Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
twitter

Escherichia coli K-12 substr. MG1655 Enzyme: protein phosphatase 1 modulates phosphoproteins, signals protein misfolding



Gene: pphA Accession Numbers: G7011 (EcoCyc), b1838, ECK1837

Synonyms: yebX, prpA

Regulation Summary Diagram: ?

Summary:
PrpA and PrpB are phosphatases that act in transduction of the misfolded protein stress signal in a pathway that includes the CpxR-CpxA two-component system and which activates transcription of the htrA gene [Missiakas97a]. PrpA is involved in induction of the heat shock response [Missiakas97a]. PrpA and PrpB exhibit phosphatase activity toward phosphorylated serine/threonine and phosphorylated tyrosine in protein substrates [Missiakas97a].

PrpA and PrpB have similarity to the phosphoprotein phosphatase of bacteriophage lambda (lambdaPP) [White01a] and to Salmonella enterica serovar Typhimurium PrpA and PrpB proteins [Shi01a].

Review: [Pallen97].

Locations: cytosol

Map Position: [1,920,337 <- 1,920,993] (41.39 centisomes)
Length: 657 bp / 218 aa

Molecular Weight of Polypeptide: 25.274 kD (from nucleotide sequence)

Unification Links: ASAP:ABE-0006114 , EchoBASE:EB3780 , EcoGene:EG14026 , EcoliWiki:b1838 , ModBase:P55798 , OU-Microarray:b1838 , PortEco:pphA , PR:PRO_000023577 , Protein Model Portal:P55798 , RefSeq:NP_416352 , RegulonDB:G7011 , SMR:P55798 , String:511145.b1838 , Swiss-Model:P55798 , UniProt:P55798

Relationship Links: InterPro:IN-FAMILY:IPR004843 , InterPro:IN-FAMILY:IPR006186 , Pfam:IN-FAMILY:PF00149 , Prosite:IN-FAMILY:PS00125

Gene-Reaction Schematic: ?

GO Terms:

Biological Process: GO:0009266 - response to temperature stimulus Inferred from experiment [Missiakas97a]
GO:0016311 - dephosphorylation Inferred by computational analysis Inferred from experiment [Missiakas97a, UniProtGOA11, GOA01a]
GO:0008152 - metabolic process Inferred by computational analysis [UniProtGOA11, GOA01]
Molecular Function: GO:0008138 - protein tyrosine/serine/threonine phosphatase activity Inferred from experiment [Missiakas97a]
GO:0004721 - phosphoprotein phosphatase activity Inferred by computational analysis [UniProtGOA11, GOA01a]
GO:0016787 - hydrolase activity Inferred by computational analysis [UniProtGOA11, GOA01]
GO:0046872 - metal ion binding Inferred by computational analysis [UniProtGOA11]
Cellular Component: GO:0005829 - cytosol Inferred by computational analysis [DiazMejia09]

MultiFun Terms: cell processes adaptations other (mechanical, nutritional, oxidative stress)
cell processes adaptations temperature extremes
information transfer protein related posttranslational modification
regulation type of regulation posttranscriptional covalent modification, demodification, maturation
regulation type of regulation posttranscriptional inhibition / activation of enzymes

Essentiality data for pphA knockouts: ?

Growth Medium Growth? T (°C) O2 pH Osm/L Growth Observations
LB enriched Yes 37 Aerobic 6.95   Yes [Gerdes03, Comment 1]
LB Lennox Yes 37 Aerobic 7   Yes [Baba06, Comment 2]
M9 medium with 1% glycerol Yes 37 Aerobic 7.2 0.35 Yes [Joyce06, Comment 3]
MOPS medium with 0.4% glucose Yes 37 Aerobic 7.2 0.22 Yes [Baba06, Comment 2]

Enzymatic reaction of: protein-tyrosine-phosphatase (protein phosphatase 1 modulates phosphoproteins, signals protein misfolding)

Synonyms: phosphotyrosine phosphatase, protein-tyrosine-phosphate phosphohydrolase

EC Number: 3.1.3.48

a [protein]-L-tyrosine phosphate + H2O <=> a [protein]-L-tyrosine + phosphate

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.

The reaction is physiologically favored in the direction shown.

Citations: [Missiakas97a]


Enzymatic reaction of: phosphoprotein phosphatase (protein phosphatase 1 modulates phosphoproteins, signals protein misfolding)

Synonyms: phosphoprotein phosphohydrolase, serine/threonine specific protein phosphatase

EC Number: 3.1.3.16

a [protein] (L-serine/L-threonine) phosphate + H2O <=> a [protein]-(L-serine/L-threonine) + phosphate

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.

The reaction is physiologically favored in the direction shown.

