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Database: UniProt
Entry: CDSA_BACSU
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ID   CDSA_BACSU              Reviewed;         269 AA.
AC   O31752;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   27-MAR-2024, entry version 129.
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=BSU16540;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA   Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA   Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA   Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA   Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA   Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA   Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA   Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA   Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA   Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA   Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA   Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA   Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA   Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA   Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA   Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA   Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA   Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA   Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA   Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
RN   [2]
RP   SUBCELLULAR LOCATION.
RX   PubMed=15743965; DOI=10.1128/jb.187.6.2163-2174.2005;
RA   Nishibori A., Kusaka J., Hara H., Umeda M., Matsumoto K.;
RT   "Phosphatidylethanolamine domains and localization of phospholipid
RT   synthases in Bacillus subtilis membranes.";
RL   J. Bacteriol. 187:2163-2174(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:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}. Note=Localized in the septal membrane.
CC       {ECO:0000269|PubMed:15743965}.
CC   -!- SIMILARITY: Belongs to the CDS family. {ECO:0000305}.
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DR   EMBL; AL009126; CAB13527.1; -; Genomic_DNA.
DR   PIR; G69597; G69597.
DR   RefSeq; NP_389536.1; NC_000964.3.
DR   RefSeq; WP_003231924.1; NZ_JNCM01000035.1.
DR   AlphaFoldDB; O31752; -.
DR   SMR; O31752; -.
DR   STRING; 224308.BSU16540; -.
DR   PaxDb; 224308-BSU16540; -.
DR   EnsemblBacteria; CAB13527; CAB13527; BSU_16540.
DR   GeneID; 939607; -.
DR   KEGG; bsu:BSU16540; -.
DR   PATRIC; fig|224308.43.peg.1749; -.
DR   eggNOG; COG4589; Bacteria.
DR   InParanoid; O31752; -.
DR   OrthoDB; 9799199at2; -.
DR   PhylomeDB; O31752; -.
DR   BioCyc; BSUB:BSU16540-MONOMER; -.
DR   SABIO-RK; O31752; -.
DR   UniPathway; UPA00557; UER00614.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0004605; F:phosphatidate cytidylyltransferase activity; IBA:GO_Central.
DR   GO; GO:0016024; P:CDP-diacylglycerol biosynthetic process; IBA:GO_Central.
DR   InterPro; IPR000374; PC_trans.
DR   PANTHER; PTHR46382; PHOSPHATIDATE CYTIDYLYLTRANSFERASE; 1.
DR   PANTHER; PTHR46382:SF1; PHOSPHATIDATE CYTIDYLYLTRANSFERASE; 1.
DR   Pfam; PF01148; CTP_transf_1; 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..269
FT                   /note="Phosphatidate cytidylyltransferase"
FT                   /id="PRO_0000090726"
FT   TRANSMEM        13..33
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        50..70
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        81..101
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        110..130
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        138..158
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        180..200
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        201..221
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        247..267
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   269 AA;  30211 MW;  E364690D8EC9DFC3 CRC64;
     MVDMKQRILT GVLAAIVFLF LVIVGKLPFT ILIYAMGSVA LFELLRMKKL KLVSLPGLIG
     LLLLWMFLLP SQYSFFEADG ISKMEIALFA VLLLLTYTVL VKNTFTFDEV GFITLAAIYI
     GMCFHYFIEI RNLDQYGLTY IFYACVVIWS TDSGAYFVGK SLGKRKLWPE ISPNKTVEGF
     AGGIVIALVL ATIFQLVAQL PIPYIYLLLI TLFLSVFGQL GDLVESALKR HYDVKDSGNI
     LPGHGGILDR FDSFLFVMPF LYFLLALFS
//
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