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
