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P0A925 (PGPB_ECO57) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 62. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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:Z2529, ECs1851
OrganismEscherichia coli O157:H7 [Complete proteome] [HAMAP]
Taxonomic identifier83334 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length254 AA.
Sequence statusComplete.
Protein existenceInferred from homology

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 By similarity.

Catalytic activity

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.

Pathway

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

Subcellular location

Cell inner membrane; Multi-pass membrane protein By similarity. Cell outer membrane; Multi-pass membrane protein By similarity.

Post-translational modification

The N-terminus is blocked By similarity.

Sequence similarities

Belongs to the PA-phosphatase related phosphoesterase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 254254Phosphatidylglycerophosphatase B
PRO_0000058361

Regions

Topological domain1 – 88Cytoplasmic By similarity
Transmembrane9 – 2921Helical; Potential
Topological domain30 – 4718Periplasmic By similarity
Transmembrane48 – 6821Helical; Potential
Topological domain69 – 713Cytoplasmic By similarity
Transmembrane72 – 9221Helical; Potential
Topological domain93 – 15866Periplasmic By similarity
Transmembrane159 – 17921Helical; Potential
Topological domain180 – 1845Cytoplasmic By similarity
Transmembrane185 – 20521Helical; Potential
Topological domain206 – 2105Periplasmic By similarity
Transmembrane211 – 23121Helical; Potential
Topological domain232 – 25423Cytoplasmic By similarity
Region97 – 1059Phosphatase sequence motif I
Region160 – 1634Phosphatase sequence motif II
Region200 – 21112Phosphatase sequence motif III

Sequences

Sequence LengthMass (Da)Tools
P0A925 [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

[1]"Genome sequence of enterohaemorrhagic Escherichia coli O157:H7."
Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J., Davis N.W. expand/collapse author list , Lim A., Dimalanta E.T., Potamousis K., Apodaca J., Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A., Blattner F.R.
Nature 409:529-533(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: O157:H7 / EDL933 / ATCC 700927 / EHEC.
[2]"Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and genomic comparison with a laboratory strain K-12."
Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K., Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T. expand/collapse author list , Kuhara S., Shiba T., Hattori M., Shinagawa H.
DNA Res. 8:11-22(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: O157:H7 / Sakai / RIMD 0509952 / EHEC.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE005174 Genomic DNA. Translation: AAG56535.1.
BA000007 Genomic DNA. Translation: BAB35274.1.
PIRC85759.
C90860.
RefSeqNP_287919.1. NC_002655.2.
NP_309878.1. NC_002695.1.

3D structure databases

ProteinModelPortalP0A925.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING155864.Z2529.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAG56535; AAG56535; Z2529.
BAB35274; BAB35274; BAB35274.
GeneID912812.
961380.
KEGGece:Z2529.
ecs:ECs1851.
PATRIC18353695. VBIEscCol44059_2064.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0671.
HOGENOMHOG000286191.
KOK01096.
OMAGMHYPID.
OrthoDBEOG60CWKV.

Enzyme and pathway databases

BioCycECOL386585:GJFA-1826-MONOMER.
ECOO157:PGPB-MONOMER.
UniPathwayUPA00084; UER00504.

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...

Entry information

Entry namePGPB_ECO57
AccessionPrimary (citable) accession number: P0A925
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 62 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