PGSA_STAAN
ID PGSA_STAAN Reviewed; 192 AA.
AC P63756; Q99UI9;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 103.
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=SA1126;
OS Staphylococcus aureus (strain N315).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=158879;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=N315;
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).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=N315;
RA Vaezzadeh A.R., Deshusses J., Lescuyer P., Hochstrasser D.F.;
RT "Shotgun proteomic analysis of total and membrane protein extracts of S.
RT aureus strain N315.";
RL Submitted (OCT-2007) to UniProtKB.
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; BA000018; BAB42378.1; -; Genomic_DNA.
DR PIR; F89902; F89902.
DR RefSeq; WP_001025093.1; NC_002745.2.
DR PDB; 7DRJ; X-ray; 2.50 A; A/B=1-192.
DR PDB; 7DRK; X-ray; 3.00 A; A/B=1-192.
DR PDBsum; 7DRJ; -.
DR PDBsum; 7DRK; -.
DR AlphaFoldDB; P63756; -.
DR SMR; P63756; -.
DR EnsemblBacteria; BAB42378; BAB42378; BAB42378.
DR KEGG; sau:SA1126; -.
DR HOGENOM; CLU_051314_2_3_9; -.
DR OMA; WSMVYYL; -.
DR UniPathway; UPA00084; UER00503.
DR Proteomes; UP000000751; 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 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Lipid biosynthesis; Lipid metabolism;
KW Membrane; 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_0000056786"
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"
FT HELIX 3..23
FT /evidence="ECO:0007829|PDB:7DRJ"
FT STRAND 30..32
FT /evidence="ECO:0007829|PDB:7DRJ"
FT STRAND 33..35
FT /evidence="ECO:0007829|PDB:7DRK"
FT STRAND 38..40
FT /evidence="ECO:0007829|PDB:7DRJ"
FT HELIX 41..55
FT /evidence="ECO:0007829|PDB:7DRJ"
FT HELIX 59..66
FT /evidence="ECO:0007829|PDB:7DRJ"
FT HELIX 72..95
FT /evidence="ECO:0007829|PDB:7DRJ"
FT HELIX 101..123
FT /evidence="ECO:0007829|PDB:7DRJ"
FT HELIX 132..149
FT /evidence="ECO:0007829|PDB:7DRJ"
FT HELIX 155..158
FT /evidence="ECO:0007829|PDB:7DRJ"
FT HELIX 162..184
FT /evidence="ECO:0007829|PDB:7DRJ"
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
