Difference between revisions of "Phosphoproteins"

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(→‎Phosphoproteins in B. subtilis)
(→‎Phosphoproteins in B. subtilis)
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===Phosphorylation on an Arg residue===
 
===Phosphorylation on an Arg residue===
 
* [[CtsR]], phosphorylated by [[McsB]]
 
* [[CtsR]], phosphorylated by [[McsB]]
 +
 +
===Phosphorylation on an Asp residue: Response regulators of [[two-component systems]]===
 +
* [[ComA]]: phosphorylated by [[ComP]]
 +
* [[DegU]]: phosphorylated by [[DegS]]
 +
* [[DesR]]: phosphorylated by [[DesK]]
 +
* [[LiaR]]: phosphorylated by [[LiaS]]
 +
* [[YdfI]]: phosphorylated by [[YdfH]]
 +
* [[YfiK]]: phosphorylated by [[YfiJ]]
 +
* [[YhcZ]]: phosphorylated by [[YhcY]]
 +
* [[YvfU]]: phosphorylated by [[YvfT]]
 +
* [[YxjL]]: phosphorylated by [[YxjM]]
 +
* [[BceR]]: phosphorylated by [[BceS]]
 +
* [[CssR]]: phosphorylated by [[CssS]]
 +
* [[NatR]]: phosphorylated by [[NatK]]
 +
* [[PhoP]]: phosphorylated by [[PhoR]]
 +
* [[ResD]]: phosphorylated by [[ResE]]
 +
* [[WalR]]: phosphorylated by [[WalK]]
 +
* [[YbdJ]]: phosphorylated by [[YbdK]]
 +
* [[YcbL]]: phosphorylated by [[YcbM]]
 +
* [[YclJ]]: phosphorylated by [[YclK]]
 +
* [[YkoG]]: phosphorylated by [[YkoH]]
 +
* [[YrkP]]: phosphorylated by [[YrkO]]
 +
* [[YvcP]]: phosphorylated by [[YvcQ]]
 +
* [[YvrHb]]: phosphorylated by [[YvrG]]
 +
* [[YxdJ]]: phosphorylated by [[YxdK]]
 +
* [[CheY]]: phosphorylated by [[CheA]]
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* [[CitT]]: phosphorylated by [[CitS]]
 +
* [[DctR]]: phosphorylated by [[DctS]]
 +
* [[GlnL]]: phosphorylated by [[GlnK]]
 +
* [[MalR]]: phosphorylated by [[MalK]]
 +
* [[LytT]]: phosphorylated by [[LytS]]
 +
* [[YesN]]: phosphorylated by [[YesM]]
 +
* [[Spo0F]]: phosphorylated by [[KinA]], [[KinB]], [[KinC]], [[KinD]], or [[KinE]]
 +
* [[Spo0A]]: phosphorylated by [[Spo0B]]
 +
 +
===Phosphorylation on a Cys residue: Enzyme IIB components of the [[PTS]]===
 +
** [[PtsG]]: glucose permease, EIICBA: phosphorylated by [[PtsG]]-IIA domain
 +
** [[GamP]]: glucosamine permease, EIICBA: phosphorylated by [[GamP]]-IIA domain
 +
** [[MurP]]: N-acetyl muramic acid-specific phosphotransferase system, EIIBC: likely phosphorylated by [[PtsG]]-IIA domain
 +
** [[SacP]]: sucrose permease (high affinity): phosphorylated by [[PtsG]]-IIA domain
 +
** [[SacY]]: sucrose permease (low affinity): phosphorylated by [[PtsG]]-IIA domain
 +
** [[MtlA]]: mannitol permease: phosphorylated by [[MtlF]]
 +
** [[GmuB]]: galactomannan permease: phosphorylated by [[GmuA]]
 +
** [[TreP]]: trehalose permease: phosphorylated by [[PtsG]]-IIA domain
 +
** [[MalP]]: maltose permease: likely phosphorylated by [[PtsG]]-IIA domain
 +
** [[FruA]]: fructose permease: phosphorylated by [[FruA]]-IIA domain
 +
** [[ManP]]: mannose permease: phosphorylated by [[ManP]]-IIA domain
 +
** [[LicB]]: lichenan permease: phosphorylated by [[LicA]]
 +
** [[BglP]]: ß-glucoside permease: phosphorylated by [[BglP]]-IIA domain
 +
 
