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P0A924

- PGPB_ECOLI

UniProt

P0A924 - PGPB_ECOLI

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Protein

Phosphatidylglycerophosphatase B

Gene

pgpB

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.4 Publications

Catalytic activityi

Phosphatidylglycerophosphate + H2O = phosphatidylglycerol + phosphate.
1,2-diacyl-sn-glycerol 3-diphosphate + H2O = 1,2-diacyl-sn-glycerol 3-phosphate + phosphate.
A 1,2-diacylglycerol 3-phosphate + H2O = a 1,2-diacyl-sn-glycerol + phosphate.
Ditrans,octacis-undecaprenyl diphosphate + H2O = ditrans,octacis-undecaprenyl phosphate + phosphate.

Enzyme regulationi

Inhibited by Mn2+ ions.

Kineticsi

  1. KM=530 µM for undecaprenyl pyrophosphate2 Publications
  2. KM=96 µM for farnesyl pyrophosphate2 Publications
  3. KM=80 µM for diacylglycerol pyrophosphate2 Publications
  4. KM=1700 µM for phosphatidate2 Publications

Vmax=2167 nmol/min/mg enzyme with diacylglycerol pyrophosphate as substrate2 Publications

Vmax=313 nmol/min/mg enzyme with phosphatidate as substrate2 Publications

pH dependencei

Optimum pH is 6.5 for DGPP phosphatase activity and 6.5-7.5 for undecaprenyl pyrophosphate phosphatase activity.2 Publications

Pathwayi

GO - Molecular functioni

  1. diacylglycerol diphosphate phosphatase activity Source: UniProtKB-EC
  2. phosphatidate phosphatase activity Source: UniProtKB-EC
  3. phosphatidylglycerophosphatase activity Source: EcoCyc
  4. undecaprenyl-diphosphatase activity Source: EcoCyc

GO - Biological processi

  1. dephosphorylation Source: GOC
  2. glycerophospholipid biosynthetic process Source: EcoCyc
  3. peptidoglycan biosynthetic process Source: EcoCyc
  4. phosphatidylglycerol biosynthetic process Source: UniProtKB-UniPathway
  5. phospholipid catabolic process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Lipid degradation, Lipid metabolism, Phospholipid degradation, Phospholipid metabolism

Enzyme and pathway databases

BioCyciEcoCyc:PGPPHOSPHAB-MONOMER.
ECOL316407:JW1270-MONOMER.
MetaCyc:PGPPHOSPHAB-MONOMER.
UniPathwayiUPA00084; UER00504.

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphatidylglycerophosphatase B (EC:3.1.3.27)
Alternative name(s):
Diacylglycerol pyrophosphate phosphatase (EC:3.1.3.81)
Short name:
DGPP phosphatase
Phosphatidate phosphatase (EC:3.1.3.4)
Undecaprenyl pyrophosphate phosphatase (EC:3.6.1.27)
Undecaprenyl-diphosphatase
Gene namesi
Name:pgpB
Ordered Locus Names:b1278, JW1270
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG10705. pgpB.

Subcellular locationi

Cell inner membrane 1 Publication; Multi-pass membrane protein 1 Publication. Cell outer membrane 1 Publication; Multi-pass membrane protein 1 Publication

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini2 – 87CytoplasmicSequence Analysis
Transmembranei9 – 2921HelicalSequence AnalysisAdd
BLAST
Topological domaini30 – 4718PeriplasmicSequence AnalysisAdd
BLAST
Transmembranei48 – 6821HelicalSequence AnalysisAdd
BLAST
Topological domaini69 – 713CytoplasmicSequence Analysis
Transmembranei72 – 9221HelicalSequence AnalysisAdd
BLAST
Topological domaini93 – 15866PeriplasmicSequence AnalysisAdd
BLAST
Transmembranei159 – 17921HelicalSequence AnalysisAdd
BLAST
Topological domaini180 – 1845CytoplasmicSequence Analysis
Transmembranei185 – 20521HelicalSequence AnalysisAdd
BLAST
Topological domaini206 – 2105PeriplasmicSequence Analysis
Transmembranei211 – 23121HelicalSequence AnalysisAdd
BLAST
Topological domaini232 – 25423CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. cell outer membrane Source: EcoCyc
  2. integral component of plasma membrane Source: EcoCyc
  3. plasma membrane Source: EcoCyc
Complete GO annotation...

Keywords - Cellular componenti

Cell inner membrane, Cell membrane, Cell outer membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed
Chaini2 – 254253Phosphatidylglycerophosphatase BPRO_0000058362Add
BLAST

Post-translational modificationi

The N-terminus is blocked.

Expressioni

Gene expression databases

GenevestigatoriP0A924.

