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 01-MAY-2013, entry version 80.
DE RecName: Full=Phosphatidate cytidylyltransferase;
DE EC=2.7.7.41;
DE AltName: Full=CDP-DAG synthase;
DE AltName: Full=CDP-DG synthase;
DE AltName: Full=CDP-diacylglycerol synthase;
DE Short=CDS;
DE AltName: Full=CDP-diglyceride pyrophosphorylase;
DE AltName: Full=CDP-diglyceride synthase;
DE AltName: Full=CTP:phosphatidate cytidylyltransferase;
GN Name=cdsA; OrderedLocusNames=CT_451;
OS Chlamydia trachomatis (strain D/UW-3/Cx).
OC Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC Chlamydia/Chlamydophila group; Chlamydia.
OX NCBI_TaxID=272561;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=D/UW-3/Cx;
RX 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; NC_000117.1.
DR STRING; 272561.CT451; -.
DR EnsemblBacteria; AAC68051; AAC68051; CT_451.
DR GeneID; 884225; -.
DR KEGG; ctr:CT451; -.
DR PATRIC; 20380471; VBIChlTra43535_0488.
DR eggNOG; COG0575; -.
DR KO; K00981; -.
DR OMA; YVFILVW; -.
DR ProtClustDB; CLSK871390; -.
DR UniPathway; UPA00557; UER00614.
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:0016024; P:CDP-diacylglycerol biosynthetic process; IEA:UniProtKB-UniPathway.
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; Lipid biosynthesis;
KW Lipid metabolism; Membrane; Nucleotidyltransferase;
KW Phospholipid biosynthesis; Phospholipid metabolism;
KW Reference proteome; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1 305 Phosphatidate cytidylyltransferase.
FT /FTId=PRO_0000090733.
FT TRANSMEM 27 47 Helical; (Potential).
FT TRANSMEM 67 87 Helical; (Potential).
FT TRANSMEM 96 116 Helical; (Potential).
FT TRANSMEM 124 144 Helical; (Potential).
FT TRANSMEM 150 170 Helical; (Potential).
FT TRANSMEM 202 222 Helical; (Potential).
FT TRANSMEM 232 252 Helical; (Potential).
FT TRANSMEM 277 297 Helical; (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
//