===Phosphorylation on a His residue===
 
===Phosphorylation on a His residue===
 
* [[PTS]] proteins
 
* [[PTS]] proteins
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** [[PtsG]]: glucose permease, EIICBA: phosphorylated by [[ptsH|HPr]]
 
** [[PtsG]]: glucose permease, EIICBA: phosphorylated by [[ptsH|HPr]]
 
** [[GamP]]: glucosamine permease, EIICBA: phosphorylated by [[ptsH|HPr]]
 
** [[GamP]]: glucosamine permease, EIICBA: phosphorylated by [[ptsH|HPr]]
−
** [[MtlA]], [[MtlF]]: mannitol permease: phosphorylated by [[ptsH|HPr]]
+
** [[MtlF]]: mannitol permease: phosphorylated by [[ptsH|HPr]]
−
** [[GmuA]], [[GmuB]], [[GmuC]]: galactomannan permease: phosphorylated by [[ptsH|HPr]]
+
** [[GmuA]]: galactomannan permease: phosphorylated by [[ptsH|HPr]]
−
** [[TreP]]: trehalose permease: phosphorylated by [[ptsH|HPr]]
 
 
** [[MalP]]: maltose permease: phosphorylated by [[ptsH|HPr]]
 
** [[MalP]]: maltose permease: phosphorylated by [[ptsH|HPr]]
 
** [[FruA]]: fructose permease: phosphorylated by [[ptsH|HPr]]
 
** [[FruA]]: fructose permease: phosphorylated by [[ptsH|HPr]]
 
** [[ManP]]: mannose permease: phosphorylated by [[ptsH|HPr]]
 
** [[ManP]]: mannose permease: phosphorylated by [[ptsH|HPr]]
−
** [[LevD]], [[LevE]], [[LevF]], [[LevG]]: fructose permease: phosphorylated by [[ptsH|HPr]]
+
** [[LevD]]: fructose permease: phosphorylated by [[ptsH|HPr]]
−
** [[LicA]], [[LicB]], [[LicC]]: lichenan permease: phosphorylated by [[ptsH|HPr]]
+
** [[LevE]]: fructose permease: phosphorylated by [[LevD]]
 +
** [[LicA]]: lichenan permease: phosphorylated by [[ptsH|HPr]]
 
** [[BglP]]: ß-glucoside permease
 
** [[BglP]]: ß-glucoside permease
 
** [[YpqE]]: unknown EIIA component: phosphorylated by [[ptsH|HPr]]
 
** [[YpqE]]: unknown EIIA component: phosphorylated by [[ptsH|HPr]]
−
** [[YyzE]]: unknown PTS protein
+
** [[YyzE]]: truncated PTS IIA protein: might perhaps be phosphorylated by [[ptsH|HPr]]
  
 
* Non-[[PTS]] proteins controlled by [[PTS]]-dependent phosphorylation
 
* Non-[[PTS]] proteins controlled by [[PTS]]-dependent phosphorylation
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** [[MtlR]]: phosphorylated by [[ptsH|HPr]] and likely by [[MtlA]]
 
** [[MtlR]]: phosphorylated by [[ptsH|HPr]] and likely by [[MtlA]]
  
−
* Protein kinases of [[two-component systems]]
+
* Protein kinases of [[two-component systems]] (These kinases are dimeric proteins. Phosphorylation occurs from one subunit to the other (not quite an autophosphorylation).)
−
These kinases are dimeric proteins. Phosphorylation occurs from one subunit to the other (not quite an autophosphorylation).
 
 
** [[ComP]]
 
** [[ComP]]
 
** [[DegS]]
 
** [[DegS]]

Revision as of 19:45, 20 January 2010

These proteins are subject to a phosphorylation event. Most often, protein phosphorylation affects the conformation of the protein resulting in changes in biological activity and/ or localization.

