CDSA_CHLTR
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 25-MAY-2022, entry version 112.
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., Davis R.W.;
RT "Genome sequence of an obligate intracellular pathogen of humans: Chlamydia
RT trachomatis.";
RL Science 282:754-759(1998).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphate + CTP + H(+) = a CDP-1,2-
CC diacyl-sn-glycerol + diphosphate; Xref=Rhea:RHEA:16229,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:37563,
CC ChEBI:CHEBI:58332, ChEBI:CHEBI:58608; EC=2.7.7.41;
CC -!- PATHWAY: Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-
CC diacylglycerol from sn-glycerol 3-phosphate: step 3/3.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the CDS family. {ECO:0000305}.
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DR EMBL; AE001273; AAC68051.1; -; Genomic_DNA.
DR PIR; F71512; F71512.
DR RefSeq; NP_219964.1; NC_000117.1.
DR RefSeq; WP_009871809.1; NC_000117.1.
DR AlphaFoldDB; O84457; -.
DR SMR; O84457; -.
DR STRING; 813.O172_02470; -.
DR EnsemblBacteria; AAC68051; AAC68051; CT_451.
DR GeneID; 884225; -.
DR KEGG; ctr:CT_451; -.
DR PATRIC; fig|272561.5.peg.488; -.
DR HOGENOM; CLU_037294_3_3_0; -.
DR InParanoid; O84457; -.
DR OMA; GCIFLTM; -.
DR UniPathway; UPA00557; UER00614.
DR Proteomes; UP000000431; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0004605; F:phosphatidate cytidylyltransferase activity; IBA:GO_Central.
DR GO; GO:0016024; P:CDP-diacylglycerol biosynthetic process; IBA:GO_Central.
PE 3: Inferred from homology;
KW Cell membrane; Lipid biosynthesis; Lipid metabolism; Membrane;
KW Nucleotidyltransferase; Phospholipid biosynthesis; Phospholipid metabolism;
KW Reference proteome; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..305
FT /note="Phosphatidate cytidylyltransferase"
FT /id="PRO_0000090733"
FT TRANSMEM 27..47
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 67..87
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 96..116
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 124..144
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 150..170
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 202..222
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 232..252
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 277..297
FT /note="Helical"
FT /evidence="ECO:0000255"
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
