Difference between revisions of "Phosphoproteins"

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(→‎Phosphorylation on either a Ser, Thr or Tyr residue)
(→‎Phosphorylation on an Arg residue)
 
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==Phosphoproteins in ''B. subtilis''==
 
==Phosphoproteins in ''B. subtilis''==
 
===Phosphorylation on an Arg residue===
 
===Phosphorylation on an Arg residue===
−
* [[CtsR]], phosphorylated by [[McsB]]
+
* [[CtsR]] (R55), phosphorylated by [[McsB]]
 
* [[AccD]]
 
* [[AccD]]
 
* [[AhpF]]
 
* [[AhpF]]
 
* [[AlaR]]
 
* [[AlaR]]
 +
* [[AlbF]] (R17)
 
* [[Apt]]
 
* [[Apt]]
 
* [[ArgG]]
 
* [[ArgG]]
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* [[AtpH]]
 
* [[AtpH]]
 
* [[BdhA]]
 
* [[BdhA]]
 +
* [[BfmBAB]] (R23)
 
* [[ClpC]]
 
* [[ClpC]]
 
* [[ClpP]]
 
* [[ClpP]]
Line 46: Line 48:
 
* [[ComGA]]
 
* [[ComGA]]
 
* [[ComK]]
 
* [[ComK]]
−
 
+
* [[CsoR]] (R24)
 
* [[DivIVA]]
 
* [[DivIVA]]
 
* [[FadB]]
 
* [[FadB]]
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* [[IlvB]]
 
* [[IlvB]]
 
* [[IlvC]]
 
* [[IlvC]]
 +
* [[IolE]] (R216)
 
* [[KatA]]
 
* [[KatA]]
 +
* [[Kre]] (R26)
 
* [[LeuB]]
 
* [[LeuB]]
 
* [[LeuC]]
 
* [[LeuC]]
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* [[McsA]]
 
* [[McsA]]
 
* [[Mdh]]
 
* [[Mdh]]
 +
* [[MelA]] (R56)
 
* [[MenB]]
 
* [[MenB]]
 +
* [[MntB]] (R132)
 
* [[MtnA]]
 
* [[MtnA]]
  
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* [[Nin]]
 
* [[Nin]]
 
* [[OdhA]]
 
* [[OdhA]]
−
* [[OdhB]]
+
* [[OdhB]] (R300)
 
* [[OxdC]]
 
* [[OxdC]]
 
* [[PdxS]]
 
* [[PdxS]]
Line 90: Line 96:
 
* [[RecA]]
 
* [[RecA]]
 
* [[RplK]]
 
* [[RplK]]
−
* [[RplN]]
+
* [[RplN]] (R17)
 +
* [[RplV]] (R11)
 
* [[RplW]]
 
* [[RplW]]
 +
* [[RpmEB]]
 
* [[RpmGA]]
 
* [[RpmGA]]
 
* [[RpoB]]
 
* [[RpoB]]
 
* [[RpoC]]
 
* [[RpoC]]
 
* [[RpsG]]
 
* [[RpsG]]
−
* [[RpsH]]
+
* [[RpsH]] (R47, R72)
 
* [[RpsI]]
 
* [[RpsI]]
 
* [[RpsL]]
 
* [[RpsL]]
Line 102: Line 110:
 
* [[RpsN]]
 
* [[RpsN]]
 
* [[ScoC]]
 
* [[ScoC]]
 +
* [[SrfAA]] (R226)
 
* [[SrfAB]]
 
* [[SrfAB]]
 
* [[SsbA]]
 
* [[SsbA]]
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* [[ThyB]]
 
* [[ThyB]]
 
* [[Tig]]
 
* [[Tig]]
−
* [[TufA]]
+
* [[TufA]] (R384)
 
* [[YceE]]
 
* [[YceE]]
 
* [[YciC]]
 
* [[YciC]]
 
* [[YdcI]]
 
* [[YdcI]]
 
* [[YdjO]]
 
* [[YdjO]]
 +
* [[YerA]] (R14)
 
* [[YfmG]]
 
* [[YfmG]]
 
* [[YheA]]
 
* [[YheA]]
 +
* [[YkoM]] (R89)
 +
 
* [[YlbN]]
 
* [[YlbN]]
 
* [[YloV]]
 
