CDSA_BRUAB
ID CDSA_BRUAB Reviewed; 270 AA.
AC P0C102; Q57CY2; Q59173;
DT 07-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-FEB-2006, sequence version 1.
DT 03-AUG-2022, entry version 78.
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=BruAb1_1163;
OS Brucella abortus biovar 1 (strain 9-941).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX NCBI_TaxID=262698;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=9-941;
RX PubMed=15805518; DOI=10.1128/jb.187.8.2715-2726.2005;
RA Halling S.M., Peterson-Burch B.D., Bricker B.J., Zuerner R.L., Qing Z.,
RA Li L.-L., Kapur V., Alt D.P., Olsen S.C.;
RT "Completion of the genome sequence of Brucella abortus and comparison to
RT the highly similar genomes of Brucella melitensis and Brucella suis.";
RL J. Bacteriol. 187:2715-2726(2005).
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 inner membrane {ECO:0000250}; Multi-pass
CC membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the CDS family. {ECO:0000305}.
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DR EMBL; AE017223; AAX74502.1; -; Genomic_DNA.
DR RefSeq; WP_002964284.1; NC_006932.1.
DR AlphaFoldDB; P0C102; -.
DR SMR; P0C102; -.
DR EnsemblBacteria; AAX74502; AAX74502; BruAb1_1163.
DR GeneID; 3788651; -.
DR KEGG; bmb:BruAb1_1163; -.
DR HOGENOM; CLU_037294_1_1_5; -.
DR OMA; PKFWPRV; -.
DR UniPathway; UPA00557; UER00614.
DR Proteomes; UP000000540; Chromosome I.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004605; F:phosphatidate cytidylyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0016024; P:CDP-diacylglycerol biosynthetic process; IEA:UniProtKB-UniPathway.
DR InterPro; IPR000374; PC_trans.
DR PROSITE; PS01315; CDS; 1.
PE 3: Inferred from homology;
KW Cell inner membrane; Cell membrane; Lipid biosynthesis; Lipid metabolism;
KW Membrane; Nucleotidyltransferase; Phospholipid biosynthesis;
KW Phospholipid metabolism; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..270
FT /note="Phosphatidate cytidylyltransferase"
FT /id="PRO_0000090727"
FT TRANSMEM 19..39
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 53..73
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 76..96
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 101..121
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 126..146
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 183..203
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 248..268
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 270 AA; 28448 MW; 47F253043415FF06 CRC64;
MSNLQTRIIT AIVLGTITLW LTWVGGVGFT LFSIAIGLAM FYEWTELSAT RQTAFSRLFG
WAWLIVTGIL LILDRGALLT IGFLVAGCAI LLVTQWKSGR GWPAAGLFYA GFSALSLSLL
RGDEPFGFTT IVFLFAVVWS TDITAYFNGR ALGGPKLAPR FSPNKTWSGA IGGAAAAVAG
GLLVASLVAA PGGWGVPVLA LLLSIVSQIG DLAESWVKRQ FGAKDSGRLL PGHGGVLDRV
DGLVAAAALL YLFGAIFAEP DVLSAIFFSF