Phosphoproteins in B. subtilis

Phosphorylation on an Arg residue

Phosphorylation on an Asp residue: Response regulators of two-component systems

Phosphorylation on a Cys residue: Enzyme IIB components of the PTS

    • PtsG: glucose permease, EIICBA: phosphorylated by PtsG-IIA domain
    • GamP: glucosamine permease, EIICBA: phosphorylated by GamP-IIA domain
    • MurP: N-acetyl muramic acid-specific phosphotransferase system, EIIBC: likely phosphorylated by PtsG-IIA domain
    • SacP: sucrose permease (high affinity): phosphorylated by PtsG-IIA domain
    • SacY: sucrose permease (low affinity): phosphorylated by PtsG-IIA domain
    • MtlA: mannitol permease: phosphorylated by MtlF
    • GmuB: galactomannan permease: phosphorylated by GmuA
    • TreP: trehalose permease: phosphorylated by PtsG-IIA domain
    • MalP: maltose permease: likely phosphorylated by PtsG-IIA domain
    • FruA: fructose permease: phosphorylated by FruA-IIA domain
    • ManP: mannose permease: phosphorylated by ManP-IIA domain
    • LicB: lichenan permease: phosphorylated by LicA
    • BglP: ß-glucoside permease: phosphorylated by BglP-IIA domain

Phosphorylation on a His residue

  • PTS proteins
    • Enzyme I: autophosphorylated using phosphoenolpyruvate as phosphate donor
    • HPr: phosphorylated by Enzyme I
    • PtsG: glucose permease, EIICBA: phosphorylated by HPr
    • GamP: glucosamine permease, EIICBA: phosphorylated by HPr
    • MtlF: mannitol permease: phosphorylated by HPr
    • GmuA: galactomannan permease: phosphorylated by HPr
    • MalP: maltose permease: phosphorylated by HPr
    • FruA: fructose permease: phosphorylated by HPr
    • ManP: mannose permease: phosphorylated by HPr
    • LevD: fructose permease: phosphorylated by HPr
    • LevE: fructose permease: phosphorylated by LevD
    • LicA: lichenan permease: phosphorylated by HPr
    • BglP: ß-glucoside permease
    • YpqE: unknown EIIA component: phosphorylated by HPr
    • YyzE: truncated PTS IIA protein: might perhaps be phosphorylated by HPr

Proteins closely related to the PTS

  • Crh: HPr-like protein with exculsively regulatory functions (His-15 is not conserved
  • HprK: HPr-kinase, key factor for carbon catabolite repression

Related Lists

Original papers on the B. subtilis phosphoproteome

Christine Eymann, Dörte Becher, Jörg Bernhardt, Katrin Gronau, Anja Klutzny, Michael Hecker
Dynamics of protein phosphorylation on Ser/Thr/Tyr in Bacillus subtilis.
Proteomics: 2007, 7(19);3509-26
[PubMed:17726680] [WorldCat.org] [DOI] (P p)

Boris Macek, Ivan Mijakovic, Jesper V Olsen, Florian Gnad, Chanchal Kumar, Peter R Jensen, Matthias Mann
The serine/threonine/tyrosine phosphoproteome of the model bacterium Bacillus subtilis.
Mol Cell Proteomics: 2007, 6(4);697-707
[PubMed:17218307] [WorldCat.org] [DOI] (P p)

Alain Lévine, Françoise Vannier, Cédric Absalon, Lauriane Kuhn, Peter Jackson, Elaine Scrivener, Valérie Labas, Joëlle Vinh, Patrick Courtney, Jérôme Garin, Simone J Séror
Analysis of the dynamic Bacillus subtilis Ser/Thr/Tyr phosphoproteome implicated in a wide variety of cellular processes.
Proteomics: 2006, 6(7);2157-73
[PubMed:16493705] [WorldCat.org] [DOI] (P p)


Reviews

Daniel C Lee, Zongchao Jia
Emerging structural insights into bacterial tyrosine kinases.
Trends Biochem Sci: 2009, 34(7);351-7
[PubMed:19525115] [WorldCat.org] [DOI] (I p)

Mary Katherine Tarrant, Philip A Cole
The chemical biology of protein phosphorylation.
Annu Rev Biochem: 2009, 78;797-825
[PubMed:19489734] [WorldCat.org] [DOI] (I p)

Paul G Besant, Paul V Attwood
Detection and analysis of protein histidine phosphorylation.
Mol Cell Biochem: 2009, 329(1-2);93-106
[PubMed:19387796] [WorldCat.org] [DOI] (I p)

