DR   GenomeReviews; CP000053_GR; RF_0655.
DR   KEGG; rfe:RF_0655; -.
DR   NMPDR; fig|315456.3.peg.566; -.
DR   HOGENOM; Q4ULR7; -.
DR   OMA; Q4ULR7; MEDTNRW.
DR   BioCyc; RFEL315456:RF_0655-MON; -.
DR   BRENDA; 2.7.7.41; 297363.
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    227       Phosphatidate cytidylyltransferase.
FT                                /FTId=PRO_0000281058.
FT   TRANSMEM     31     51       Potential.
FT   TRANSMEM     65     85       Potential.
FT   TRANSMEM     93    113       Potential.
FT   TRANSMEM    131    151       Potential.
FT   TRANSMEM    165    185       Potential.
FT   TRANSMEM    206    226       Potential.
SQ   SEQUENCE   227 AA;  25624 MW;  44E64F36CDE950FE CRC64;
     MITQKGKEHL AKDKQNIYLR ILSGIVLVPL FVIAILWFKP LFYILMILVG MGMLSEWYNM
     TYSSIPYLLI GLIIIPIPIS LLTFLSMEDT NRWLIMLYFC IIWSVDSFAM IGGKTFKGAK
     LAPKISPKKT WSGLVTGVLS AGLVAVLASF IPNFHIENYY FSNKIYLFII SCILALIAQS
     SDLFISYLKR KFNIKDSGHI IPGHGGVLDR FDSIILTAPV LFFISIL
//