PGSA_SALPA
ID PGSA_SALPA Reviewed; 182 AA.
AC Q5PI18;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 25-MAY-2022, entry version 85.
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=SPA0924;
OS Salmonella paratyphi A (strain ATCC 9150 / SARB42).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=295319;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 9150 / SARB42;
RX PubMed=15531882; DOI=10.1038/ng1470;
RA McClelland M., Sanderson K.E., Clifton S.W., Latreille P., Porwollik S.,
RA Sabo A., Meyer R., Bieri T., Ozersky P., McLellan M., Harkins C.R.,
RA Wang C., Nguyen C., Berghoff A., Elliott G., Kohlberg S., Strong C., Du F.,
RA Carter J., Kremizki C., Layman D., Leonard S., Sun H., Fulton L., Nash W.,
RA Miner T., Minx P., Delehaunty K., Fronick C., Magrini V., Nhan M.,
RA Warren W., Florea L., Spieth J., Wilson R.K.;
RT "Comparison of genome degradation in Paratyphi A and Typhi, human-
RT restricted serovars of Salmonella enterica that cause typhoid.";
RL Nat. Genet. 36:1268-1274(2004).
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; CP000026; AAV76903.1; -; Genomic_DNA.
DR RefSeq; WP_001160192.1; NC_006511.1.
DR AlphaFoldDB; Q5PI18; -.
DR SMR; Q5PI18; -.
DR DNASU; 3178041; -.
DR EnsemblBacteria; AAV76903; AAV76903; SPA0924.
DR KEGG; spt:SPA0924; -.
DR HOGENOM; CLU_051314_2_1_6; -.
DR OMA; WSMVYYL; -.
DR UniPathway; UPA00084; UER00503.
DR Proteomes; UP000008185; 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 INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..182
FT /note="CDP-diacylglycerol--glycerol-3-phosphate 3-
FT phosphatidyltransferase"
FT /id="PRO_0000239126"
FT TOPO_DOM 2..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; 20731 MW; B56963332314AA79 CRC64;
MQFNIPTLLT LFRVILIPFF VVVFYLPFAW APMVSALIFC IAAITDWFDG FLARRWNQST
RFGAFLDPVA DKVLVAIAMV LVTEHYHSWW VTLPAATMIA REIIISALRE WMAELGKRSS
VAVSWIGKVK TTAQMVALAW LLWRPNIWVE YAGIALFFVA AVLTLWSMLQ YLSAARGDLL
DQ
