Difference between revisions of "Phosphoproteins"

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(→‎Phosphoproteins in B. subtilis)
(→‎Phosphoproteins in B. subtilis)
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* [[LytT]]: phosphorylated by [[LytS]]
 
* [[LytT]]: phosphorylated by [[LytS]]
 
* [[YesN]]: phosphorylated by [[YesM]]
 
* [[YesN]]: phosphorylated by [[YesM]]
−
* [[Spo0F]]: phosphorylated by [[KinA]], [[KinB]], [[KinC]], [[KinD]], or [[KinE]]
+
* [[Spo0F]]: part of the [[phosphorelay]], phosphorylated by [[KinA]], [[KinB]], [[KinC]], [[KinD]], or [[KinE]]
−
* [[Spo0A]]: phosphorylated by [[Spo0B]]
+
* [[Spo0A]]: part of the [[phosphorelay]], phosphorylated by [[Spo0B]]
  
 
===Phosphorylation on a Cys residue: Enzyme IIB components of the [[PTS]]===
 
===Phosphorylation on a Cys residue: Enzyme IIB components of the [[PTS]]===
−
** [[PtsG]]: glucose permease, EIICBA: phosphorylated by [[PtsG]]-IIA domain
+
* [[PtsG]]: glucose permease, EIICBA: phosphorylated by [[PtsG]]-IIA domain
−
** [[GamP]]: glucosamine permease, EIICBA: phosphorylated by [[GamP]]-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
+
* [[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
+
* [[SacP]]: sucrose permease (high affinity): phosphorylated by [[PtsG]]-IIA domain
−
** [[SacY]]: sucrose permease (low affinity): phosphorylated by [[PtsG]]-IIA domain
+
* [[SacY]]: sucrose permease (low affinity): phosphorylated by [[PtsG]]-IIA domain
−
** [[MtlA]]: mannitol permease: phosphorylated by [[MtlF]]
+
* [[MtlA]]: mannitol permease: phosphorylated by [[MtlF]]
−
** [[GmuB]]: galactomannan permease: phosphorylated by [[GmuA]]
+
* [[GmuB]]: galactomannan permease: phosphorylated by [[GmuA]]
−
** [[TreP]]: trehalose permease: phosphorylated by [[PtsG]]-IIA domain
+
* [[TreP]]: trehalose permease: phosphorylated by [[PtsG]]-IIA domain
−
** [[MalP]]: maltose permease: likely phosphorylated by [[PtsG]]-IIA domain
+
* [[MalP]]: maltose permease: likely phosphorylated by [[PtsG]]-IIA domain
−
** [[FruA]]: fructose permease: phosphorylated by [[FruA]]-IIA domain
+
* [[FruA]]: fructose permease: phosphorylated by [[FruA]]-IIA domain
−
** [[ManP]]: mannose permease: phosphorylated by [[ManP]]-IIA domain
+
* [[ManP]]: mannose permease: phosphorylated by [[ManP]]-IIA domain
−
** [[LicB]]: lichenan permease: phosphorylated by [[LicA]]
+
* [[LicB]]: lichenan permease: phosphorylated by [[LicA]]
−
** [[BglP]]: ß-glucoside permease: phosphorylated by [[BglP]]-IIA domain
+
* [[BglP]]: ß-glucoside permease: phosphorylated by [[BglP]]-IIA domain
  
 
===Phosphorylation on a His residue===
 
===Phosphorylation on a His residue===

Revision as of 07:13, 21 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


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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