CDSA_BRUA2
ID CDSA_BRUA2 Reviewed; 270 AA.
AC Q2YRP9; Q57CY2; Q59173;
DT 07-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 25-MAY-2022, 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=BAB1_1179;
OS Brucella abortus (strain 2308).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX NCBI_TaxID=359391;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Bearden S.W., Ficht T.A.;
RT "Isolation and sequence of the group 1 outer membrane protein of Brucella
RT abortus.";
RL Submitted (MAR-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2308;
RX PubMed=16299333; DOI=10.1128/iai.73.12.8353-8361.2005;
RA Chain P.S., Comerci D.J., Tolmasky M.E., Larimer F.W., Malfatti S.A.,
RA Vergez L.M., Aguero F., Land M.L., Ugalde R.A., Garcia E.;
RT "Whole-genome analyses of speciation events in pathogenic Brucellae.";
RL Infect. Immun. 73:8353-8361(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; U51683; AAA96785.1; -; Genomic_DNA.
DR EMBL; AM040264; CAJ11135.1; -; Genomic_DNA.
DR RefSeq; WP_002964284.1; NZ_KN046823.1.
DR AlphaFoldDB; Q2YRP9; -.
DR SMR; Q2YRP9; -.
DR STRING; 359391.BAB1_1179; -.
DR EnsemblBacteria; CAJ11135; CAJ11135; BAB1_1179.
DR GeneID; 3788651; -.
DR KEGG; bmf:BAB1_1179; -.
DR PATRIC; fig|359391.11.peg.77; -.
DR HOGENOM; CLU_037294_1_1_5; -.
DR OMA; PKFWPRV; -.
DR PhylomeDB; Q2YRP9; -.
DR UniPathway; UPA00557; UER00614.
DR Proteomes; UP000002719; 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; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..270
FT /note="Phosphatidate cytidylyltransferase"
FT /id="PRO_0000090728"
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