ID E6YZI8_BARSR Unreviewed; 258 AA.
AC E6YZI8;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 24-JAN-2024, entry version 39.
DE RecName: Full=Phosphatidylcholine synthase {ECO:0000256|ARBA:ARBA00015623, ECO:0000256|PIRNR:PIRNR000851};
DE Short=PC synthase {ECO:0000256|PIRNR:PIRNR000851};
DE Short=PCS {ECO:0000256|PIRNR:PIRNR000851};
DE EC=2.7.8.24 {ECO:0000256|ARBA:ARBA00013195, ECO:0000256|PIRNR:PIRNR000851};
DE AltName: Full=CDP-diglyceride-choline O-phosphatidyltransferase {ECO:0000256|ARBA:ARBA00033321, ECO:0000256|PIRNR:PIRNR000851};
GN ORFNames=B11C_40131 {ECO:0000313|EMBL:CBI82276.1}, BscR1v2_008050
GN {ECO:0000313|EMBL:AQX30740.1};
OS Bartonella schoenbuchensis (strain DSM 13525 / NCTC 13165 / R1).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Bartonellaceae; Bartonella.
OX NCBI_TaxID=687861 {ECO:0000313|EMBL:CBI82276.1};
RN [1] {ECO:0000313|EMBL:CBI82276.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=R1 {ECO:0000313|EMBL:CBI82276.1};
RX PubMed=21347280; DOI=10.1371/journal.pgen.1001296;
RA Engel P., Salzburger W., Liesch M., Chang C.C., Maruyama S., Lanz C.,
RA Calteau A., Lajus A., Medigue C., Schuster S.C., Dehio C.;
RT "Parallel evolution of a type IV secretion system in radiating lineages of
RT the host-restricted bacterial pathogen Bartonella.";
RL PLoS Genet. 7:E1001296-E1001296(2011).
RN [2] {ECO:0000313|Proteomes:UP000190811}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R1 {ECO:0000313|Proteomes:UP000190811};
RX PubMed=28338931; DOI=10.1093/gbe/evx042;
RA Harms A., Segers F.H., Quebatte M., Mistl C., Manfredi P., Korner J.,
RA Chomel B.B., Kosoy M., Maruyama S., Engel P., Dehio C.;
RT "Evolutionary Dynamics of Pathoadaptation Revealed by Three Independent
RT Acquisitions of the VirB/D4 Type IV Secretion System in Bartonella.";
RL Genome Biol. Evol. 9:761-776(2017).
RN [3] {ECO:0000313|EMBL:AQX30740.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R1 {ECO:0000313|EMBL:AQX30740.1};
RA Harms A., Segers F.H.I.D., Quebatte M., Mistl C., Manfredi P., Koerner J.,
RA Chomel B., Kosoy M., Maruyama S., Engel P., Dehio C.;
RT "Evolutionary dynamics of pathoadaptation revealed by three independent
RT acquisitions of the VirB/D4 type IV secretion system in Bartonella.";
RL Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Condenses choline with CDP-diglyceride to produce
CC phosphatidylcholine and CMP. {ECO:0000256|ARBA:ARBA00037468,
CC ECO:0000256|PIRNR:PIRNR000851}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a CDP-1,2-diacyl-sn-glycerol + choline = a 1,2-diacyl-sn-
CC glycero-3-phosphocholine + CMP + H(+); Xref=Rhea:RHEA:14597,
CC ChEBI:CHEBI:15354, ChEBI:CHEBI:15378, ChEBI:CHEBI:57643,
CC ChEBI:CHEBI:58332, ChEBI:CHEBI:60377; EC=2.7.8.24;
CC Evidence={ECO:0000256|ARBA:ARBA00000958,
CC ECO:0000256|PIRNR:PIRNR000851};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936,
CC ECO:0000256|PIRNR:PIRNR000851};
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000256|ARBA:ARBA00004429, ECO:0000256|PIRNR:PIRNR000851}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004429,
CC ECO:0000256|PIRNR:PIRNR000851}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the CDP-alcohol phosphatidyltransferase class-I
CC family. {ECO:0000256|PIRNR:PIRNR000851}.
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DR EMBL; CP019789; AQX30740.1; -; Genomic_DNA.
DR EMBL; FN645509; CBI82276.1; -; Genomic_DNA.
DR AlphaFoldDB; E6YZI8; -.
DR STRING; 687861.BscR1v2_008050; -.
DR Proteomes; UP000190811; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0050520; F:phosphatidylcholine synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0008654; P:phospholipid biosynthetic process; IEA:UniProtKB-KW.
DR Gene3D; 1.20.120.1760; -; 1.
DR InterPro; IPR000462; CDP-OH_P_trans.
DR InterPro; IPR043130; CDP-OH_PTrfase_TM_dom.
DR InterPro; IPR026027; PcS.
DR Pfam; PF01066; CDP-OH_P_transf; 1.
DR PIRSF; PIRSF000851; PcS; 1.
PE 3: Inferred from homology;
KW Cell inner membrane {ECO:0000256|ARBA:ARBA00022519,
KW ECO:0000256|PIRNR:PIRNR000851};
KW Cell membrane {ECO:0000256|PIRNR:PIRNR000851};
KW Lipid biosynthesis {ECO:0000256|PIRNR:PIRNR000851};
KW Lipid metabolism {ECO:0000256|PIRNR:PIRNR000851};
KW Manganese {ECO:0000256|PIRNR:PIRNR000851};
KW Membrane {ECO:0000256|PIRNR:PIRNR000851, ECO:0000256|SAM:Phobius};
KW Phospholipid biosynthesis {ECO:0000256|PIRNR:PIRNR000851};
KW Phospholipid metabolism {ECO:0000256|PIRNR:PIRNR000851};
KW Transferase {ECO:0000256|PIRNR:PIRNR000851, ECO:0000313|EMBL:CBI82276.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 26..48
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 116..134
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 146..163
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 169..188
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 200..218
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 224..247
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 258 AA; 29163 MW; 360F7926B476360A CRC64;
MRRKLTRKIK TNTDRLRSKT VTMPQARAFS VHLLTASGSF LAFLSLIAAS KKEWIAMFYW
LGLALLVDGI DGPIARKLNV KSILPTWSGE LLDNIIDYVT YVLIPAFALY QSGFMGAGLS
FLLSAIIVIS SAIYYADTGM KTKENFFKGF PVVWNMMIFT LFVVRPEEWV AFVIIFLSAI
LSFLPIYFIH PIRVIRLRML NLSVFLAWCS FGIAAFFYQL NAPHWIKIGI SITGIYIYCI
GAIMQLFPTL GAQKSDPK
//
