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Database: UniProt
Entry: A0A0C4YA13_9BURK
LinkDB: A0A0C4YA13_9BURK
Original site: A0A0C4YA13_9BURK 
ID   A0A0C4YA13_9BURK        Unreviewed;       273 AA.
AC   A0A0C4YA13;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=Phosphatidate cytidylyltransferase {ECO:0000256|ARBA:ARBA00019373, ECO:0000256|RuleBase:RU003938};
DE            EC=2.7.7.41 {ECO:0000256|ARBA:ARBA00012487, ECO:0000256|RuleBase:RU003938};
GN   ORFNames=RR42_m2398 {ECO:0000313|EMBL:AJG19790.1};
OS   Cupriavidus basilensis.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Cupriavidus.
OX   NCBI_TaxID=68895 {ECO:0000313|EMBL:AJG19790.1, ECO:0000313|Proteomes:UP000031843};
RN   [1] {ECO:0000313|EMBL:AJG19790.1, ECO:0000313|Proteomes:UP000031843}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=4G11 {ECO:0000313|EMBL:AJG19790.1};
RX   PubMed=25977418;
RA   Ray J., Waters R.J., Skerker J.M., Kuehl J.V., Price M.N., Huang J.,
RA   Chakraborty R., Arkin A.P., Deutschbauer A.;
RT   "Complete Genome Sequence of Cupriavidus basilensis 4G11, Isolated from the
RT   Oak Ridge Field Research Center Site.";
RL   Genome Announc. 3:0-0(2015).
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         ECO:0000256|RuleBase:RU003938};
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, ECO:0000256|RuleBase:RU003938}.
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       ECO:0000256|RuleBase:RU003938}.
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DR   EMBL; CP010536; AJG19790.1; -; Genomic_DNA.
DR   RefSeq; WP_043346944.1; NZ_CP010536.1.
DR   AlphaFoldDB; A0A0C4YA13; -.
DR   STRING; 68895.RR42_m2398; -.
DR   KEGG; cbw:RR42_m2398; -.
DR   OrthoDB; 9799199at2; -.
DR   UniPathway; UPA00557; UER00614.
DR   Proteomes; UP000031843; Chromosome main.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
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   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 {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:0000256|RuleBase:RU003938};
KW   Reference proteome {ECO:0000313|Proteomes:UP000031843};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003938};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW   ECO:0000256|RuleBase:RU003938};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        6..39
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        51..68
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        80..99
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        106..127
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        133..154
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        175..196
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        208..232
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
SQ   SEQUENCE   273 AA;  28823 MW;  B2BA757B61EF8D3A CRC64;
     MLLTRVITAV CLLLLILPIL FLAPPSALAG LVAVIVVLAG WEFGRLIGLR GFWPYVYAVA
     CLVALIGWHD AADRQALTRL LQIGVACWGV AVVLLARGVR QASPSFTLLG AILGLFMLPA
     FGHATLILRE LGIGVLLSVA VLVWAADIGA YFVGKAIGRR KLAPTISPGK SWEGALGGWL
     LVLLIALGLA ATQAFSPTWF SRMADHNGLA VVALLSTLLV VASVVGDLFE SLLKRQVGMK
     DSSRLLPGHG GVLDRIDALL PVFPLAALLA IYL
//
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