ID   PGSA_STAEQ              Reviewed;         193 AA.
AC   Q5HPQ8;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   25-MAY-2022, entry version 96.
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=SERP0850;
OS   Staphylococcus epidermidis (strain ATCC 35984 / RP62A).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=176279;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35984 / RP62A;
RX   PubMed=15774886; DOI=10.1128/jb.187.7.2426-2438.2005;
RA   Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T., Ravel J.,
RA   Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J., Dodson R.J.,
RA   Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., Haft D.H.,
RA   Vamathevan J.J., Khouri H., Utterback T.R., Lee C., Dimitrov G., Jiang L.,
RA   Qin H., Weidman J., Tran K., Kang K.H., Hance I.R., Nelson K.E.,
RA   Fraser C.M.;
RT   "Insights on evolution of virulence and resistance from the complete genome
RT   analysis of an early methicillin-resistant Staphylococcus aureus strain and
RT   a biofilm-producing methicillin-resistant Staphylococcus epidermidis
RT   strain.";
RL   J. Bacteriol. 187:2426-2438(2005).
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; CP000029; AAW54227.1; -; Genomic_DNA.
DR   RefSeq; WP_002439546.1; NC_002976.3.
DR   AlphaFoldDB; Q5HPQ8; -.
DR   SMR; Q5HPQ8; -.
DR   STRING; 176279.SERP0850; -.
DR   EnsemblBacteria; AAW54227; AAW54227; SERP0850.
DR   KEGG; ser:SERP0850; -.
DR   eggNOG; COG0558; Bacteria.
DR   HOGENOM; CLU_051314_2_3_9; -.
DR   OMA; WSMVYYL; -.
DR   OrthoDB; 1702107at2; -.
DR   UniPathway; UPA00084; UER00503.
DR   Proteomes; UP000000531; 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; Reference proteome;
KW   Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..193
FT                   /note="CDP-diacylglycerol--glycerol-3-phosphate 3-
FT                   phosphatidyltransferase"
FT                   /id="PRO_0000056791"
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   193 AA;  21497 MW;  B59344586D41B319 CRC64;
     MNIPNQITVF RVILIPFFIL FALVDFGFGQ ISILGGNHIR IEILISAIIF VVASLSDFAD
     GYLARKWQLV TNMGKFLDPL ADKLLVASAL IVMVQLGFTN SVVAIIIIAR EFAVTGLRLL
     QIEQGFVSAA GQLGKIKTAV TMVAIIWILL GDPFVHYLRF PIGVWLLYIG VFFTILSGIE
     YFYKGRDVFK HSK