CDSA_HELPJ
ID CDSA_HELPJ Reviewed; 266 AA.
AC Q9ZML7;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 25-MAY-2022, entry version 116.
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=jhp_0201;
OS Helicobacter pylori (strain J99 / ATCC 700824) (Campylobacter pylori J99).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=85963;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=J99 / ATCC 700824;
RX PubMed=9923682; DOI=10.1038/16495;
RA Alm R.A., Ling L.-S.L., Moir D.T., King B.L., Brown E.D., Doig P.C.,
RA Smith D.R., Noonan B., Guild B.C., deJonge B.L., Carmel G., Tummino P.J.,
RA Caruso A., Uria-Nickelsen M., Mills D.M., Ives C., Gibson R., Merberg D.,
RA Mills S.D., Jiang Q., Taylor D.E., Vovis G.F., Trust T.J.;
RT "Genomic sequence comparison of two unrelated isolates of the human gastric
RT pathogen Helicobacter pylori.";
RL Nature 397:176-180(1999).
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; AE001439; AAD05785.1; -; Genomic_DNA.
DR PIR; F71961; F71961.
DR RefSeq; WP_000656959.1; NZ_CP011330.1.
DR AlphaFoldDB; Q9ZML7; -.
DR SMR; Q9ZML7; -.
DR STRING; 85963.jhp_0201; -.
DR EnsemblBacteria; AAD05785; AAD05785; jhp_0201.
DR KEGG; hpj:jhp_0201; -.
DR PATRIC; fig|85963.30.peg.817; -.
DR eggNOG; COG0575; Bacteria.
DR OMA; VFGDLYE; -.
DR UniPathway; UPA00557; UER00614.
DR Proteomes; UP000000804; Chromosome.
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..266
FT /note="Phosphatidate cytidylyltransferase"
FT /id="PRO_0000090738"
FT TRANSMEM 16..36
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 52..72
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 78..98
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 101..121
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 125..145
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 164..184
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 186..206
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 237..257
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 266 AA; 28788 MW; 99C48ED30B45AF45 CRC64;
MKEELFKEKS RYITGVVLIV VAGLILYADN LLLFWAVLGG IYAVGFFEAL RLFQVKASFS
LYLILVLSWV AAYFNGHPVE CALISAMVMA SVIAYQKAHH SEAILPFLYP GVGFFALFGV
YKDFGAVAII WLLVVVVASD VGAFFGGKLL GKTPFTATSP NKTLEGALIG VVLASVLGSF
VGMGKLSGGF LMALLFSFLI ALMAVFGDLY ESYLKRKVGV KDSGKILPGH GGVLDRLDSM
LFGALSLHVL LYFLEIWKET AVFLGD