PGPA_ECOLI
ID PGPA_ECOLI Reviewed; 172 AA.
AC P18200; P77321; Q2MC08;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Phosphatidylglycerophosphatase A;
DE EC=3.1.3.27;
DE AltName: Full=Phosphatidylglycerolphosphate phosphatase A;
DE Short=PGP phosphatase A;
GN Name=pgpA; Synonyms=yajN; OrderedLocusNames=b0418, JW0408;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP DISRUPTION PHENOTYPE.
RC STRAIN=K12;
RX PubMed=2846510; DOI=10.1128/jb.170.11.5110-5116.1988;
RA Icho T.;
RT "Membrane-bound phosphatases in Escherichia coli: sequence of the pgpA
RT gene.";
RL J. Bacteriol. 170:5110-5116(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RA Iida A., Hayashi M., Fujio T., Teshiba S.;
RL Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RA Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M.,
RA Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D.,
RA Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.;
RT "Sequence of minutes 4-25 of Escherichia coli.";
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
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 FUNCTION, CATALYTIC ACTIVITY, AND DISRUPTION PHENOTYPE.
RC STRAIN=K12;
RX PubMed=6296050; DOI=10.1128/jb.153.2.722-730.1983;
RA Icho T., Raetz C.R.;
RT "Multiple genes for membrane-bound phosphatases in Escherichia coli and
RT their action on phospholipid precursors.";
RL J. Bacteriol. 153:722-730(1983).
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 FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=20485265; DOI=10.1038/emboj.2010.98;
RA Osman C., Haag M., Wieland F.T., Brugger B., Langer T.;
RT "A mitochondrial phosphatase required for cardiolipin biosynthesis: the PGP
RT phosphatase Gep4.";
RL EMBO J. 29:1976-1987(2010).
RN [9]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBCELLULAR LOCATION, AND
RP DISRUPTION PHENOTYPE.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=21148555; DOI=10.1074/jbc.m110.199265;
RA Lu Y.H., Guan Z., Zhao J., Raetz C.R.;
RT "Three phosphatidylglycerol-phosphate phosphatases in the inner membrane of
RT Escherichia coli.";
RL J. Biol. Chem. 286:5506-5518(2011).
CC -!- FUNCTION: Lipid phosphatase which dephosphorylates
CC phosphatidylglycerophosphate (PGP) to phosphatidylglycerol (PG).
CC {ECO:0000269|PubMed:20485265, ECO:0000269|PubMed:21148555,
CC ECO:0000269|PubMed:2846510, ECO:0000269|PubMed:6296050}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycero-3'-phosphate) +
CC H2O = 1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycerol) + phosphate;
CC Xref=Rhea:RHEA:33751, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:60110, ChEBI:CHEBI:64716; EC=3.1.3.27;
CC Evidence={ECO:0000269|PubMed:20485265, ECO:0000269|PubMed:21148555,
CC ECO:0000269|PubMed:2846510, ECO:0000269|PubMed:6296050};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:21148555};
CC -!- PATHWAY: Phospholipid metabolism; phosphatidylglycerol biosynthesis;
CC phosphatidylglycerol from CDP-diacylglycerol: step 2/2.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000269|PubMed:21148555}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:21148555}.
CC -!- DISRUPTION PHENOTYPE: Displays 7-10 fold higher levels of
CC phosphatidylglycerophosphate (PGP) than wild-type. Simultaneous
CC deletion of pgpA and pgpB leads to 40 times higher PGP levels compared
CC to wild-type, while simultaneous deletion of pgpA and pgpC leads to
CC almost 100 times higher PGP levels. Lethal when combined with the
CC deletion of both pgpB and pgpC. {ECO:0000269|PubMed:21148555,
CC ECO:0000269|PubMed:2846510, ECO:0000269|PubMed:6296050}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA24325.1; Type=Frameshift; Note=In addition, due to translation of the incorrect DNA strand, an unrelated ORF was predicted.; Evidence={ECO:0000305};
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DR EMBL; M23546; AAA24325.1; ALT_SEQ; Genomic_DNA.
DR EMBL; D17333; BAA21779.1; -; Genomic_DNA.
DR EMBL; U82664; AAB40174.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73521.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76198.1; -; Genomic_DNA.
DR PIR; A30192; PAECGA.
DR PIR; B64771; B64771.
DR RefSeq; NP_414952.1; NC_000913.3.
DR RefSeq; WP_000154044.1; NZ_STEB01000007.1.
DR AlphaFoldDB; P18200; -.
DR BioGRID; 4259341; 300.
DR STRING; 511145.b0418; -.
DR SwissLipids; SLP:000000222; -.
DR PaxDb; P18200; -.
DR PRIDE; P18200; -.
DR EnsemblBacteria; AAC73521; AAC73521; b0418.
DR EnsemblBacteria; BAE76198; BAE76198; BAE76198.
DR GeneID; 66671283; -.
DR GeneID; 947542; -.
DR KEGG; ecj:JW0408; -.
DR KEGG; eco:b0418; -.
DR PATRIC; fig|1411691.4.peg.1859; -.
DR EchoBASE; EB0698; -.
DR eggNOG; COG1267; Bacteria.
DR HOGENOM; CLU_103734_0_1_6; -.
DR InParanoid; P18200; -.
DR OMA; VWDEIAG; -.
DR PhylomeDB; P18200; -.
DR BioCyc; EcoCyc:PGPPHOSPHAA-MON; -.
DR BioCyc; MetaCyc:PGPPHOSPHAA-MON; -.
DR UniPathway; UPA00084; UER00504.
DR PRO; PR:P18200; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; TAS:EcoCyc.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0042577; F:lipid phosphatase activity; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008962; F:phosphatidylglycerophosphatase activity; IDA:UniProtKB.
DR GO; GO:0046474; P:glycerophospholipid biosynthetic process; IMP:EcoCyc.
DR GO; GO:0006655; P:phosphatidylglycerol biosynthetic process; IDA:UniProtKB.
DR GO; GO:0009395; P:phospholipid catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0046839; P:phospholipid dephosphorylation; IDA:UniProtKB.
DR GO; GO:0032026; P:response to magnesium ion; IDA:UniProtKB.
DR CDD; cd06971; PgpA; 1.
DR InterPro; IPR026037; PgpA.
DR InterPro; IPR036681; PgpA-like_sf.
DR InterPro; IPR007686; YutG/PgpA.
DR PANTHER; PTHR36305; PTHR36305; 1.
DR Pfam; PF04608; PgpA; 1.
DR PIRSF; PIRSF006162; PgpA; 1.
DR SUPFAM; SSF101307; SSF101307; 1.
PE 1: Evidence at protein level;
KW Cell inner membrane; Cell membrane; Hydrolase; Lipid degradation;
KW Lipid metabolism; Magnesium; Membrane; Metal-binding;
KW Phospholipid degradation; Phospholipid metabolism; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..172
FT /note="Phosphatidylglycerophosphatase A"
FT /id="PRO_0000058359"
FT TOPO_DOM 1..31
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 32..52
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 53
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 54..74
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 75..141
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 142..162
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 163..172
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
SQ SEQUENCE 172 AA; 19418 MW; 9DA1C817CA36C8B9 CRC64;
MTILPRHKDV AKSRLKMSNP WHLLAVGFGS GLSPIVPGTM GSLAAIPFWY LMTFLPWQLY
SLVVMLGICI GVYLCHQTAK DMGVHDHGSI VWDEFIGMWI TLMALPTNDW QWVAAGFVIF
RILDMWKPWP IRWFDRNVHG GMGIMIDDIV AGVISAGILY FIGHHWPLGI LS
