PGSA_STAAC
ID PGSA_STAAC Reviewed; 192 AA.
AC Q5HGE8;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 25-MAY-2022, entry version 102.
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=SACOL1302;
OS Staphylococcus aureus (strain COL).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=93062;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=COL;
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}.
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DR EMBL; CP000046; AAW38133.1; -; Genomic_DNA.
DR RefSeq; WP_001025093.1; NC_002951.2.
DR AlphaFoldDB; Q5HGE8; -.
DR SMR; Q5HGE8; -.
DR EnsemblBacteria; AAW38133; AAW38133; SACOL1302.
DR KEGG; sac:SACOL1302; -.
DR HOGENOM; CLU_051314_2_3_9; -.
DR OMA; WSMVYYL; -.
DR UniPathway; UPA00084; UER00503.
DR Proteomes; UP000000530; 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_0000056784"
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