PGSA_BLOPB
ID PGSA_BLOPB Reviewed; 183 AA.
AC Q492P7;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 94.
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=BPEN_427;
OS Blochmannia pennsylvanicus (strain BPEN).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; ant endosymbionts; Candidatus Blochmannia.
OX NCBI_TaxID=291272;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BPEN;
RX PubMed=16077009; DOI=10.1101/gr.3771305;
RA Degnan P.H., Lazarus A.B., Wernegreen J.J.;
RT "Genome sequence of Blochmannia pennsylvanicus indicates parallel
RT evolutionary trends among bacterial mutualists of insects.";
RL Genome Res. 15:1023-1033(2005).
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; CP000016; AAZ41048.1; -; Genomic_DNA.
DR RefSeq; WP_011282958.1; NC_007292.1.
DR AlphaFoldDB; Q492P7; -.
DR SMR; Q492P7; -.
DR STRING; 291272.BPEN_427; -.
DR EnsemblBacteria; AAZ41048; AAZ41048; BPEN_427.
DR KEGG; bpn:BPEN_427; -.
DR eggNOG; COG0558; Bacteria.
DR HOGENOM; CLU_051314_2_1_6; -.
DR OMA; WSMVYYL; -.
DR BioCyc; CBLO291272:BPEN_RS02100-MON; -.
DR UniPathway; UPA00084; UER00503.
DR Proteomes; UP000007794; 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..183
FT /note="CDP-diacylglycerol--glycerol-3-phosphate 3-
FT phosphatidyltransferase"
FT /id="PRO_0000239122"
FT TOPO_DOM 1..13
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01437"
FT TRANSMEM 14..38
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01437"
FT TOPO_DOM 39..61
FT /note="Periplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01437"
FT TRANSMEM 62..82
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01437"
FT TOPO_DOM 83..87
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01437"
FT TRANSMEM 88..108
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01437"
FT TOPO_DOM 109..146
FT /note="Periplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01437"
FT TRANSMEM 147..169
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01437"
FT TOPO_DOM 170..182
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01437"
SQ SEQUENCE 183 AA; 21239 MW; 85CEF5AB4DC89A8D CRC64;
MDIINIPTYL TLLRVVMVPF FTVMFYLPVR WAPMICTIMF FVAAVTDWFD GFLARRWKQT
TSFGKFLDPV ADKVMIVAAL VLIAEHFHTW WVTLPASIII IREVIILALR EWVAAIGSRN
GIGVLWISKI KTFVQMLALT ALLWSSDEWI VIIGIVALYV SVLLTFWSMC LYLYIVRYDL
FNY
