ID PGSA_ECOLI Reviewed; 182 AA. AC P0ABF8; P06978; DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 02-SEP-2026, entry version 136. DE RecName: Full=CDP-diacylglycerol--glycerol-3-phosphate 3-phosphatidyltransferase; DE EC=2.7.8.5 {ECO:0000269|PubMed:3003065, ECO:0000269|PubMed:8824831}; DE AltName: Full=Phosphatidylglycerophosphate synthase; DE Short=PGP synthase; GN Name=pgsA; OrderedLocusNames=b1912, JW1897; OS Escherichia coli (strain K12). OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; OC Enterobacterales; Enterobacteriaceae; Escherichia. OX NCBI_TaxID=83333; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=3003065; DOI=10.1016/s0021-9258(17)36095-7; RA Gopalakrishnan A.S., Chen Y.-C., Temkin M., Dowhan W.; RT "Structure and expression of the gene locus encoding the RT phosphatidylglycerophosphate synthase of Escherichia coli."; RL J. Biol. Chem. 261:1329-1338(1986). RN [2] RP SEQUENCE REVISION, AND MUTANTS PGSA3 AND PGSA10. RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; RX PubMed=8195097; DOI=10.1128/jb.176.11.3389-3392.1994; RA Usui M., Sembongi H., Matsuzaki H., Matsumoto K., Shibuya I.; RT "Primary structures of the wild-type and mutant alleles encoding the RT phosphatidylglycerophosphate synthase of Escherichia coli."; RL J. Bacteriol. 176:3389-3392(1994). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; RX PubMed=9097040; DOI=10.1093/dnares/3.6.379; RA Itoh T., Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., RA Kasai H., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T., RA Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S., Nakamura Y., RA Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y., RA Sivasundaram S., Tagami H., Takeda J., Takemoto K., Wada C., Yamamoto Y., RA Horiuchi T.; RT "A 460-kb DNA sequence of the Escherichia coli K-12 genome corresponding to RT the 40.1-50.0 min region on the linkage map."; RL DNA Res. 3:379-392(1996). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / MG1655 / ATCC 47076; RX PubMed=9278503; DOI=10.1126/science.277.5331.1453; RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., RA Shao Y.; RT "The complete genome sequence of Escherichia coli K-12."; RL Science 277:1453-1462(1997). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; RX PubMed=16738553; DOI=10.1038/msb4100049; RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.; RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 RT and W3110."; RL Mol. Syst. Biol. 2:E1-E5(2006). RN [6] RP REVIEW. RX PubMed=1323047; DOI=10.1016/0076-6879(92)09039-6; RA Dowhan W.; RT "Phosphatidylglycerophosphate synthase from Escherichia coli."; RL Methods Enzymol. 209:313-321(1992). RN [7] RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND MUTAGENESIS OF THR-60. RX PubMed=8824831; DOI=10.1271/bbb.60.111; RA Saha S.K., Nishijima S., Matsuzaki H., Shibuya I., Matsumoto K.; RT "A regulatory mechanism for the balanced synthesis of membrane phospholipid RT species in Escherichia coli."; RL Biosci. Biotechnol. Biochem. 60:111-116(1996). RN [8] RP TOPOLOGY [LARGE SCALE ANALYSIS], AND SUBCELLULAR LOCATION. RC STRAIN=K12 / MG1655 / ATCC 47076; RX PubMed=15919996; DOI=10.1126/science.1109730; RA Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.; RT "Global topology analysis of the Escherichia coli inner membrane RT proteome."; RL Science 308:1321-1323(2005). RN [9] RP STRUCTURE BY NMR OF 6-25 AND 149-176. RX PubMed=8917447; DOI=10.1111/j.1432-1033.1996.00489.x; RA Morein S., Trouard T.P., Hauksson J.B., Arvidson G., Lindblom G.; RT "Two-dimensional 1H-NMR of transmembrane peptides from Escherichia coli RT phosphatidylglycerophosphate synthase in micelles."; RL Eur. J. Biochem. 241:489-497(1996). CC -!- FUNCTION: Catalyzes the conversion of cytidine diphosphate CC diacylglycerol (CDP-DG) and glycerol 3-phosphate into CC phosphatidylglycerol (PubMed:3003065, PubMed:8824831). Essential for CC the synthesis of anionic phospholipids, thereby playing a role in CC balancing the ratio of zwitterionic and anionic phospholipids, which is CC thought to be important for normal membrane function (PubMed:3003065, CC PubMed:8824831). {ECO:0000269|PubMed:3003065, CC ECO:0000269|PubMed:8824831}. CC -!- CATALYTIC ACTIVITY: CC Reaction=a CDP-1,2-diacyl-sn-glycerol + sn-glycerol 3-phosphate = a CC 1,2-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:0000269|PubMed:3003065, ECO:0000269|PubMed:8824831}; CC -!