ID CDSA_RICFE Reviewed; 227 AA. AC Q4ULR7; DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2005, sequence version 1. DT 27-MAR-2024, entry version 92. 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=RF_0655; OS Rickettsia felis (strain ATCC VR-1525 / URRWXCal2) (Rickettsia azadi). OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales; OC Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group. OX NCBI_TaxID=315456; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC VR-1525 / URRWXCal2; RX PubMed=15984913; DOI=10.1371/journal.pbio.0030248; RA Ogata H., Renesto P., Audic S., Robert C., Blanc G., Fournier P.-E., RA Parinello H., Claverie J.-M., Raoult D.; RT "The genome sequence of Rickettsia felis identifies the first putative RT conjugative plasmid in an obligate intracellular parasite."; RL PLoS Biol. 3:1-12(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:0000250}; Multi-pass membrane CC protein {ECO:0000250}. CC -!- SIMILARITY: Belongs to the CDS family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP000053; AAY61506.1; -; Genomic_DNA. DR AlphaFoldDB; Q4ULR7; -. DR SMR; Q4ULR7; -. DR STRING; 315456.RF_0655; -. DR KEGG; rfe:RF_0655; -. DR eggNOG; COG0575; Bacteria. DR HOGENOM; CLU_037294_1_1_5; -. DR OrthoDB; 9799199at2; -. DR UniPathway; UPA00557; UER00614. DR Proteomes; UP000008548; Chromosome. 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 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 Transferase; Transmembrane; Transmembrane helix. FT CHAIN 1..227 FT /note="Phosphatidate cytidylyltransferase" FT /id="PRO_0000281058" FT TRANSMEM 31..51 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 65..85 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 93..113 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 131..151 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 165..185 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 206..226 FT /note="Helical" FT /evidence="ECO:0000255" SQ SEQUENCE 227 AA; 25624 MW; 44E64F36CDE950FE CRC64; MITQKGKEHL AKDKQNIYLR ILSGIVLVPL FVIAILWFKP LFYILMILVG MGMLSEWYNM TYSSIPYLLI GLIIIPIPIS LLTFLSMEDT NRWLIMLYFC IIWSVDSFAM IGGKTFKGAK LAPKISPKKT WSGLVTGVLS AGLVAVLASF IPNFHIENYY FSNKIYLFII SCILALIAQS SDLFISYLKR KFNIKDSGHI IPGHGGVLDR FDSIILTAPV LFFISIL //