ID   PGSA_ECOL6              Reviewed;         182 AA.
AC   P0ABF9; P06978;
DT   01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   10-JUN-2026, entry version 108.
DE   RecName: Full=CDP-diacylglycerol--glycerol-3-phosphate 3-phosphatidyltransferase {ECO:0000255|HAMAP-Rule:MF_01437};
DE            EC=2.7.8.5 {ECO:0000255|HAMAP-Rule:MF_01437};
DE   AltName: Full=Phosphatidylglycerophosphate synthase {ECO:0000255|HAMAP-Rule:MF_01437};
DE            Short=PGP synthase {ECO:0000255|HAMAP-Rule:MF_01437};
GN   Name=pgsA {ECO:0000255|HAMAP-Rule:MF_01437}; OrderedLocusNames=c2325;
OS   Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Enterobacterales; Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=199310;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CFT073 / ATCC 700928 / UPEC;
RX   PubMed=12471157; DOI=10.1073/pnas.252529799;
RA   Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA   Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA   Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA   Donnenberg M.S., Blattner F.R.;
RT   "Extensive mosaic structure revealed by the complete genome sequence of
RT   uropathogenic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
CC   -!- FUNCTION: Catalyzes the conversion of cytidine diphosphate
CC       diacylglycerol (CDP-DG) and glycerol 3-phosphate into
CC       phosphatidylglycerol. Essential for the synthesis of anionic
CC       phospholipids, thereby playing a role in balancing the ratio of
CC       zwitterionic and anionic phospholipids, which is thought to be
CC       important for normal membrane function. {ECO:0000255|HAMAP-
CC       Rule:MF_01437}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a CDP-1,2-diacyl-sn-glycerol + sn-glycerol 3-phosphate = a
CC         1,2-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:0000255|HAMAP-Rule:MF_01437};
CC   -!- PATHWAY: Phospholipid metabolism; phosphatidylglycerol biosynthesis;
CC       phosphatidylglycerol from CDP-diacylglycerol: step 1/2.
CC       {ECO:0000255|HAMAP-Rule:MF_01437}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC       Rule:MF_01437}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_01437}.
CC   -!- SIMILARITY: Belongs to the CDP-alcohol phosphatidyltransferase class-I
CC       family. {ECO:0000255|HAMAP-Rule:MF_01437}.
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DR   EMBL; AE014075; AAN80784.1; -; Genomic_DNA.
DR   RefSeq; WP_001160187.1; NC_004431.1.
DR   AlphaFoldDB; P0ABF9; -.
DR   SMR; P0ABF9; -.
DR   STRING; 199310.c2325; -.
DR   GeneID; 67172161; -.
DR   GeneID; 93776217; -.
DR   KEGG; ecc:c2325; -.
DR   eggNOG; COG0558; Bacteria.
DR   HOGENOM; CLU_051314_2_1_6; -.
DR   BioCyc; ECOL199310:C2325-MONOMER; -.
DR   UniPathway; UPA00084; UER00503.
DR   Proteomes; UP000001410; Chromosome.
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-UniRule.
DR   GO; GO:0006655; P:phosphatidylglycerol biosynthetic process; IEA:UniProtKB-UniRule.
DR   FunFam; 1.20.120.1760:FF:000001; CDP-diacylglycerol--glycerol-3-phosphate 3-phosphatidyltransferase; 1.
DR   Gene3D; 1.20.120.1760; -; 1.
DR   HAMAP; MF_01437; PgsA; 1.
DR   InterPro; IPR050324; CDP-alcohol_PTase-I.
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; IPR023762; PGP_synthase_bac.
DR   InterPro; IPR004570; Phosphatidylglycerol_P_synth.
DR   NCBIfam; TIGR00560; pgsA; 1.
DR   NCBIfam; NF008090; PRK10832.1; 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   Cell inner membrane; Cell membrane; Lipid biosynthesis; Lipid metabolism;
KW   Membrane; Phospholipid biosynthesis; Phospholipid metabolism;
KW   Reference proteome; Transferase; Transmembrane; Transmembrane helix.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..182
FT                   /note="CDP-diacylglycerol--glycerol-3-phosphate 3-
FT                   phosphatidyltransferase"
FT                   /id="PRO_0000056775"
FT   TOPO_DOM        2..13
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01437"
FT   TRANSMEM        14..38
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01437"
FT   TOPO_DOM        39..61
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01437"
FT   TRANSMEM        62..82
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01437"
FT   TOPO_DOM        83..87
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01437"
FT   TRANSMEM        88..108
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01437"
FT   TOPO_DOM        109..146
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01437"
FT   TRANSMEM        147..169
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01437"
FT   TOPO_DOM        170..182
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01437"
SQ   SEQUENCE   182 AA;  20701 MW;  F8F0502ABE6DC8D5 CRC64;
     MQFNIPTLLT LFRVILIPFF VLVFYLPVTW SPFAAALIFC VAAVTDWFDG FLARRWNQST
     RFGAFLDPVA DKVLVAIAMV LVTEHYHSWW VTLPAATMIA REIIISALRE WMAELGKRSS
     VAVSWIGKVK TTAQMVALAW LLWRPNIWVE YAGIALFFVA AVLTLWSMLQ YLSAARADLL
     DQ
//