Difference between revisions of "Phosphoproteins"
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===Phosphorylation on an Arg residue=== | ===Phosphorylation on an Arg residue=== | ||
* [[CtsR]], phosphorylated by [[McsB]] | * [[CtsR]], phosphorylated by [[McsB]] | ||
+ | ===Phosphorylation on a His residue==== | ||
+ | * PTS proteins | ||
+ | ** [[ptsI|Enzyme I]]: autophosphorylated using phosphoenolpyruvate as phosphate donor | ||
+ | ** [[ptsH|HPr]]: phosphorylated by [[ptsI|Enzyme I]] | ||
+ | ** [[PtsG]]: glucose permease, EIICBA: phosphorylated by [[ptsH|HPr]] | ||
+ | ** [[GamP]]: glucosamine permease, EIICBA: phosphorylated by [[ptsH|HPr]] | ||
+ | ** [[MtlA]], [[MtlF]]: mannitol permease: phosphorylated by [[ptsH|HPr]] | ||
+ | ** [[GmuA]], [[GmuB]], [[GmuC]]: galactomannan permease: phosphorylated by [[ptsH|HPr]] | ||
+ | ** [[TreP]]: trehalose permease: phosphorylated by [[ptsH|HPr]] | ||
+ | ** [[MalP]]: maltose permease: phosphorylated by [[ptsH|HPr]] | ||
+ | ** [[FruA]]: fructose permease: phosphorylated by [[ptsH|HPr]] | ||
+ | ** [[ManP]]: mannose permease: phosphorylated by [[ptsH|HPr]] | ||
+ | ** [[LevD]], [[LevE]], [[LevF]], [[LevG]]: fructose permease: phosphorylated by [[ptsH|HPr]] | ||
+ | ** [[LicA]], [[LicB]], [[LicC]]: lichenan permease: phosphorylated by [[ptsH|HPr]] | ||
+ | ** [[BglP]]: ß-glucoside permease | ||
+ | ** [[YpqE]]: unknown EIIA component: phosphorylated by [[ptsH|HPr]] | ||
+ | ** [[YyzE]]: unknown PTS protein | ||
+ | |||
+ | * Non-PTS proteins controlled by PTS-dependent phosphorylation | ||
+ | ** [[GlpK]]: phosphorylated by [[ptsH|HPr]] | ||
+ | * | ||
+ | |||
+ | ==Proteins closely related to the PTS== | ||
+ | * [[Crh]]: [[ptsH|HPr]]-like protein with exculsively regulatory functions (His-15 is not conserved | ||
+ | * [[HprK]]: [[ptsH|HPr]]-kinase, key factor for carbon catabolite repression | ||
==Related Lists== | ==Related Lists== |
Revision as of 18:56, 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.
Contents
Phosphoproteins in B. subtilis
Phosphorylation on an Arg residue
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
- MtlA, MtlF: mannitol permease: phosphorylated by HPr
- GmuA, GmuB, GmuC: galactomannan permease: phosphorylated by HPr
- TreP: trehalose permease: phosphorylated by HPr
- MalP: maltose permease: phosphorylated by HPr
- FruA: fructose permease: phosphorylated by HPr
- ManP: mannose permease: phosphorylated by HPr
- LevD, LevE, LevF, LevG: fructose permease: phosphorylated by HPr
- LicA, LicB, LicC: lichenan permease: phosphorylated by HPr
- BglP: ß-glucoside permease
- YpqE: unknown EIIA component: phosphorylated by HPr
- YyzE: unknown PTS protein
- Crh: HPr-like protein with exculsively regulatory functions (His-15 is not conserved
- HprK: HPr-kinase, key factor for carbon catabolite repression
Related Lists
- two-component systems
- PTS
- PRD-containing transcription factors
- phosphorelay
- response regulator aspartate phosphatases
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)