ID   CDSA_MYCGE              Reviewed;         305 AA.
AC   Q49433; Q49309;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   16-JUN-2009, entry version 56.
DE   RecName: Full=Putative phosphatidate cytidylyltransferase;
DE            EC=2.7.7.41;
DE   AltName: Full=CDP-diglyceride pyrophosphorylase;
DE   AltName: Full=CDP-diglyceride synthetase;
DE   AltName: Full=CDP-diacylglycerol synthase;
DE            Short=CDS;
DE   AltName: Full=CTP:phosphatidate cytidylyltransferase;
DE   AltName: Full=CDP-DG synthetase;
DE   AltName: Full=CDP-DAG synthase;
GN   Name=cdsA; OrderedLocusNames=MG437;
OS   Mycoplasma genitalium.
OC   Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX   NCBI_TaxID=2097;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33530 / G-37 / NCTC 10195;
RX   MEDLINE=96026346; 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 127-226.
RC   STRAIN=ATCC 33530 / G-37 / NCTC 10195;
RX   MEDLINE=94075230; PubMed=8253680;
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
RT   sequencing.";
RL   J. Bacteriol. 175:7918-7930(1993).
CC   -!- CATALYTIC ACTIVITY: CTP + phosphatidate = diphosphate + CDP-
CC       diacylglycerol.
CC   -!- PATHWAY: Phospholipid metabolism; CDP-diacylglycerol biosynthesis;
CC       CDP-diacylglycerol from sn-glycerol 3-phosphate: step 3/3.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein
CC       (By similarity).
CC   -!- SIMILARITY: Belongs to the CDS family.
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DR   EMBL; L43967; AAC72458.1; ALT_INIT; Genomic_DNA.
DR   EMBL; U02189; AAD12473.1; -; Genomic_DNA.
DR   PIR; T09771; T09771.
DR   RefSeq; NP_073107.2; -.
DR   GeneID; 875619; -.
DR   GenomeReviews; L43967_GR; MG437.
DR   KEGG; mge:MG_437; -.
DR   TIGR; MG437; -.
DR   HOGENOM; Q49433; -.
DR   BioCyc; MGEN243273:MG_437-MON; -.
DR   BRENDA; 2.7.7.41; 110.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004605; F:phosphatidate cytidylyltransferase activity; IEA:EC.
DR   GO; GO:0008654; P:phospholipid biosynthetic process; IEA:UniProtKB-KW.
DR   InterPro; IPR000374; PC_trans.
DR   Pfam; PF01148; CTP_transf_1; 1.
DR   PROSITE; PS01315; CDS; 1.
PE   3: Inferred from homology;
KW   Cell membrane; Complete proteome; Membrane; Nucleotidyltransferase;
KW   Phospholipid biosynthesis; Transferase; Transmembrane.
FT   CHAIN         1    305       Putative phosphatidate
FT                                cytidylyltransferase.
FT                                /FTId=PRO_0000090739.
FT   TRANSMEM     22     42       Potential.
FT   TRANSMEM     51     71       Potential.
FT   TRANSMEM     84    104       Potential.
FT   TRANSMEM    107    127       Potential.
FT   TRANSMEM    152    172       Potential.
FT   TRANSMEM    212    232       Potential.
FT   TRANSMEM    264    284       Potential.
SQ   SEQUENCE   305 AA;  34196 MW;  F149FA6BD9DDC080 CRC64;
     MIWELFTNIL KNKPKLSLSL TLLNAGIIIF GMIGTFVVVY FYKWNATVNG IWTLSFTLSV
     VLLWIIYIAC MSKTRIKFSL QLSYSLGAIA CFIASIGTIY FSVIRGWTTI FLLMSLAVSV
     DTFPFLFGKR FGKNPLIKIS PSKTWEGAFF GIISTIVVVA LLCVLYSIPF FVAKPTFNQT
     NGIALNTPQN YDSHNLITNI FLIAFISGGS SFYIYWWVST LALIFTGSVF AIGGDLFFSY
     IKRLISIKDF SKVLGKHGGV LDRFDSSSFL ISFFFVYHLI AGTISNQRLL MEPNTYFSAI
     TSIQS
//