Citations: [Missiakas97a]


Sequence Features

Feature Class Location Citations Comment
Mutagenesis-Variant 24
[Missiakas97a, UniProt11a]
Alternate sequence: D → V; UniProt: Loss of function.
Metal-Binding-Site 24
[UniProt10]
UniProt: Iron; Non-Experimental Qualifier: by similarity;
Mutagenesis-Variant 26
[Missiakas97a, UniProt11a]
Alternate sequence: H → N; UniProt: Loss of function.
Alternate sequence: H → L; UniProt: Loss of function.
Metal-Binding-Site 26
[UniProt10]
UniProt: Iron; Non-Experimental Qualifier: by similarity;
Metal-Binding-Site 53
[UniProt10]
UniProt: Iron; Non-Experimental Qualifier: by similarity;
Metal-Binding-Site 79
[UniProt10]
UniProt: Manganese; Non-Experimental Qualifier: by similarity;
Active-Site 80
[UniProt10]
UniProt: Proton donor; Non-Experimental Qualifier: by similarity;
Mutagenesis-Variant 107
[Missiakas97a, UniProt11a]
Alternate sequence: L → Q; UniProt: Loss of function.
Metal-Binding-Site 187
[UniProt10]
UniProt: Manganese; Non-Experimental Qualifier: by similarity;


Gene Local Context (not to scale): ?

Transcription Unit:

Notes:

History:
Peter D. Karp on Wed Jan 18, 2006:
Gene right-end position adjusted based on analysis performed in the 2005 E. coli annotation update [Riley06 ].
Markus Krummenacker on Tue Oct 14, 1997:
Gene object created from Blattner lab Genbank (v. M52) entry.


References

Baba06: Baba T, Ara T, Hasegawa M, Takai Y, Okumura Y, Baba M, Datsenko KA, Tomita M, Wanner BL, Mori H (2006). "Construction of Escherichia coli K-12 in-frame, single-gene knockout mutants: the Keio collection." Mol Syst Biol 2;2006.0008. PMID: 16738554

DiazMejia09: Diaz-Mejia JJ, Babu M, Emili A (2009). "Computational and experimental approaches to chart the Escherichia coli cell-envelope-associated proteome and interactome." FEMS Microbiol Rev 33(1);66-97. PMID: 19054114

Gerdes03: Gerdes SY, Scholle MD, Campbell JW, Balazsi G, Ravasz E, Daugherty MD, Somera AL, Kyrpides NC, Anderson I, Gelfand MS, Bhattacharya A, Kapatral V, D'Souza M, Baev MV, Grechkin Y, Mseeh F, Fonstein MY, Overbeek R, Barabasi AL, Oltvai ZN, Osterman AL (2003). "Experimental determination and system level analysis of essential genes in Escherichia coli MG1655." J Bacteriol 185(19);5673-84. PMID: 13129938

GOA01: GOA, DDB, FB, MGI, ZFIN (2001). "Gene Ontology annotation through association of InterPro records with GO terms."

GOA01a: GOA, MGI (2001). "Gene Ontology annotation based on Enzyme Commission mapping." Genomics 74;121-128.

Joyce06: Joyce AR, Reed JL, White A, Edwards R, Osterman A, Baba T, Mori H, Lesely SA, Palsson BO, Agarwalla S (2006). "Experimental and computational assessment of conditionally essential genes in Escherichia coli." J Bacteriol 188(23);8259-71. PMID: 17012394

Missiakas97a: Missiakas D, Raina S (1997). "Signal transduction pathways in response to protein misfolding in the extracytoplasmic compartments of E. coli: role of two new phosphoprotein phosphatases PrpA and PrpB." EMBO J 16(7);1670-85. PMID: 9130712

Pallen97: Pallen MJ, Wren BW (1997). "The HtrA family of serine proteases." Mol Microbiol 26(2);209-21. PMID: 9383148

Riley06: Riley M, Abe T, Arnaud MB, Berlyn MK, Blattner FR, Chaudhuri RR, Glasner JD, Horiuchi T, Keseler IM, Kosuge T, Mori H, Perna NT, Plunkett G, Rudd KE, Serres MH, Thomas GH, Thomson NR, Wishart D, Wanner BL (2006). "Escherichia coli K-12: a cooperatively developed annotation snapshot--2005." Nucleic Acids Res 34(1);1-9. PMID: 16397293

Shi01a: Shi L, Kehres DG, Maguire ME (2001). "The PPP-family protein phosphatases PrpA and PrpB of Salmonella enterica serovar Typhimurium possess distinct biochemical properties." J Bacteriol 183(24);7053-7. PMID: 11717262

UniProt10: UniProt Consortium (2010). "UniProt version 2010-07 released on 2010-06-15 00:00:00." Database.

UniProt11a: UniProt Consortium (2011). "UniProt version 2011-06 released on 2011-06-30 00:00:00." Database.

UniProtGOA11: UniProt-GOA (2011). "Gene Ontology annotation based on manual assignment of UniProtKB keywords in UniProtKB/Swiss-Prot entries."

White01a: White DJ, Reiter NJ, Sikkink RA, Yu L, Rusnak F (2001). "Identification of the high affinity Mn2+ binding site of bacteriophage lambda phosphoprotein phosphatase: effects of metal ligand mutations on electron paramagnetic resonance spectra and phosphatase activities." Biochemistry 40(30);8918-29. PMID: 11467953


Report Errors or Provide Feedback
Please cite the following article in publications resulting from the use of EcoCyc: Nucleic Acids Research 41:D605-12 2013
Page generated by SRI International Pathway Tools version 18.5 on Fri Nov 28, 2014, biocyc13.