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Database: UniProt
Entry: F1T539_9ACTN
LinkDB: F1T539_9ACTN
Original site: F1T539_9ACTN 
ID   F1T539_9ACTN            Unreviewed;       329 AA.
AC   F1T539;
DT   31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   31-MAY-2011, sequence version 1.
DT   27-MAR-2024, entry version 43.
DE   RecName: Full=Phosphatidate cytidylyltransferase {ECO:0000256|ARBA:ARBA00019373};
DE            EC=2.7.7.41 {ECO:0000256|ARBA:ARBA00012487};
DE   AltName: Full=CDP-DAG synthase {ECO:0000256|ARBA:ARBA00032253};
DE   AltName: Full=CDP-DG synthase {ECO:0000256|ARBA:ARBA00032743};
DE   AltName: Full=CDP-diacylglycerol synthase {ECO:0000256|ARBA:ARBA00029893};
DE   AltName: Full=CDP-diglyceride pyrophosphorylase {ECO:0000256|ARBA:ARBA00032396};
DE   AltName: Full=CDP-diglyceride synthase {ECO:0000256|ARBA:ARBA00033406};
DE   AltName: Full=CTP:phosphatidate cytidylyltransferase {ECO:0000256|ARBA:ARBA00031825};
GN   Name=cdsA {ECO:0000313|EMBL:EGF23805.1};
GN   ORFNames=HMPREF0091_10752 {ECO:0000313|EMBL:EGF23805.1};
OS   Fannyhessea vaginae DSM 15829.
OC   Bacteria; Actinomycetota; Coriobacteriia; Coriobacteriales; Atopobiaceae;
OC   Fannyhessea.
OX   NCBI_TaxID=525256 {ECO:0000313|EMBL:EGF23805.1, ECO:0000313|Proteomes:UP000005947};
RN   [1] {ECO:0000313|EMBL:EGF23805.1, ECO:0000313|Proteomes:UP000005947}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15829 {ECO:0000313|EMBL:EGF23805.1,
RC   ECO:0000313|Proteomes:UP000005947};
RA   Muzny D., Qin X., Buhay C., Dugan-Rocha S., Ding Y., Chen G., Hawes A.,
RA   Holder M., Jhangiani S., Johnson A., Khan Z., Li Z., Liu W., Liu X.,
RA   Perez L., Shen H., Wang Q., Watt J., Xi L., Xin Y., Zhou J., Deng J.,
RA   Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L., Villasana D., Johnson A.,
RA   Liu J., Liyanage D., Lorensuhewa L., Robinson T., Song A., Song B.-B.,
RA   Dinh H., Thornton R., Coyle M., Francisco L., Jackson L., Javaid M.,
RA   Korchina V., Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., Nguyen N.,
RA   Okwuonu G., Ongeri F., Pham C., Simmons D., Wilczek-Boney K., Hale W.,
RA   Jakkamsetti A., Pham P., Ruth R., San Lucas F., Warren J., Zhang J.,
RA   Zhao Z., Zhou C., Zhu D., Lee S., Bess C., Blankenburg K., Forbes L.,
RA   Fu Q., Gubbala S., Hirani K., Jayaseelan J.C., Lara F., Munidasa M.,
RA   Palculict T., Patil S., Pu L.-L., Saada N., Tang L., Weissenberger G.,
RA   Zhu Y., Hemphill L., Shang Y., Youmans B., Ayvaz T., Ross M.,
RA   Santibanez J., Aqrawi P., Gross S., Joshi V., Fowler G., Nazareth L.,
RA   Reid J., Worley K., Petrosino J., Highlander S., Gibbs R.;
RL   Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases.
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         Evidence={ECO:0000256|ARBA:ARBA00001698};
CC   -!- PATHWAY: Lipid metabolism. {ECO:0000256|ARBA:ARBA00005189}.
CC   -!- PATHWAY: Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-
CC       diacylglycerol from sn-glycerol 3-phosphate: step 3/3.
CC       {ECO:0000256|ARBA:ARBA00005119}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the CDS family. {ECO:0000256|ARBA:ARBA00010185}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EGF23805.1}.
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DR   EMBL; ACGK02000001; EGF23805.1; -; Genomic_DNA.
DR   RefSeq; WP_006302934.1; NZ_ADNA01000029.1.
DR   AlphaFoldDB; F1T539; -.
DR   GeneID; 78489560; -.
DR   eggNOG; COG0575; Bacteria.
DR   OrthoDB; 9799199at2; -.
DR   Proteomes; UP000005947; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004605; F:phosphatidate cytidylyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
DR   PANTHER; PTHR46382; PHOSPHATIDATE CYTIDYLYLTRANSFERASE; 1.
DR   PANTHER; PTHR46382:SF1; PHOSPHATIDATE CYTIDYLYLTRANSFERASE; 1.
DR   Pfam; PF01148; CTP_transf_1; 1.
PE   3: Inferred from homology;
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW   ECO:0000313|EMBL:EGF23805.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005947};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EGF23805.1};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        65..85
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        116..134
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        140..158
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        170..187
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        193..216
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        237..256
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        262..282
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        311..328
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   329 AA;  36118 MW;  A392BAB3A3DB2706 CRC64;
     MSKLHVFTKR GSAHKSEQEM RSRLTSGLGL ERGIKKLEER RSQKESVRQK GELKTQRARA
     WTEKLLLRVF SGVLYSVAVV SCIYADPTST AFAIAAMAWL CCSEFFHMIK LAHYNPYDFV
     GLFVALLFPI LALFNSYTLL LGTAILYALV LSVLYIASPH VTIADTALSF FAPMYTSLLF
     SHIVLLRCSQ PNFSAAVLTL VVMCSVWAND ISAYFVGCNF GKHPLAPTIS PHKSIEGFYG
     GLVASVAVWF GIYYFGLVHI SLGYALICGL VVGIVSVIGD LFESRIKRSV HLKDSGTIMP
     GHGGLLDRSD SMLFGCTAAY FLLVLGGLI
//
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