ID   PGSA_ECOK1              Reviewed;         182 AA.
AC   A1AC64;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   25-MAY-2022, entry version 83.
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=Ecok1_17600;
GN   ORFNames=APECO1_954;
OS   Escherichia coli O1:K1 / APEC.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=405955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=17293413; DOI=10.1128/jb.01726-06;
RA   Johnson T.J., Kariyawasam S., Wannemuehler Y., Mangiamele P., Johnson S.J.,
RA   Doetkott C., Skyberg J.A., Lynne A.M., Johnson J.R., Nolan L.K.;
RT   "The genome sequence of avian pathogenic Escherichia coli strain O1:K1:H7
RT   shares strong similarities with human extraintestinal pathogenic E. coli
RT   genomes.";
RL   J. Bacteriol. 189:3228-3236(2007).
CC   -!- FUNCTION: This protein catalyzes the committed step to the synthesis of
CC       the acidic phospholipids. {ECO:0000255|HAMAP-Rule:MF_01437}.
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: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; CP000468; ABJ01254.1; -; Genomic_DNA.
DR   RefSeq; WP_001160187.1; NC_008563.1.
DR   AlphaFoldDB; A1AC64; -.
DR   SMR; A1AC64; -.
DR   EnsemblBacteria; ABJ01254; ABJ01254; APECO1_954.
DR   GeneID; 67415812; -.
DR   KEGG; ecv:APECO1_954; -.
DR   HOGENOM; CLU_051314_2_1_6; -.
DR   OMA; WSMVYYL; -.
DR   UniPathway; UPA00084; UER00503.
DR   Proteomes; UP000008216; Chromosome.
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-UniRule.
DR   GO; GO:0006655; P:phosphatidylglycerol biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 1.20.120.1760; -; 1.
DR   HAMAP; MF_01437; PgsA; 1.
DR   InterPro; IPR000462; CDP-OH_P_trans.
DR   InterPro; IPR043130; CDP-OH_PTrfase_TM_dom.
DR   InterPro; IPR023762; PGP_synthase_bac.
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 inner membrane; Cell membrane; Lipid biosynthesis; Lipid metabolism;
KW   Membrane; Phospholipid biosynthesis; Phospholipid metabolism; Transferase;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..182
FT                   /note="CDP-diacylglycerol--glycerol-3-phosphate 3-
FT                   phosphatidyltransferase"
FT                   /id="PRO_0000301862"
FT   TOPO_DOM        1..12
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01437"
FT   TRANSMEM        13..37
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01437"
FT   TOPO_DOM        38..60
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01437"
FT   TRANSMEM        61..81
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01437"
FT   TOPO_DOM        82..86
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01437"
FT   TRANSMEM        87..107
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01437"
FT   TOPO_DOM        108..145
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01437"
FT   TRANSMEM        146..168
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01437"
FT   TOPO_DOM        169..181
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