* [[YloV]]
 +
* [[YpiF]] (R4)
 
* [[YrvO]]
 
* [[YrvO]]
−
* [[YtiA]]
+
 
 
* [[YtxH]]
 
* [[YtxH]]
 +
* [[YvfU]] (R116, R143)
 
* [[YvrO]]
 
* [[YvrO]]
  
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* [[CitZ]] [http://www.ncbi.nlm.nih.gov/pubmed/17218307 Macek ''et al''., 2007]  
 
* [[CitZ]] [http://www.ncbi.nlm.nih.gov/pubmed/17218307 Macek ''et al''., 2007]  
 
* [[CodY]] [http://www.ncbi.nlm.nih.gov/pubmed/17218307 Macek ''et al''., 2007]
 
* [[CodY]] [http://www.ncbi.nlm.nih.gov/pubmed/17218307 Macek ''et al''., 2007]
 +
* [[CotB]] [http://www.ncbi.nlm.nih.gov/pubmed/27185916 Nguyen ''et al''., 2016]
 
* [[CotG]] [http://www.ncbi.nlm.nih.gov/pubmed/25115591 Saggese ''et al''., 2014]
 
* [[CotG]] [http://www.ncbi.nlm.nih.gov/pubmed/25115591 Saggese ''et al''., 2014]
 
* [[DegS]] [http://www.ncbi.nlm.nih.gov/pubmed/17218307 Macek ''et al''., 2007]
 
* [[DegS]] [http://www.ncbi.nlm.nih.gov/pubmed/17218307 Macek ''et al''., 2007]

Latest revision as of 11:12, 24 October 2016

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

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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
    • SacX: 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
    • NagP: N-acetylglucosamine permease: phosphorylated by PtsG-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

Phosphorylation on a Ser residue

Phosphorylation on a Thr residue

Phosphorylation on a Tyr residue

Phosphorylation on either a Ser, Thr or Tyr residue

Original papers on the B. subtilis phosphoproteome

Vaishnavi Ravikumar, Lei Shi, Karsten Krug, Abderahmane Derouiche, Carsten Jers, Charlotte Cousin, Ahasanul Kobir, Ivan Mijakovic, Boris Macek
Quantitative phosphoproteome analysis of Bacillus subtilis reveals novel substrates of the kinase PrkC and phosphatase PrpC.
Mol Cell Proteomics: 2014, 13(8);1965-78
[PubMed:24390483] [WorldCat.org] [DOI] (I p)

Andreas Schmidt, Débora Broch Trentini, Silvia Spiess, Jakob Fuhrmann, Gustav Ammerer, Karl Mechtler, Tim Clausen
Quantitative phosphoproteomics reveals the role of protein arginine phosphorylation in the bacterial stress response.
Mol Cell Proteomics: 2014, 13(2);537-50
[PubMed:24263382] [WorldCat.org] [DOI] (I p)

Alexander K W Elsholz, Kürsad Turgay, Stephan Michalik, Bernd Hessling, Katrin Gronau, Dan Oertel, Ulrike Mäder, Jörg Bernhardt, Dörte Becher, Michael Hecker, Ulf Gerth
Global impact of protein arginine phosphorylation on the physiology of Bacillus subtilis.
Proc Natl Acad Sci U S A: 2012, 109(19);7451-6
[PubMed:22517742] [WorldCat.org] [DOI] (I p)

Boumediene Soufi, Chanchal Kumar, Florian Gnad, Matthias Mann, Ivan Mijakovic, Boris Macek
Stable isotope labeling by amino acids in cell culture (SILAC) applied to quantitative proteomics of Bacillus subtilis.
J Proteome Res: 2010, 9(7);3638-46
[PubMed:20509597] [WorldCat.org] [DOI] (I p)

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

Ahasanul Kobir, Lei Shi, Ana Boskovic, Christophe Grangeasse, Damjan Franjevic, Ivan Mijakovic
Protein phosphorylation in bacterial signal transduction.
Biochim Biophys Acta: 2011, 1810(10);989-94
[PubMed:21266190] [WorldCat.org] [DOI] (P p)

Jörg Stülke
More than just activity control: phosphorylation may control all aspects of a protein's properties.
Mol Microbiol: 2010, 77(2);273-5
[PubMed:20497498] [WorldCat.org] [DOI] (I p)

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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