ID   PGSA_STAAM              Reviewed;         192 AA.
AC   P63755; Q99UI9;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 104.
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; OrderedLocusNames=SAV1283;
OS   Staphylococcus aureus (strain Mu50 / ATCC 700699).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=158878;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Mu50 / ATCC 700699;
RX   PubMed=11418146; DOI=10.1016/s0140-6736(00)04403-2;
RA   Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I., Cui L.,
RA   Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M.,
RA   Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y.,
RA   Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K., Hirakawa H.,
RA   Kuhara S., Goto S., Yabuzaki J., Kanehisa M., Yamashita A., Oshima K.,
RA   Furuya K., Yoshino C., Shiba T., Hattori M., Ogasawara N., Hayashi H.,
RA   Hiramatsu K.;
RT   "Whole genome sequencing of meticillin-resistant Staphylococcus aureus.";
RL   Lancet 357:1225-1240(2001).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; BA000017; BAB57445.1; -; Genomic_DNA.
DR   RefSeq; WP_001025093.1; NC_002758.2.
DR   AlphaFoldDB; P63755; -.
DR   SMR; P63755; -.
DR   PaxDb; P63755; -.
DR   EnsemblBacteria; BAB57445; BAB57445; SAV1283.
DR   KEGG; sav:SAV1283; -.
DR   HOGENOM; CLU_051314_2_3_9; -.
DR   OMA; WSMVYYL; -.
DR   PhylomeDB; P63755; -.
DR   BioCyc; SAUR158878:SAV_RS06910-MON; -.
DR   UniPathway; UPA00084; UER00503.
DR   Proteomes; UP000002481; 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-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..192
FT                   /note="CDP-diacylglycerol--glycerol-3-phosphate 3-
FT                   phosphatidyltransferase"
FT                   /id="PRO_0000056785"
FT   TRANSMEM        7..29
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        44..63
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        84..106
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        129..151
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        157..179
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   192 AA;  21014 MW;  9DE1A740E101C674 CRC64;
     MNIPNQITVF RVVLIPVFIL FALVDFGFGN VSFLGGYEIR IELLISGFIF ILASLSDFVD
     GYLARKWNLV TNMGKFLDPL ADKLLVASAL IVLVQLGLTN SVVAIIIIAR EFAVTGLRLL
     QIEQGFVSAA GQLGKIKTAV TMVAITWLLL GDPLATLIGL SLGQILLYIG VIFTILSGIE
     YFYKGRDVFK QK