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P0A924 (PGPB_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 76. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Phosphatidylglycerophosphatase B

EC=3.1.3.27
Alternative name(s):
Diacylglycerol pyrophosphate phosphatase
Short name=DGPP phosphatase
EC=3.1.3.81
Phosphatidate phosphatase
EC=3.1.3.4
Undecaprenyl pyrophosphate phosphatase
EC=3.6.1.27
Undecaprenyl-diphosphatase
Gene names
Name:pgpB
Ordered Locus Names:b1278, JW1270
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length254 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the dephosphorylation of diacylglycerol diphosphate (DGPP) to phosphatidate (PA) and the subsequent dephosphorylation of PA to diacylglycerol (DAG). Also has undecaprenyl pyrophosphate phosphatase activity, required for the biosynthesis of the lipid carrier undecaprenyl phosphate. Can also use lysophosphatidic acid (LPA) and phosphatidylglycerophosphate as substrates. The pattern of activities varies according to subcellular location, PGP phosphatase activity is higher in the cytoplasmic membrane, whereas PA and LPA phosphatase activities are higher in the outer membrane. Activity is independent of a divalent cation ion and insensitive to inhibition by N-ethylmaleimide. Ref.5 Ref.6 Ref.8 Ref.9

Catalytic activity

Phosphatidylglycerophosphate + H2O = phosphatidylglycerol + phosphate. Ref.5 Ref.8

1,2-diacyl-sn-glycerol 3-diphosphate + H2O = 1,2-diacyl-sn-glycerol 3-phosphate + phosphate. Ref.5 Ref.8

A 1,2-diacylglycerol 3-phosphate + H2O = a 1,2-diacyl-sn-glycerol + phosphate. Ref.5 Ref.8

Ditrans,octacis-undecaprenyl diphosphate + H2O = ditrans,octacis-undecaprenyl phosphate + phosphate. Ref.5 Ref.8

Enzyme regulation

Inhibited by Mn2+ ions.

Pathway

Phospholipid metabolism; phosphatidylglycerol biosynthesis; phosphatidylglycerol from CDP-diacylglycerol: step 2/2.

Subcellular location

Cell inner membrane; Multi-pass membrane protein. Cell outer membrane; Multi-pass membrane protein Ref.1 Ref.7.

Post-translational modification

The N-terminus is blocked.

Sequence similarities

Belongs to the PA-phosphatase related phosphoesterase family.

Biophysicochemical properties

Kinetic parameters:

KM=530 µM for undecaprenyl pyrophosphate Ref.5 Ref.8

KM=96 µM for farnesyl pyrophosphate

KM=80 µM for diacylglycerol pyrophosphate

KM=1700 µM for phosphatidate

Vmax=2167 nmol/min/mg enzyme with diacylglycerol pyrophosphate as substrate

Vmax=313 nmol/min/mg enzyme with phosphatidate as substrate

pH dependence:

Optimum pH is 6.5 for DGPP phosphatase activity and 6.5-7.5 for undecaprenyl pyrophosphate phosphatase activity.

Mass spectrometry

Molecular mass is 30151 Da from positions 2 - 254. Determined by MALDI. Reported mass includes mass of a C-terminal His6 tag. Ref.8

Ontologies

Keywords
   Biological processLipid degradation
Lipid metabolism
Phospholipid degradation
Phospholipid metabolism
   Cellular componentCell inner membrane
Cell membrane
Cell outer membrane
Membrane
   DomainTransmembrane
Transmembrane helix
   Molecular functionHydrolase
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processdephosphorylation

Inferred from mutant phenotype PubMed 6296050. Source: GOC

glycerophospholipid biosynthetic process

Inferred from mutant phenotype PubMed 6296050. Source: EcoCyc

peptidoglycan biosynthetic process

Inferred from mutant phenotype Ref.6. Source: EcoCyc

phosphatidylglycerol biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

phospholipid catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcell outer membrane

Inferred from mutant phenotype Ref.1. Source: EcoCyc

integral component of plasma membrane

Inferred from direct assay Ref.8. Source: EcoCyc

plasma membrane

Inferred from mutant phenotype Ref.1. Source: EcoCyc

   Molecular_functiondiacylglycerol diphosphate phosphatase activity

Inferred from electronic annotation. Source: UniProtKB-EC

phosphatidate phosphatase activity

Inferred from electronic annotation. Source: UniProtKB-EC

phosphatidylglycerophosphatase activity

Inferred from mutant phenotype PubMed 6296050. Source: EcoCyc

undecaprenyl-diphosphatase activity

Inferred from direct assay Ref.8. Source: EcoCyc

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed
Chain2 – 254253Phosphatidylglycerophosphatase B
PRO_0000058362

Regions

Topological domain2 – 87Cytoplasmic Potential
Transmembrane9 – 2921Helical; Potential
Topological domain30 – 4718Periplasmic Potential
Transmembrane48 – 6821Helical; Potential
Topological domain69 – 713Cytoplasmic Potential
Transmembrane72 – 9221Helical; Potential
Topological domain93 – 15866Periplasmic Potential
Transmembrane159 – 17921Helical; Potential
Topological domain180 – 1845Cytoplasmic Potential
Transmembrane185 – 20521Helical; Potential
Topological domain206 – 2105Periplasmic Potential
Transmembrane211 – 23121Helical; Potential
Topological domain232 – 25423Cytoplasmic Potential
Region97 – 1059Phosphatase sequence motif I
Region160 – 1634Phosphatase sequence motif II
Region200 – 21112Phosphatase sequence motif III

Sequences

Sequence LengthMass (Da)Tools
P0A924 [UniParc].

