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Database: UniProt
Entry: I7B3M3_PSEPT
LinkDB: I7B3M3_PSEPT
Original site: I7B3M3_PSEPT 
ID   I7B3M3_PSEPT            Unreviewed;       156 AA.
AC   I7B3M3;
DT   03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   03-OCT-2012, sequence version 1.
DT   27-MAR-2024, entry version 45.
DE   RecName: Full=CDP-diacylglycerol--glycerol-3-phosphate 3-phosphatidyltransferase {ECO:0000256|ARBA:ARBA00014944};
DE            EC=2.7.8.5 {ECO:0000256|ARBA:ARBA00013170};
GN   Name=pgsA {ECO:0000313|EMBL:AFO45898.1};
GN   OrderedLocusNames=T1E_0039 {ECO:0000313|EMBL:AFO45898.1};
OS   Pseudomonas putida (strain DOT-T1E).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=1196325 {ECO:0000313|EMBL:AFO45898.1, ECO:0000313|Proteomes:UP000006503};
RN   [1] {ECO:0000313|Proteomes:UP000006503}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DOT-T1E {ECO:0000313|Proteomes:UP000006503};
RX   PubMed=23815283; DOI=10.1111/1751-7915.12061;
RA   Udaondo Z., Molina L., Daniels C., Gomez M.J., Molina-Henares M.A.,
RA   Matilla M.A., Roca A., Fernandez M., Duque E., Segura A., Ramos J.L.;
RT   "Metabolic potential of the organic-solvent tolerant Pseudomonas putida
RT   DOT-T1E deduced from its annotated genome.";
RL   Microb. Biotechnol. 6:598-611(2013).
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 + 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; CP003734; AFO45898.1; -; Genomic_DNA.
DR   AlphaFoldDB; I7B3M3; -.
DR   KEGG; ppx:T1E_0039; -.
DR   PATRIC; fig|1196325.3.peg.39; -.
DR   HOGENOM; CLU_051314_2_1_6; -.
DR   Proteomes; UP000006503; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0008444; F:CDP-diacylglycerol-glycerol-3-phosphate 3-phosphatidyltransferase activity; IEA:InterPro.
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; IPR048254; CDP_ALCOHOL_P_TRANSF_CS.
DR   InterPro; IPR004570; Phosphatidylglycerol_P_synth.
DR   NCBIfam; TIGR00560; pgsA; 1.
DR   PANTHER; PTHR14269:SF62; CDP-DIACYLGLYCEROL--GLYCEROL-3-PHOSPHATE 3-PHOSPHATIDYLTRANSFERASE 1, CHLOROPLASTIC; 1.
DR   PANTHER; PTHR14269; CDP-DIACYLGLYCEROL--GLYCEROL-3-PHOSPHATE 3-PHOSPHATIDYLTRANSFERASE-RELATED; 1.
DR   Pfam; PF01066; CDP-OH_P_transf; 1.
DR   PIRSF; PIRSF000847; Phos_ph_gly_syn; 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   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        42..67
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        103..121
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        127..146
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
SQ   SEQUENCE   156 AA;  16873 MW;  99DA8F55A9B81962 CRC64;
     MAASSVFAVA AATDWLDGYL ARRLQQSTPF GAFLDPVADK LMVAVALVLL VQTHANFWLT
     LPAAVIIGRE IVVSALREWM AELGARAHVA VSNLGKWKTA AQMLALVILL GNPPAVTFWV
     ILGYGLLLVA AGLTLWSMVH YLLAAWPHLR EGSEKK
//
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