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CDSA_MYCGE
ID   CDSA_MYCGE              Reviewed;         397 AA.
AC   Q49433; Q49309;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   31-JAN-2018, sequence version 2.
DT   03-AUG-2022, entry version 115.
DE   RecName: Full=Putative 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=MG437;
OS   Mycoplasma genitalium (strain ATCC 33530 / DSM 19775 / NCTC 10195 / G37)
OS   (Mycoplasmoides genitalium).
OC   Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX   NCBI_TaxID=243273;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33530 / DSM 19775 / NCTC 10195 / G37;
RX   PubMed=7569993; DOI=10.1126/science.270.5235.397;
RA   Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A.,
RA   Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M.,
RA   Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L.,
RA   Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M.,
RA   Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S.,
RA   Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.;
RT   "The minimal gene complement of Mycoplasma genitalium.";
RL   Science 270:397-403(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 219-318.
RC   STRAIN=ATCC 33530 / DSM 19775 / NCTC 10195 / G37;
RX   PubMed=8253680; DOI=10.1128/jb.175.24.7918-7930.1993;
RA   Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III;
RT   "A survey of the Mycoplasma genitalium genome by using random sequencing.";
RL   J. Bacteriol. 175:7918-7930(1993).
RN   [3]
RP   SEQUENCE REVISION TO N-TERMINUS AND 124, AND DISRUPTION PHENOTYPE.
RC   STRAIN=ATCC 33530 / DSM 19775 / NCTC 10195 / G37;
RX   PubMed=16407165; DOI=10.1073/pnas.0510013103;
RA   Glass J.I., Assad-Garcia N., Alperovich N., Yooseph S., Lewis M.R.,
RA   Maruf M., Hutchison C.A. III, Smith H.O., Venter J.C.;
RT   "Essential genes of a minimal bacterium.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:425-430(2006).
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   -!- DISRUPTION PHENOTYPE: Not essential, it can be deleted.
CC       {ECO:0000269|PubMed:16407165}.
CC   -!- SIMILARITY: Belongs to the CDS family. {ECO:0000305}.
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DR   EMBL; L43967; AAC72458.2; -; Genomic_DNA.
DR   EMBL; U02189; AAD12473.1; -; Genomic_DNA.
DR   PIR; T09771; T09771.
DR   RefSeq; WP_009885597.1; NZ_AAGX01000001.1.
DR   AlphaFoldDB; Q49433; -.
DR   STRING; 243273.MG_437; -.
DR   EnsemblBacteria; AAC72458; AAC72458; MG_437.
DR   KEGG; mge:MG_437; -.
DR   eggNOG; COG0575; Bacteria.
DR   HOGENOM; CLU_694118_0_0_14; -.
DR   OrthoDB; 1533756at2; -.
DR   UniPathway; UPA00557; UER00614.
DR   Proteomes; UP000000807; 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   InterPro; IPR016720; PC_Trfase_euk.
DR   PANTHER; PTHR13773; PTHR13773; 1.
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..397
FT                   /note="Putative phosphatidate cytidylyltransferase"
FT                   /id="PRO_0000090739"
FT   TRANSMEM        13..33
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        78..98
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        114..134
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        143..163
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        176..196
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        199..219
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        244..264
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        288..310
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        317..339
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        356..376
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   397 AA;  44484 MW;  D2591CFF7663A58E CRC64;
     MNEKAKQFIK KRTSVFIALL VVFCFFLLIS AFADGFNFWS PWSADFNSRT LKVEQASGVT
     SVISTEINEN FKAVRFSFSI IIILIVGVIG SLMIWELFTN ILKNKPKLSL SLTLLNAGII
     IFGMIGTFVV VYFYKWNATV NGIWTLSFTL SVVLLWIIYI ACMSKTRIKF SLQLSYSLGA
     IACFIASIGT IYFSVIRGWT TIFLLMSLAV SVDTFSFLFG KRFGKNPLIK ISPSKTWEGA
     FFGIISTIVV VALLCVLYSI PFFVAKPTFN QTNGIALNTP QNYDSHNLIT NIFLIAFISG
     GSSFYIYWWV STLALIFTGS VFAIGGDLFF SYIKRLISIK DFSKVLGKHG GVLDRFDSSS
     FLISFFFVYH LIAGTISNQR LLMEPNTYFS AITSIQS
 
 
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