CDSA_ECOLI
ID CDSA_ECOLI Reviewed; 285 AA.
AC P0ABG1; P06466;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2007, sequence version 2.
DT 03-AUG-2022, entry version 108.
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; Synonyms=cds; OrderedLocusNames=b0175, JW5810;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2995358; DOI=10.1016/s0021-9258(17)38988-3;
RA Icho T., Sparrow C.P., Raetz C.R.H.;
RT "Molecular cloning and sequencing of the gene for CDP-diglyceride
RT synthetase of Escherichia coli.";
RL J. Biol. Chem. 260:12078-12083(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RA Takemoto K., Mori H., Murayama N., Kataoka K., Yano M., Itoh T.,
RA Yamamoto Y., Inokuchi H., Miki T., Hatada E., Fukuda R., Ichihara S.,
RA Mizuno T., Makino K., Nakata A., Yura T., Sampei G., Mizobuchi K.;
RT "Systematic sequencing of the Escherichia coli genome: analysis of the 4.0
RT - 6.0 min (189,987 - 281,416bp) region.";
RL Submitted (FEB-1996) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RA Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M.,
RA Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D.,
RA Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.;
RT "Sequence of minutes 4-25 of Escherichia coli.";
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [6]
RP CHARACTERIZATION.
RX PubMed=2995359; DOI=10.1016/s0021-9258(17)38989-5;
RA Sparrow C.P., Raetz C.R.H.;
RT "Purification and properties of the membrane-bound CDP-diglyceride
RT synthetase from Escherichia coli.";
RL J. Biol. Chem. 260:12084-12091(1985).
RN [7]
RP TOPOLOGY [LARGE SCALE ANALYSIS].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=15919996; DOI=10.1126/science.1109730;
RA Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.;
RT "Global topology analysis of the Escherichia coli inner membrane
RT proteome.";
RL Science 308:1321-1323(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; Multi-pass membrane protein.
CC -!- SIMILARITY: Belongs to the CDS family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA23545.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAB08604.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; M11330; AAA23545.1; ALT_INIT; Genomic_DNA.
DR EMBL; U70214; AAB08604.1; ALT_INIT; Genomic_DNA.
DR EMBL; U00096; AAC73286.2; -; Genomic_DNA.
DR EMBL; AP009048; BAA77850.2; -; Genomic_DNA.
DR PIR; A23898; SYECDG.
DR RefSeq; NP_414717.2; NC_000913.3.
DR RefSeq; WP_000922446.1; NZ_STEB01000032.1.
DR AlphaFoldDB; P0ABG1; -.
DR SMR; P0ABG1; -.
DR BioGRID; 4261198; 7.
DR STRING; 511145.b0175; -.
DR PaxDb; P0ABG1; -.
DR PRIDE; P0ABG1; -.
DR EnsemblBacteria; AAC73286; AAC73286; b0175.
DR EnsemblBacteria; BAA77850; BAA77850; BAA77850.
DR GeneID; 66671537; -.
DR GeneID; 944876; -.
DR KEGG; ecj:JW5810; -.
DR KEGG; eco:b0175; -.
DR PATRIC; fig|511145.12.peg.182; -.
DR EchoBASE; EB0137; -.
DR eggNOG; COG0575; Bacteria.
DR HOGENOM; CLU_037294_1_2_6; -.
DR InParanoid; P0ABG1; -.
DR OMA; WEWGRLN; -.
DR PhylomeDB; P0ABG1; -.
DR BioCyc; EcoCyc:CDPDIGLYSYN-MON; -.
DR BioCyc; MetaCyc:CDPDIGLYSYN-MON; -.
DR BRENDA; 2.7.7.41; 2026.
DR UniPathway; UPA00557; UER00614.
DR PRO; PR:P0ABG1; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0004605; F:phosphatidate cytidylyltransferase activity; IDA:EcoCyc.
DR GO; GO:0016024; P:CDP-diacylglycerol biosynthetic process; IDA:EcoCyc.
DR InterPro; IPR000374; PC_trans.
DR PROSITE; PS01315; CDS; 1.
PE 1: Evidence at protein level;
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..285
FT /note="Phosphatidate cytidylyltransferase"
FT /id="PRO_0000090734"
FT TRANSMEM 31..51
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 56..76
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 93..113
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 121..141
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 151..171
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 190..210
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 213..233
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 264..284
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 285 AA; 31454 MW; 0D77DCD5EC5FBA9F CRC64;
MLKYRLISAF VLIPVVIAAL FLLPPVGFAI VTLVVCMLAA WEWGQLSGFT TRSQRVWLAV
LCGLLLALML FLLPEYHRNI HQPLVEISLW ASLGWWIVAL LLVLFYPGSA AIWRNSKTLR
LIFGVLTIVP FFWGMLALRA WHYDENHYSG AIWLLYVMIL VWGADSGAYM FGKLFGKHKL
APKVSPGKTW QGFIGGLATA AVISWGYGMW ANLDVAPVTL LICSIVAALA SVLGDLTESM
FKREAGIKDS GHLIPGHGGI LDRIDSLTAA VPVFACLLLL VFRTL
