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P18200 (PGPA_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 114. 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 A

EC=3.1.3.27
Alternative name(s):
Phosphatidylglycerolphosphate phosphatase A
Short name=PGP phosphatase A
Gene names
Name:pgpA
Synonyms:yajN
Ordered Locus Names:b0418, JW0408
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length172 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Lipid phosphatase which dephosphorylates phosphatidylglycerophosphate (PGP) to phosphatidylglycerol (PG). Ref.1 Ref.6 Ref.8 Ref.9

Catalytic activity

Phosphatidylglycerophosphate + H2O = phosphatidylglycerol + phosphate. Ref.1 Ref.6 Ref.8 Ref.9

Cofactor

Magnesium. Ref.9

Pathway

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

Subcellular location

Cell inner membrane; Multi-pass membrane protein Ref.9.

Disruption phenotype

Displays 7-10 fold higher levels of phosphatidylglycerophosphate (PGP) than wild-type. Simultaneous deletion of pgpA and pgpB leads to 40 times higher PGP levels compared to wild-type, while simultaneous deletion of pgpA and pgpC leads to almost 100 times higher PGP levels. Lethal when combined with the deletion of both pgpB and pgpC. Ref.1 Ref.6 Ref.9

Sequence caution

The sequence AAA24325.1 differs from that shown. Reason: Frameshift at position 42. In addition, due to translation of the incorrect DNA strand, an unrelated ORF was predicted.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 172172Phosphatidylglycerophosphatase A
PRO_0000058359

Regions

Topological domain1 – 3131Cytoplasmic Potential
Transmembrane32 – 5221Helical; Potential
Topological domain531Periplasmic Potential
Transmembrane54 – 7421Helical; Potential
Topological domain75 – 14167Cytoplasmic Potential
Transmembrane142 – 16221Helical; Potential
Topological domain163 – 17210Periplasmic Potential

Sequences

Sequence LengthMass (Da)Tools
P18200 [UniParc].

Last modified November 1, 1997. Version 2.
Checksum: 9DA1C817CA36C8B9

FASTA17219,418
        10         20         30         40         50         60 
MTILPRHKDV AKSRLKMSNP WHLLAVGFGS GLSPIVPGTM GSLAAIPFWY LMTFLPWQLY 

        70         80         90        100        110        120 
SLVVMLGICI GVYLCHQTAK DMGVHDHGSI VWDEFIGMWI TLMALPTNDW QWVAAGFVIF 

       130        140        150        160        170 
RILDMWKPWP IRWFDRNVHG GMGIMIDDIV AGVISAGILY FIGHHWPLGI LS 

« Hide

References

« Hide 'large scale' references
[1]"Membrane-bound phosphatases in Escherichia coli: sequence of the pgpA gene."
Icho T.
J. Bacteriol. 170:5110-5116(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, DISRUPTION PHENOTYPE.
Strain: K12.
[2]Iida A., Hayashi M., Fujio T., Teshiba S.
Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[3]"Sequence of minutes 4-25 of Escherichia coli."
Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M., Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D., Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.
Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[4]"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.
[5]"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.
[6]"Multiple genes for membrane-bound phosphatases in Escherichia coli and their action on phospholipid precursors."
Icho T., Raetz C.R.
J. Bacteriol. 153:722-730(1983) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, CATALYTIC ACTIVITY, DISRUPTION PHENOTYPE.
Strain: K12.
[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: TOPOLOGY [LARGE SCALE ANALYSIS].
Strain: K12 / MG1655 / ATCC 47076.
[8]"A mitochondrial phosphatase required for cardiolipin biosynthesis: the PGP phosphatase Gep4."
Osman C., Haag M., Wieland F.T., Brugger B., Langer T.
EMBO J. 29:1976-1987(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, CATALYTIC ACTIVITY.
[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, CATALYTIC ACTIVITY, COFACTOR, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE.
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M23546 Genomic DNA. Translation: AAA24325.1. Sequence problems.
D17333 Genomic DNA. Translation: BAA21779.1.
U82664 Genomic DNA. Translation: AAB40174.1.
U00096 Genomic DNA. Translation: AAC73521.1.
AP009048 Genomic DNA. Translation: BAE76198.1.
PIRPAECGA. A30192.
B64771.
RefSeqNP_414952.1. NC_000913.3.
YP_488710.1. NC_007779.1.

3D structure databases

ProteinModelPortalP18200.
SMRP18200. Positions 84-163.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING511145.b0418.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC73521; AAC73521; b0418.
BAE76198; BAE76198; BAE76198.
GeneID12930347.
947542.
KEGGecj:Y75_p0406.
eco:b0418.
PATRIC32115985. VBIEscCol129921_0434.

Organism-specific databases

EchoBASEEB0698.
EcoGeneEG10704. pgpA.

Phylogenomic databases

eggNOGCOG1267.
HOGENOMHOG000256112.
KOK01095.
OMAYICDKAA.
OrthoDBEOG6P5ZM2.
PhylomeDBP18200.

Enzyme and pathway databases

BioCycEcoCyc:PGPPHOSPHAA-MONOMER.
ECOL316407:JW0408-MONOMER.
MetaCyc:PGPPHOSPHAA-MONOMER.
UniPathwayUPA00084; UER00504.

Gene expression databases

GenevestigatorP18200.

Family and domain databases

InterProIPR026037. PgpA.
IPR007686. YutG/PgpA.
[Graphical view]
PfamPF04608. PgpA. 1 hit.
[Graphical view]
PIRSFPIRSF006162. PgpA. 1 hit.
SUPFAMSSF101307. SSF101307. 1 hit.
ProtoNetSearch...

Other

PROP18200.

Entry information

Entry namePGPA_ECOLI
AccessionPrimary (citable) accession number: P18200
Secondary accession number(s): P77321, Q2MC08
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: November 1, 1997
Last modified: July 9, 2014
This is version 114 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

Escherichia coli

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