- PATHWAY: Phospholipid metabolism; phosphatidylglycerol biosynthesis; CC phosphatidylglycerol from CDP-diacylglycerol: step 1/2. CC {ECO:0000269|PubMed:8824831}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane CC {ECO:0000269|PubMed:15919996}; Multi-pass membrane protein CC {ECO:0000255}. CC -!- PTM: The N-terminus is probably blocked. {ECO:0000269|PubMed:3003065}. CC -!- SIMILARITY: Belongs to the CDP-alcohol phosphatidyltransferase class-I CC family. {ECO:0000255|HAMAP-Rule:MF_01437, 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; M12299; AAA98754.1; -; Genomic_DNA. DR EMBL; U00096; AAC74979.1; -; Genomic_DNA. DR EMBL; AP009048; BAA15732.2; -; Genomic_DNA. DR PIR; E64954; XNECPG. DR RefSeq; NP_416422.1; NC_000913.3. DR RefSeq; WP_001160187.1; NZ_CP009789.1. DR AlphaFoldDB; P0ABF8; -. DR SMR; P0ABF8; -. DR BioGRID; 4261587; 268. DR FunCoup; P0ABF8; 720. DR IntAct; P0ABF8; 1. DR STRING; 511145.b1912; -. DR ChEMBL; CHEMBL3309009; -. DR jPOST; P0ABF8; -. DR PaxDb; 511145-b1912; -. DR EnsemblBacteria; AAC74979; AAC74979; b1912. DR GeneID; 67172161; -. DR GeneID; 93776217; -. DR GeneID; 945791; -. DR KEGG; ecj:JW1897; -. DR KEGG; eco:b1912; -. DR KEGG; ecoc:C3026_10850; -. DR PATRIC; fig|1411691.4.peg.338; -. DR EchoBASE; EB0700; -. DR eggNOG; COG0558; Bacteria. DR InParanoid; P0ABF8; -. DR OMA; WSMVYYL; -. DR OrthoDB; 9796672at2; -. DR PhylomeDB; P0ABF8; -. DR BioCyc; EcoCyc:PHOSPHAGLYPSYN-MONOMER; -. DR BioCyc; MetaCyc:PHOSPHAGLYPSYN-MONOMER; -. DR BRENDA; 2.7.8.5; 2026. DR SABIO-RK; P0ABF8; -. DR UniPathway; UPA00084; UER00503. DR PRO; PR:P0ABF8; -. DR Proteomes; UP000000625; Chromosome. DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc. DR GO; GO:0008444; F:CDP-diacylglycerol-glycerol-3-phosphate 3-phosphatidyltransferase activity; IDA:EcoliWiki. DR GO; GO:0006655; P:phosphatidylglycerol biosynthetic process; IEA:UniProtKB-UniRule. DR FunFam; 1.20.120.1760:FF:000001; CDP-diacylglycerol--glycerol-3-phosphate 3-phosphatidyltransferase; 1. DR Gene3D; 1.20.120.1760; -; 1. DR HAMAP; MF_01437; PgsA; 1. DR InterPro; IPR050324; CDP-alcohol_PTase-I. DR InterPro; IPR000462; CDP-OH_P_trans. DR InterPro; IPR043130; CDP-OH_PTrfase_TM_dom. DR InterPro; IPR048254; CDP_ALCOHOL_P_TRANSF_CS. DR InterPro; IPR023762; PGP_synthase_bac. DR InterPro; IPR004570; Phosphatidylglycerol_P_synth. DR NCBIfam; TIGR00560; pgsA; 1. DR NCBIfam; NF008090; PRK10832.1; 1. DR PANTHER; PTHR14269:SF62; CDP-DIACYLGLYCEROL--GLYCEROL-3-PHOSPHATE 3-PHOSPHATIDYLTRANSFERASE 1, CHLOROPLASTIC; 1. DR PANTHER; PTHR14269; CDP-DIACYLGLYCEROL--GLYCEROL-3-PHOSPHATE 3-PHOSPHATIDYLTRANSFERASE-RELATED; 1. DR Pfam; PF01066; CDP-OH_P_transf; 1. DR PIRSF; PIRSF000847; Phos_ph_gly_syn; 1. DR PROSITE; PS00379; CDP_ALCOHOL_P_TRANSF; 1. PE 1: Evidence at protein level; KW Cell inner membrane; Cell membrane; Lipid biosynthesis; Lipid metabolism; KW Membrane; Phospholipid biosynthesis; Phospholipid metabolism; KW Reference proteome; Transferase; Transmembrane; Transmembrane helix. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000305|PubMed:3003065" FT CHAIN 2..182 FT /note="CDP-diacylglycerol--glycerol-3-phosphate 3- FT phosphatidyltransferase" FT /id="PRO_0000056773" FT TOPO_DOM 2..13 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 14..38 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 39..61 FT /note="Periplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 62..82 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 83..87 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 88..108 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 109..146 FT /note="Periplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 147..169 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 170..182 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT MUTAGEN 60 FT /note="T->P: In pgsA3; lowers activity, increases FT phosphatidic acid levels and reduces both the acidic FT phospholipids in the membrane and the total levels of FT phospholipids. Reduces the membrane-association of FT phosphatidylserine synthase PssA." FT /evidence="ECO:0000269|PubMed:8195097, FT ECO:0000269|PubMed:8824831" FT MUTAGEN 92 FT /note="T->I: In pgsA10; lower activity." FT /evidence="ECO:0000269|PubMed:8195097" SQ SEQUENCE 182 AA; 20701 MW; F8F0502ABE6DC8D5 CRC64; MQFNIPTLLT LFRVILIPFF VLVFYLPVTW SPFAAALIFC VAAVTDWFDG FLARRWNQST RFGAFLDPVA DKVLVAIAMV LVTEHYHSWW VTLPAATMIA REIIISALRE WMAELGKRSS VAVSWIGKVK TTAQMVALAW LLWRPNIWVE YAGIALFFVA AVLTLWSMLQ YLSAARADLL DQ //