Last modified July 19, 2005. Version 1.
Checksum: 9F4E6E88C34D458C

FASTA25429,021
        10         20         30         40         50         60 
MRSIARRTAV GAALLLVMPV AVWISGWRWQ PGEQSWLLKA AFWVTETVTQ PWGVITHLIL 

        70         80         90        100        110        120 
FGWFLWCLRF RIKAAFVLFA ILAAAILVGQ GVKSWIKDKV QEPRPFVIWL EKTHHIPVDE 

       130        140        150        160        170        180 
FYTLKRAERG NLVKEQLAEE KNIPQYLRSH WQKETGFAFP SGHTMFAASW ALLAVGLLWP 

       190        200        210        220        230        240 
RRRTLTIAIL LVWATGVMGS RLLLGMHWPR DLVVATLISW ALVAVATWLA QRICGPLTPP 

       250 
AEENREIAQR EQES 

« Hide

References

« Hide 'large scale' references
[1]"Membrane-bound phosphatases in Escherichia coli: sequence of the pgpB gene and dual subcellular localization of the pgpB product."
Icho T.
J. Bacteriol. 170:5117-5124(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 19-28, DUAL SUBCELLULAR LOCATION.
Strain: K12 / CS520.
[2]"A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 28.0-40.1 min region on the linkage map."
Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T., Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T., Mizobuchi K., Mori H., Mori T., Motomura K. expand/collapse author list , Nakade S., Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y., Wada C., Yamamoto Y., Horiuchi T.
DNA Res. 3:363-377(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[3]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[4]"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]"The Escherichia coli pgpB gene encodes for a diacylglycerol pyrophosphate phosphatase activity."
Dillon D.A., Wu W.I., Riedel B., Wissing J.B., Dowhan W., Carman G.M.
J. Biol. Chem. 271:30548-30553(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
Strain: K12.
[6]"Identification of multiple genes encoding membrane proteins with undecaprenyl pyrophosphate phosphatase (UppP) activity in Escherichia coli."
El Ghachi M., Derbise A., Bouhss A., Mengin-Lecreulx D.
J. Biol. Chem. 280:18689-18695(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[7]"Global topology analysis of the Escherichia coli inner membrane proteome."
Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.
Science 308:1321-1323(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
Strain: K12 / MG1655 / ATCC 47076.
[8]"Substrate specificity and membrane topology of Escherichia coli PgpB, an undecaprenyl pyrophosphate phosphatase."
Touze T., Blanot D., Mengin-Lecreulx D.
J. Biol. Chem. 283:16573-16583(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, MASS SPECTROMETRY.
[9]"Three phosphatidylglycerol-phosphate phosphatases in the inner membrane of Escherichia coli."
Lu Y.H., Guan Z., Zhao J., Raetz C.R.
J. Biol. Chem. 286:5506-5518(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M23628 Unassigned DNA. Translation: AAB36618.1.
U00096 Genomic DNA. Translation: AAC74360.1.
AP009048 Genomic DNA. Translation: BAA14832.1.
PIRPAECGB. A30193.
RefSeqNP_415794.1. NC_000913.3.
YP_489546.1. NC_007779.1.

3D structure databases

ProteinModelPortalP0A924.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP0A924. 1 interaction.
STRING511145.b1278.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC74360; AAC74360; b1278.
BAA14832; BAA14832; BAA14832.
GeneID12933201.
945863.
KEGGecj:Y75_p1253.
eco:b1278.
PATRIC32117818. VBIEscCol129921_1329.

Organism-specific databases

EchoBASEEB0699.
EcoGeneEG10705. pgpB.

Phylogenomic databases

eggNOGCOG0671.
HOGENOMHOG000286191.
KOK01096.
OMAGMHYPID.
OrthoDBEOG60CWKV.

Enzyme and pathway databases

BioCycEcoCyc:PGPPHOSPHAB-MONOMER.
ECOL316407:JW1270-MONOMER.
MetaCyc:PGPPHOSPHAB-MONOMER.
UniPathwayUPA00084; UER00504.

Gene expression databases

GenevestigatorP0A924.

Family and domain databases

Gene3D1.20.144.10. 2 hits.
InterProIPR000326. P_Acid_Pase_2/haloperoxidase.
[Graphical view]
PfamPF01569. PAP2. 1 hit.
[Graphical view]
SMARTSM00014. acidPPc. 1 hit.
[Graphical view]
SUPFAMSSF48317. SSF48317. 2 hits.
ProtoNetSearch...

Other

PROP0A924.

Entry information

Entry namePGPB_ECOLI
AccessionPrimary (citable) accession number: P0A924
Secondary accession number(s): P18201
Entry history
Integrated into UniProtKB/Swiss-Prot: July 19, 2005
Last sequence update: July 19, 2005
Last modified: May 14, 2014
This is version 76 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene