PGSA_YERPN
ID PGSA_YERPN Reviewed; 182 AA.
AC Q1CHE5; C4GUE8;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2006, sequence version 1.
DT 25-MAY-2022, entry version 83.
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=YPN_2257;
GN ORFNames=YP516_2536;
OS Yersinia pestis bv. Antiqua (strain Nepal516).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=377628;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Nepal516;
RX PubMed=16740952; DOI=10.1128/jb.00124-06;
RA Chain P.S.G., Hu P., Malfatti S.A., Radnedge L., Larimer F., Vergez L.M.,
RA Worsham P., Chu M.C., Andersen G.L.;
RT "Complete genome sequence of Yersinia pestis strains Antiqua and Nepal516:
RT evidence of gene reduction in an emerging pathogen.";
RL J. Bacteriol. 188:4453-4463(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Nepal516;
RA Plunkett G. III, Anderson B.D., Baumler D.J., Burland V., Cabot E.L.,
RA Glasner J.D., Mau B., Neeno-Eckwall E., Perna N.T., Munk A.C., Tapia R.,
RA Green L.D., Rogers Y.C., Detter J.C., Bruce D.C., Brettin T.S.;
RT "Yersinia pestis Nepal516A whole genome shotgun sequencing project.";
RL Submitted (APR-2009) to the EMBL/GenBank/DDBJ databases.
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; CP000305; ABG18585.1; -; Genomic_DNA.
DR EMBL; ACNQ01000013; EEO76335.1; -; Genomic_DNA.
DR RefSeq; WP_002220475.1; NZ_ACNQ01000013.1.
DR AlphaFoldDB; Q1CHE5; -.
DR SMR; Q1CHE5; -.
DR EnsemblBacteria; ABG18585; ABG18585; YPN_2257.
DR GeneID; 66841827; -.
DR KEGG; ypn:YPN_2257; -.
DR HOGENOM; CLU_051314_2_1_6; -.
DR OMA; WSMVYYL; -.
DR UniPathway; UPA00084; UER00503.
DR Proteomes; UP000008936; 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; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..182
FT /note="CDP-diacylglycerol--glycerol-3-phosphate 3-
FT phosphatidyltransferase"
FT /id="PRO_0000301867"
FT TOPO_DOM 1..12
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01437"
FT TRANSMEM 13..37
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01437"
FT TOPO_DOM 38..60
FT /note="Periplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01437"
FT TRANSMEM 61..81
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01437"
FT TOPO_DOM 82..86
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01437"
FT TRANSMEM 87..107
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01437"
FT TOPO_DOM 108..145
FT /note="Periplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01437"
FT TRANSMEM 146..168
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01437"
FT TOPO_DOM 169..181
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01437"
SQ SEQUENCE 182 AA; 20806 MW; 5227A0724C651B9D CRC64;
MQLNIPTWLT LFRVVLIPFF VLAFYLPFVW APMVCAIIFV FAAATDWFDG FLARRWKQTT
RFGAFLDPVA DKVMVAVALV LVAEHYHSWW ITLPAATMIA REIIISSLRE WMAEIGKRSS
VAVSWVGKVK TMAQMGSLVG LLWRPDHNVE LASFVLLYIA AVLTFWSMFQ YLNAAWSDLL
EP
