PGSA_ECOLI
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 03-AUG-2022, entry version 117.
DE RecName: Full=CDP-diacylglycerol--glycerol-3-phosphate 3-phosphatidyltransferase;
DE EC=2.7.8.5 {ECO:0000269|PubMed:3003065};
DE AltName: Full=Phosphatidylglycerophosphate synthase;
DE Short=PGP synthase;
GN Name=pgsA; OrderedLocusNames=b1912, JW1897;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], CATALYTIC ACTIVITY, AND FUNCTION.
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 TOPOLOGY [LARGE SCALE ANALYSIS].
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 [8]
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: This protein catalyzes the committed step to the synthesis of
CC the acidic phospholipids. {ECO:0000269|PubMed:3003065}.
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:0000269|PubMed:3003065};
CC -!- PATHWAY: Phospholipid metabolism; phosphatidylglycerol biosynthesis;
CC phosphatidylglycerol from CDP-diacylglycerol: step 1/2.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein.
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: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; BAA15732.1; -; Genomic_DNA.
DR PIR; E64954; XNECPG.
DR RefSeq; NP_416422.1; NC_000913.3.
DR RefSeq; WP_001160187.1; NZ_STEB01000026.1.
DR AlphaFoldDB; P0ABF8; -.
DR SMR; P0ABF8; -.
DR BioGRID; 4261587; 267.
DR IntAct; P0ABF8; 1.
DR STRING; 511145.b1912; -.
DR ChEMBL; CHEMBL3309009; -.
DR jPOST; P0ABF8; -.
DR PaxDb; P0ABF8; -.
DR PRIDE; P0ABF8; -.
DR EnsemblBacteria; AAC74979; AAC74979; b1912.
DR EnsemblBacteria; BAA15732; BAA15732; BAA15732.
DR GeneID; 67415812; -.
DR GeneID; 945791; -.
DR KEGG; ecj:JW1897; -.
DR KEGG; eco:b1912; -.
DR PATRIC; fig|1411691.4.peg.338; -.
DR EchoBASE; EB0700; -.
DR eggNOG; COG0558; Bacteria.
DR InParanoid; P0ABF8; -.
DR OMA; WSMVYYL; -.
DR PhylomeDB; P0ABF8; -.
DR BioCyc; EcoCyc:PHOSPHAGLYPSYN-MON; -.
DR BioCyc; MetaCyc:PHOSPHAGLYPSYN-MON; -.
DR BRENDA; 2.7.8.5; 2026.
DR SABIO-RK; P0ABF8; -.
DR UniPathway; UPA00084; UER00503.
DR PRO; PR:P0ABF8; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IDA:EcoliWiki.
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:0046474; P:glycerophospholipid biosynthetic process; IBA:GO_Central.
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 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; lower activity."
FT MUTAGEN 92
FT /note="T->I: In pgsA10; lower activity."
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
