CDSA_STAAW
ID CDSA_STAAW Reviewed; 260 AA.
AC Q7A121;
DT 07-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 98.
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=MW1144;
OS Staphylococcus aureus (strain MW2).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=196620;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MW2;
RX PubMed=12044378; DOI=10.1016/s0140-6736(02)08713-5;
RA Baba T., Takeuchi F., Kuroda M., Yuzawa H., Aoki K., Oguchi A., Nagai Y.,
RA Iwama N., Asano K., Naimi T., Kuroda H., Cui L., Yamamoto K., Hiramatsu K.;
RT "Genome and virulence determinants of high virulence community-acquired
RT MRSA.";
RL Lancet 359:1819-1827(2002).
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; BA000033; BAB95009.1; -; Genomic_DNA.
DR RefSeq; WP_000868413.1; NC_003923.1.
DR AlphaFoldDB; Q7A121; -.
DR SMR; Q7A121; -.
DR EnsemblBacteria; BAB95009; BAB95009; BAB95009.
DR KEGG; sam:MW1144; -.
DR HOGENOM; CLU_037294_2_2_9; -.
DR OMA; FTFDEVG; -.
DR UniPathway; UPA00557; UER00614.
DR Proteomes; UP000000418; 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 membrane; Lipid biosynthesis; Lipid metabolism; Membrane;
KW Nucleotidyltransferase; Phospholipid biosynthesis; Phospholipid metabolism;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..260
FT /note="Phosphatidate cytidylyltransferase"
FT /id="PRO_0000090752"
FT TRANSMEM 9..29
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 46..66
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 70..90
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 102..122
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 130..150
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 172..192
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 196..216
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 260 AA; 28964 MW; 02C2727C3801C694 CRC64;
MKVRTLTAII ALIVFLPILL KGGLVLMIFA NILALIALKE LLNMNMIKFV SVPGLISAVG
LIIIMLPQHA GPWVQVIQLK SLIAMSFIVL SYTVLSKNRF SFMDAAFCLM SVAYVGIGFM
FFYETRSEGL HYILYAFLIV WLTDTGAYLF GKMMGKHKLW PVISPNKTIE GFIGGLFCSL
IVPLAMLYFV DFNMNVWILL GVTLILSLFG QLGDLVESGF KRHFGVKDSG RILPGHGGIL
DRFDSFMFVL PLLNILLIQS
