ID   CDSA_STAEQ              Reviewed;         260 AA.
AC   Q5HPT0;
DT   07-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   25-MAY-2022, entry version 87.
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=SERP0828;
OS   Staphylococcus epidermidis (strain ATCC 35984 / RP62A).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=176279;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35984 / RP62A;
RX   PubMed=15774886; DOI=10.1128/jb.187.7.2426-2438.2005;
RA   Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T., Ravel J.,
RA   Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J., Dodson R.J.,
RA   Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., Haft D.H.,
RA   Vamathevan J.J., Khouri H., Utterback T.R., Lee C., Dimitrov G., Jiang L.,
RA   Qin H., Weidman J., Tran K., Kang K.H., Hance I.R., Nelson K.E.,
RA   Fraser C.M.;
RT   "Insights on evolution of virulence and resistance from the complete genome
RT   analysis of an early methicillin-resistant Staphylococcus aureus strain and
RT   a biofilm-producing methicillin-resistant Staphylococcus epidermidis
RT   strain.";
RL   J. Bacteriol. 187:2426-2438(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 membrane {ECO:0000250}; Multi-pass membrane
CC       protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the CDS family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000029; AAW54181.1; -; Genomic_DNA.
DR   RefSeq; WP_001829499.1; NC_002976.3.
DR   AlphaFoldDB; Q5HPT0; -.
DR   SMR; Q5HPT0; -.
DR   STRING; 176279.SERP0828; -.
DR   EnsemblBacteria; AAW54181; AAW54181; SERP0828.
DR   GeneID; 50018927; -.
DR   KEGG; ser:SERP0828; -.
DR   eggNOG; COG4589; Bacteria.
DR   HOGENOM; CLU_037294_2_2_9; -.
DR   OMA; FTFDEVG; -.
DR   OrthoDB; 1533756at2; -.
DR   UniPathway; UPA00557; UER00614.
DR   Proteomes; UP000000531; 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   Reference proteome; Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..260
FT                   /note="Phosphatidate cytidylyltransferase"
FT                   /id="PRO_0000090754"
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;  29179 MW;  B52A542C097449B9 CRC64;
     MKVRTLTAII ALLIFLPILL KGGLILMLFA FLLALIALKE LLNMNMIKFL SIPGLISALA
     LIIIMLPQDA GEWVQVIQLK GLIAMSFIVL SYTVLSKNRF SFMDAAFCLM SVAYVGIGFM
     YFYETRSEGL RYILFAFLIV WLTDTGAYIF GRLMGKHKLW PVISPNKTIE GFFGGILCSI
     LVPLVMQMFV DLHMNIWLLL LVTIVLSMFG QLGDLVESGF KRHFGVKDSG RILPGHGGIL
     DRFDSFMFVL PLLNILLIQT