ID   CDSA_CHLTR              Reviewed;         305 AA.
AC   O84457;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   16-JUN-2009, entry version 55.
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=CT_451;
OS   Chlamydia trachomatis.
OC   Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae; Chlamydia.
OX   NCBI_TaxID=813;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=D/UW-3/Cx;
RX   MEDLINE=99000809; PubMed=9784136; DOI=10.1126/science.282.5389.754;
RA   Stephens R.S., Kalman S., Lammel C.J., Fan J., Marathe R., Aravind L.,
RA   Mitchell W.P., Olinger L., Tatusov R.L., Zhao Q., Koonin E.V.,
RA   Davis R.W.;
RT   "Genome sequence of an obligate intracellular pathogen of humans:
RT   Chlamydia trachomatis.";
RL   Science 282:754-759(1998).
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; AE001273; AAC68051.1; -; Genomic_DNA.
DR   PIR; F71512; F71512.
DR   RefSeq; NP_219964.1; -.
DR   GeneID; 884225; -.
DR   GenomeReviews; AE001273_GR; CT_451.
DR   KEGG; ctr:CT451; -.
DR   HOGENOM; O84457; -.
DR   OMA; O84457; LYVSVPI.
DR   BioCyc; CTRA315277:CT451-MON; -.
DR   BRENDA; 2.7.7.41; 108.
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; FALSE_NEG.
PE   3: Inferred from homology;
KW   Cell membrane; Complete proteome; Membrane; Nucleotidyltransferase;
KW   Phospholipid biosynthesis; Transferase; Transmembrane.
FT   CHAIN         1    305       Phosphatidate cytidylyltransferase.
FT                                /FTId=PRO_0000090733.
FT   TRANSMEM     27     47       Potential.
FT   TRANSMEM     67     87       Potential.
FT   TRANSMEM     96    116       Potential.
FT   TRANSMEM    124    144       Potential.
FT   TRANSMEM    150    170       Potential.
FT   TRANSMEM    202    222       Potential.
FT   TRANSMEM    232    252       Potential.
FT   TRANSMEM    277    297       Potential.
SQ   SEQUENCE   305 AA;  33805 MW;  BAC435DC5677FFCC CRC64;
     MFDSDHNSIF QSDLCQRLVV HSILLTFLVI LLCTSLYPSS AFIVGLLSSA CAALGTYEMG
     AMVRIKFPFS FTRYSALGSA IFIALTCLTA RCKMCFPEHI DLLPWFFLFF WTIRLVFKSR
     HYKLGPIGST GLALFCMLYV SVPIRLFLHI LYGFVHTDTP FVGIWWAIFL IATTKSSDIF
     GYFFGKAFGK KRIAPVISPN KTVVGFIAGC CGSILVSLLF YSHLPKAFAD QIAVPWILIA
     LGTVLGVSGF FGDIIESTFK RDAQIKNSSD LESIGGMLDV LDSLLLSTPI VYAILLITQN
     RTFLG
//