ID   PGSA_BLOFL              Reviewed;         190 AA.
AC   Q7VR12;
DT   30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   03-AUG-2022, entry version 100.
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=Bfl415;
OS   Blochmannia floridanus.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; ant endosymbionts; Candidatus Blochmannia.
OX   NCBI_TaxID=203907;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=12886019; DOI=10.1073/pnas.1533499100;
RA   Gil R., Silva F.J., Zientz E., Delmotte F., Gonzalez-Candelas F.,
RA   Latorre A., Rausell C., Kamerbeek J., Gadau J., Hoelldobler B.,
RA   van Ham R.C.H.J., Gross R., Moya A.;
RT   "The genome sequence of Blochmannia floridanus: comparative analysis of
RT   reduced genomes.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:9388-9393(2003).
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; BX248583; CAD83479.1; -; Genomic_DNA.
DR   RefSeq; WP_011126686.1; NC_005061.1.
DR   AlphaFoldDB; Q7VR12; -.
DR   SMR; Q7VR12; -.
DR   STRING; 203907.Bfl415; -.
DR   EnsemblBacteria; CAD83479; CAD83479; Bfl415.
DR   KEGG; bfl:Bfl415; -.
DR   eggNOG; COG0558; Bacteria.
DR   HOGENOM; CLU_051314_2_1_6; -.
DR   OMA; RIVPPWI; -.
DR   OrthoDB; 1702107at2; -.
DR   UniPathway; UPA00084; UER00503.
DR   Proteomes; UP000002192; 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;
KW   Reference proteome; Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..190
FT                   /note="CDP-diacylglycerol--glycerol-3-phosphate 3-
FT                   phosphatidyltransferase"
FT                   /id="PRO_0000239121"
FT   TOPO_DOM        6..17
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01437"
FT   TRANSMEM        18..42
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01437"
FT   TOPO_DOM        43..65
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01437"
FT   TRANSMEM        66..86
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01437"
FT   TOPO_DOM        87..91
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01437"
FT   TRANSMEM        92..112
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01437"
FT   TOPO_DOM        113..150
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01437"
FT   TRANSMEM        151..173
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01437"
FT   TOPO_DOM        174..186
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01437"
SQ   SEQUENCE   190 AA;  22342 MW;  1FA9F4640E093EBE CRC64;
     MFKYYGVFNI PMYLTLFRII MVPCFVAVFY WPIYWSPMLC TLIFFIAAIT DWFDGFLARR
     WNQTSRIGGF LDPIADKIMI ITALILISEH FHVWWMTLPI SSIIIREILI SSLRECIARV
     DNKNNISVIW LSKVKTFAQM LALIALLCRL NEWTVIMGVI SLYTAMLLTL WSMCYYVYSV
     SSILLQYKLK