Phosphatidylglycerophosphatase B - Escherichia coli (strain K12)

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P0A924 (PGPB_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 69. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended 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

Organism

Escherichia coli (strain K12) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia ›

Protein attributes

Sequence length	254 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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: K_M=530 µM for undecaprenyl pyrophosphate Ref.5 Ref.8 K_M=96 µM for farnesyl pyrophosphate K_M=80 µM for diacylglycerol pyrophosphate K_M=1700 µM for phosphatidate V_max=2167 nmol/min/mg enzyme with diacylglycerol pyrophosphate as substrate V_max=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 process	Lipid degradation Lipid metabolism Phospholipid degradation Phospholipid metabolism
Cellular component	Cell inner membrane Cell membrane Cell outer membrane Membrane
Domain	Transmembrane Transmembrane helix
Molecular function	Hydrolase
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	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_component	cell outer membrane Inferred from mutant phenotype Ref.1. Source: EcoCyc integral to plasma membrane Inferred from direct assay Ref.8. Source: EcoCyc
Molecular_function	diacylglycerol diphosphate phosphatase activity Inferred from electronic annotation. Source: EC phosphatidate phosphatase activity Inferred from electronic annotation. Source: 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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed

Chain

2 – 254

253

Phosphatidylglycerophosphatase B

PRO_0000058362

Regions

Topological domain

2 – 8

Cytoplasmic Potential

Transmembrane

9 – 29

Helical; Potential

Topological domain

30 – 47

Periplasmic Potential

Transmembrane

48 – 68

Helical; Potential

Topological domain

69 – 71

Cytoplasmic Potential

Transmembrane

72 – 92

Helical; Potential

Topological domain

93 – 158

Periplasmic Potential

Transmembrane

159 – 179

Helical; Potential

Topological domain

180 – 184

Cytoplasmic Potential

Transmembrane

185 – 205

Helical; Potential

Topological domain

206 – 210

Periplasmic Potential

Transmembrane

211 – 231

Helical; Potential

Topological domain

232 – 254

Cytoplasmic Potential

Region

97 – 105

Phosphatase sequence motif I

Region

160 – 163

Phosphatase sequence motif II

Region

200 – 211

Phosphatase sequence motif III

Sequences

Sequence

Length

Mass (Da)

Tools

P0A924 [UniParc].

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

254

29,021

        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' referencesShow '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.
[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. 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 277:1453-1474(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.
PIR	PAECGB. A30193.
RefSeq	NP_415794.1. NC_000913.2. YP_489546.1. NC_007779.1.
3D structure databases
ProteinModelPortal	P0A924.
ModBase	Search...
Protein-protein interaction databases
IntAct	P0A924. 1 interaction.
STRING	511145.b1278.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAC74360; AAC74360; b1278. BAA14832; BAA14832; BAA14832.
GeneID	12933201. 945863.
KEGG	ecj:Y75_p1253. eco:b1278.
PATRIC	32117818. VBIEscCol129921_1329.
Organism-specific databases
EchoBASE	EB0699.
EcoGene	EG10705. pgpB.
Phylogenomic databases
eggNOG	COG0671.
HOGENOM	HOG000286191.
KO	K01096.
OMA	SHWQFET.
ProtClustDB	PRK10699.
Enzyme and pathway databases
BioCyc	EcoCyc:PGPPHOSPHAB-MONOMER. ECOL316407:JW1270-MONOMER. MetaCyc:PGPPHOSPHAB-MONOMER.
UniPathway	UPA00084; UER00504.
Gene expression databases
Genevestigator	P0A924.
Family and domain databases
Gene3D	1.20.144.10. 2 hits.
InterPro	IPR016118. P_Acid_Pase/Cl_peroxidase_N. IPR000326. P_Acid_Pase_2/haloperoxidase. [Graphical view]
Pfam	PF01569. PAP2. 1 hit. [Graphical view]
SMART	SM00014. acidPPc. 1 hit. [Graphical view]
SUPFAM	SSF48317. AcPase_VanPerase. 1 hit.
ProtoNet	Search...

Entry information

Entry name

PGPB_ECOLI

Accession

Primary (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 1, 2013
This is version 69 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Escherichia coli

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

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Entry information

Relevant documents