Emmanuelle Bechet, Sébastien Guiral, Sophie Torres, Ivan Mijakovic, Alain-Jean Cozzone, Christophe Grangeasse
Tyrosine-kinases in bacteria: from a matter of controversy to the status of key regulatory enzymes.
Amino Acids: 2009, 37(3);499-507
[PubMed:19189200] [WorldCat.org] [DOI] (I p)

Boris Macek, Matthias Mann, Jesper V Olsen
Global and site-specific quantitative phosphoproteomics: principles and applications.
Annu Rev Pharmacol Toxicol: 2009, 49;199-221
[PubMed:18834307] [WorldCat.org] [DOI] (P p)

Carsten Jers, Boumediene Soufi, Christophe Grangeasse, Josef Deutscher, Ivan Mijakovic
Phosphoproteomics in bacteria: towards a systemic understanding of bacterial phosphorylation networks.
Expert Rev Proteomics: 2008, 5(4);619-27
[PubMed:18761471] [WorldCat.org] [DOI] (I p)

Boumediene Soufi, Carsten Jers, Mette Erichsen Hansen, Dina Petranovic, Ivan Mijakovic
Insights from site-specific phosphoproteomics in bacteria.
Biochim Biophys Acta: 2008, 1784(1);186-92
[PubMed:17881301] [WorldCat.org] [DOI] (P p)

Christophe Grangeasse, Alain J Cozzone, Josef Deutscher, Ivan Mijakovic
Tyrosine phosphorylation: an emerging regulatory device of bacterial physiology.
Trends Biochem Sci: 2007, 32(2);86-94
[PubMed:17208443] [WorldCat.org] [DOI] (P p)

Ivan Mijakovic, Dina Petranovic, Nunzio Bottini, Josef Deutscher, Peter Ruhdal Jensen
Protein-tyrosine phosphorylation in Bacillus subtilis.
J Mol Microbiol Biotechnol: 2005, 9(3-4);189-97
[PubMed:16415592] [WorldCat.org] [DOI] (P p)

Josef Deutscher, Milton H Saier
Ser/Thr/Tyr protein phosphorylation in bacteria - for long time neglected, now well established.
J Mol Microbiol Biotechnol: 2005, 9(3-4);125-31
[PubMed:16415586] [WorldCat.org] [DOI] (P p)

Liang Shi
Manganese-dependent protein O-phosphatases in prokaryotes and their biological functions.
Front Biosci: 2004, 9;1382-97
[PubMed:14977554] [WorldCat.org] [DOI] (I e)

Alain J Cozzone, Christophe Grangeasse, Patricia Doublet, Bertrand Duclos
Protein phosphorylation on tyrosine in bacteria.
Arch Microbiol: 2004, 181(3);171-81
[PubMed:14745484] [WorldCat.org] [DOI] (P p)

Susanne Klumpp, Josef Krieglstein
Phosphorylation and dephosphorylation of histidine residues in proteins.
Eur J Biochem: 2002, 269(4);1067-71
[PubMed:11856347] [WorldCat.org] [DOI] (P p)

H S Cho, J G Pelton, D Yan, S Kustu, D E Wemmer
Phosphoaspartates in bacterial signal transduction.
Curr Opin Struct Biol: 2001, 11(6);679-84
[PubMed:11751048] [WorldCat.org] [DOI] (P p)

C J Bakal, J E Davies
No longer an exclusive club: eukaryotic signalling domains in bacteria.
Trends Cell Biol: 2000, 10(1);32-8
[PubMed:10603474] [WorldCat.org] [DOI] (P p)

P J Kennelly, M Potts
Fancy meeting you here! A fresh look at "prokaryotic" protein phosphorylation.
J Bacteriol: 1996, 178(16);4759-64
[PubMed:8759835] [WorldCat.org] [DOI] (P p)

L N Johnson, D Barford
The effects of phosphorylation on the structure and function of proteins.
Annu Rev Biophys Biomol Struct: 1993, 22;199-232
[PubMed:8347989] [WorldCat.org] [DOI] (P p)

R B Bourret, K A Borkovich, M I Simon
Signal transduction pathways involving protein phosphorylation in prokaryotes.
Annu Rev Biochem: 1991, 60;401-41
[PubMed:1883200] [WorldCat.org] [DOI] (P p)

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