PGSA_PSEFL
ID PGSA_PSEFL Reviewed; 195 AA.
AC P45419;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=CDP-diacylglycerol--glycerol-3-phosphate 3-phosphatidyltransferase;
DE EC=2.7.8.5;
DE AltName: Full=Phosphatidylglycerophosphate synthase;
DE Short=PGP synthase;
GN Name=pgsA;
OS Pseudomonas fluorescens.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=294;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=BL915;
RX PubMed=8075420; DOI=10.1094/mpmi-7-0455;
RA Gaffney T.D., Lam S.T., Ligon J., Gates K., Frazelle A., Maio J., Hill S.,
RA Goodwin S., Torkewitz N., Allshouse A.M., Kempf H.J., Becker J.O.;
RT "Global regulation of expression of antifungal factors by a Pseudomonas
RT fluorescens biological control strain.";
RL Mol. Plant Microbe Interact. 7:455-463(1994).
CC -!- FUNCTION: This protein catalyzes the committed step to the synthesis of
CC the acidic phospholipids. {ECO:0000250}.
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 -!- PATHWAY: Phospholipid metabolism; phosphatidylglycerol biosynthesis;
CC phosphatidylglycerol from CDP-diacylglycerol: step 1/2.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the CDP-alcohol phosphatidyltransferase class-I
CC family. {ECO:0000305}.
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DR EMBL; L29642; AAA98757.1; -; Genomic_DNA.
DR AlphaFoldDB; P45419; -.
DR SMR; P45419; -.
DR UniPathway; UPA00084; UER00503.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008444; F:CDP-diacylglycerol-glycerol-3-phosphate 3-phosphatidyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0006655; P:phosphatidylglycerol biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 1.20.120.1760; -; 1.
DR InterPro; IPR000462; CDP-OH_P_trans.
DR InterPro; IPR043130; CDP-OH_PTrfase_TM_dom.
DR InterPro; IPR004570; Phosphatidylglycerol_P_synth.
DR Pfam; PF01066; CDP-OH_P_transf; 1.
DR PIRSF; PIRSF000847; Phos_ph_gly_syn; 1.
DR TIGRFAMs; TIGR00560; pgsA; 1.
DR PROSITE; PS00379; CDP_ALCOHOL_P_TRANSF; 1.
PE 3: Inferred from homology;
KW Cell membrane; Lipid biosynthesis; Lipid metabolism; Membrane;
KW Phospholipid biosynthesis; Phospholipid metabolism; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..195
FT /note="CDP-diacylglycerol--glycerol-3-phosphate 3-
FT phosphatidyltransferase"
FT /id="PRO_0000056781"
FT TRANSMEM 7..24
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 60..81
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 134..150
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 157..173
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 195 AA; 21846 MW; E6234FF3A5574D34 CRC64;
MNIPNLITVL RVLLIPIFIL LFYLPYNWSY MAASSVFAFA AATDWLDGYL ARRLEQSTPF
GAFLDPVADK LMVAVALVLL VQEHGNLWLT LPAAVIIGRE IVVSALREWM AELGRTRPGG
RCPTWANRKT AAQMLALVIL LANPPAFTFW VLLGYAFLLI AGGLTLWSML QYLRAAWPHL
KTDGRKEIKL FESRG