Interactioni

Protein-protein interaction databases

IntActiP0A924. 1 interaction.
STRINGi511145.b1278.

Structurei

3D structure databases

ProteinModelPortaliP0A924.
SMRiP0A924. Positions 2-254.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni97 – 1059Phosphatase sequence motif I
Regioni160 – 1634Phosphatase sequence motif II
Regioni200 – 21112Phosphatase sequence motif IIIAdd
BLAST

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0671.
HOGENOMiHOG000286191.
InParanoidiP0A924.
KOiK01096.
OMAiGMHYPID.
OrthoDBiEOG60CWKV.

Family and domain databases

Gene3Di1.20.144.10. 2 hits.
InterProiIPR000326. P_Acid_Pase_2/haloperoxidase.
[Graphical view]
PfamiPF01569. PAP2. 1 hit.
[Graphical view]
SMARTiSM00014. acidPPc. 1 hit.
[Graphical view]
SUPFAMiSSF48317. SSF48317. 2 hits.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P0A924-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MRSIARRTAV GAALLLVMPV AVWISGWRWQ PGEQSWLLKA AFWVTETVTQ
60 70 80 90 100
PWGVITHLIL FGWFLWCLRF RIKAAFVLFA ILAAAILVGQ GVKSWIKDKV
110 120 130 140 150
QEPRPFVIWL EKTHHIPVDE FYTLKRAERG NLVKEQLAEE KNIPQYLRSH
160 170 180 190 200
WQKETGFAFP SGHTMFAASW ALLAVGLLWP RRRTLTIAIL LVWATGVMGS
210 220 230 240 250
RLLLGMHWPR DLVVATLISW ALVAVATWLA QRICGPLTPP AEENREIAQR

EQES
Length:254
Mass (Da):29,021
Last modified:July 19, 2005 - v1
Checksum:i9F4E6E88C34D458C
GO

Mass spectrometryi

Molecular mass is 30151 Da from positions 2 - 254. Determined by MALDI. Reported mass includes mass of a C-terminal His6 tag.1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M23628 Unassigned DNA. Translation: AAB36618.1.
U00096 Genomic DNA. Translation: AAC74360.1.
AP009048 Genomic DNA. Translation: BAA14832.1.
PIRiA30193. PAECGB.
RefSeqiNP_415794.1. NC_000913.3.
YP_489546.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC74360; AAC74360; b1278.
BAA14832; BAA14832; BAA14832.
GeneIDi12933201.
945863.
KEGGiecj:Y75_p1253.
eco:b1278.
PATRICi32117818. VBIEscCol129921_1329.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M23628 Unassigned DNA. Translation: AAB36618.1 .
U00096 Genomic DNA. Translation: AAC74360.1 .
AP009048 Genomic DNA. Translation: BAA14832.1 .
PIRi A30193. PAECGB.
RefSeqi NP_415794.1. NC_000913.3.
YP_489546.1. NC_007779.1.

3D structure databases

ProteinModelPortali P0A924.
SMRi P0A924. Positions 2-254.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi P0A924. 1 interaction.
STRINGi 511145.b1278.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC74360 ; AAC74360 ; b1278 .
BAA14832 ; BAA14832 ; BAA14832 .
GeneIDi 12933201.
945863.
KEGGi ecj:Y75_p1253.
eco:b1278.
PATRICi 32117818. VBIEscCol129921_1329.

Organism-specific databases

EchoBASEi EB0699.
EcoGenei EG10705. pgpB.

Phylogenomic databases

eggNOGi COG0671.
HOGENOMi HOG000286191.
InParanoidi P0A924.
KOi K01096.
OMAi GMHYPID.
OrthoDBi EOG60CWKV.

Enzyme and pathway databases

UniPathwayi UPA00084 ; UER00504 .
BioCyci EcoCyc:PGPPHOSPHAB-MONOMER.
ECOL316407:JW1270-MONOMER.
MetaCyc:PGPPHOSPHAB-MONOMER.

Miscellaneous databases

PROi P0A924.

Gene expression databases

Genevestigatori P0A924.

Family and domain databases

Gene3Di 1.20.144.10. 2 hits.
InterProi IPR000326. P_Acid_Pase_2/haloperoxidase.
[Graphical view ]
Pfami PF01569. PAP2. 1 hit.
[Graphical view ]
SMARTi SM00014. acidPPc. 1 hit.
[Graphical view ]
SUPFAMi SSF48317. SSF48317. 2 hits.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  3. 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.

Entry informationi

Entry nameiPGPB_ECOLI
AccessioniPrimary (citable) accession number: P0A924
Secondary accession number(s): P18201
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 19, 2005
Last sequence update: July 19, 2005
Last modified: October 29, 2014
This is version 78 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3