ID Q888N3_PSESM Unreviewed; 283 AA.
AC Q888N3;
DT 01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT 01-JUN-2003, sequence version 1.
DT 27-MAR-2024, entry version 102.
DE RecName: Full=CDP-diacylglycerol--glycerol-3-phosphate 3-phosphatidyltransferase {ECO:0000256|ARBA:ARBA00014944};
DE EC=2.7.8.5 {ECO:0000256|ARBA:ARBA00013170};
DE EC=2.7.8.8 {ECO:0000256|ARBA:ARBA00013174};
DE AltName: Full=CDP-diacylglycerol--serine O-phosphatidyltransferase {ECO:0000256|ARBA:ARBA00017171};
DE AltName: Full=Phosphatidylserine synthase {ECO:0000256|ARBA:ARBA00032361};
GN Name=pssA-1 {ECO:0000313|EMBL:AAO54518.1};
GN OrderedLocusNames=PSPTO_0984 {ECO:0000313|EMBL:AAO54518.1};
OS Pseudomonas syringae pv. tomato (strain ATCC BAA-871 / DC3000).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=223283 {ECO:0000313|EMBL:AAO54518.1, ECO:0000313|Proteomes:UP000002515};
RN [1] {ECO:0000313|EMBL:AAO54518.1, ECO:0000313|Proteomes:UP000002515}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-871 / DC3000 {ECO:0000313|Proteomes:UP000002515};
RX PubMed=12928499; DOI=10.1073/pnas.1731982100;
RA Buell C.R., Joardar V., Lindeberg M., Selengut J., Paulsen I.T.,
RA Gwinn M.L., Dodson R.J., Deboy R.T., Durkin A.S., Kolonay J.F., Madupu R.,
RA Daugherty S., Brinkac L., Beanan M.J., Haft D.H., Nelson W.C., Davidsen T.,
RA Zafar N., Zhou L., Liu J., Yuan Q., Khouri H., Fedorova N., Tran B.,
RA Russell D., Berry K., Utterback T., Van Aken S.E., Feldblyum T.V.,
RA D'Ascenzo M., Deng W.L., Ramos A.R., Alfano J.R., Cartinhour S.,
RA Chatterjee A.K., Delaney T.P., Lazarowitz S.G., Martin G.B.,
RA Schneider D.J., Tang X., Bender C.L., White O., Fraser C.M., Collmer A.;
RT "The complete genome sequence of the Arabidopsis and tomato pathogen
RT Pseudomonas syringae pv. tomato DC3000.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:10181-10186(2003).
CC -!- FUNCTION: This protein catalyzes the committed step to the synthesis of
CC the acidic phospholipids. {ECO:0000256|ARBA:ARBA00003973}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a CDP-1,2-diacyl-sn-glycerol + L-serine = a 1,2-diacyl-sn-
CC glycero-3-phospho-L-serine + CMP + H(+); Xref=Rhea:RHEA:16913,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:33384, ChEBI:CHEBI:57262,
CC ChEBI:CHEBI:58332, ChEBI:CHEBI:60377; EC=2.7.8.8;
CC Evidence={ECO:0000256|ARBA:ARBA00000287};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a CDP-1,2-diacyl-sn-glycerol + sn-glycerol 3-phosphate = 1,2-
CC diacyl-sn-glycero-3-phospho-(1'-sn-glycero-3'-phosphate) + CMP +
CC H(+); Xref=Rhea:RHEA:12593, ChEBI:CHEBI:15378, ChEBI:CHEBI:57597,
CC ChEBI:CHEBI:58332, ChEBI:CHEBI:60110, ChEBI:CHEBI:60377; EC=2.7.8.5;
CC Evidence={ECO:0000256|ARBA:ARBA00001566};
CC -!- PATHWAY: Phospholipid metabolism; phosphatidylglycerol biosynthesis;
CC phosphatidylglycerol from CDP-diacylglycerol: step 1/2.
CC {ECO:0000256|ARBA:ARBA00005042}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the CDP-alcohol phosphatidyltransferase class-I
CC family. {ECO:0000256|ARBA:ARBA00010441, ECO:0000256|RuleBase:RU003750}.
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DR EMBL; AE016853; AAO54518.1; -; Genomic_DNA.
DR RefSeq; NP_790823.1; NC_004578.1.
DR RefSeq; WP_005770492.1; NC_004578.1.
DR AlphaFoldDB; Q888N3; -.
DR STRING; 223283.PSPTO_0984; -.
DR GeneID; 1182613; -.
DR KEGG; pst:PSPTO_0984; -.
DR PATRIC; fig|223283.9.peg.993; -.
DR eggNOG; COG1183; Bacteria.
DR HOGENOM; CLU_049944_2_0_6; -.
DR OrthoDB; 9777147at2; -.
DR PhylomeDB; Q888N3; -.
DR Proteomes; UP000002515; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0003882; F:CDP-diacylglycerol-serine O-phosphatidyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0008654; P:phospholipid biosynthetic process; IEA:UniProtKB-KW.
DR Gene3D; 1.20.120.1760; -; 1.
DR InterPro; IPR004533; CDP-diaglyc--ser_O-PTrfase.
DR InterPro; IPR000462; CDP-OH_P_trans.
DR InterPro; IPR043130; CDP-OH_PTrfase_TM_dom.
DR InterPro; IPR048254; CDP_ALCOHOL_P_TRANSF_CS.
DR NCBIfam; TIGR00473; pssA; 1.
DR PANTHER; PTHR14269; CDP-DIACYLGLYCEROL--GLYCEROL-3-PHOSPHATE 3-PHOSPHATIDYLTRANSFERASE-RELATED; 1.
DR PANTHER; PTHR14269:SF61; CDP-DIACYLGLYCEROL--SERINE O-PHOSPHATIDYLTRANSFERASE; 1.
DR Pfam; PF01066; CDP-OH_P_transf; 1.
DR PROSITE; PS00379; CDP_ALCOHOL_P_TRANSF; 1.
PE 3: Inferred from homology;
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 Phospholipid biosynthesis {ECO:0000256|ARBA:ARBA00023209};
KW Phospholipid metabolism {ECO:0000256|ARBA:ARBA00023264};
KW Reference proteome {ECO:0000313|Proteomes:UP000002515};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003750};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 40..60
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 80..97
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 118..137
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 143..161
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 173..193
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 205..224
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 236..252
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 258..276
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 283 AA; 30278 MW; 03CB0388C3A23C3C CRC64;
MSERPEEPNK ASDAESLLPI DEHVEEGHDA EGRQVRHRGI YLLPNLFTTA NLFAGFYSII
SSMSAQSAMS AGDSAAASKY FAFAAIAIFV AMVLDGLDGR VARMTNTQSA FGAEYDSLSD
MVAFGVAPAL LAFGWALGDM GKVGWMVAFI YVAGAALRLA RFNTQVGKAD KRYFIGLASP
AAAGVVAGTV WAFSDFGIQG SKLSFLVALL VAAAGMLMVS NIKYNSFKEL DLKGRVPFVA
ILAVVLVFAV VFSDPPRILL LIFLAYALSG PIQYLLRRHK ASQ
//
