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 | + | ===Phosphorylation on a His residue=== |
* [[PTS]] proteins | * [[PTS]] proteins | ||
** [[ptsI|Enzyme I]]: autophosphorylated using phosphoenolpyruvate as phosphate donor | ** [[ptsI|Enzyme I]]: autophosphorylated using phosphoenolpyruvate as phosphate donor | ||
| Line 32: | Line 32: | ||
** [[ManR]]: phosphorylated by [[ptsH|HPr]] and likely by [[ManP]] | ** [[ManR]]: phosphorylated by [[ptsH|HPr]] and likely by [[ManP]] | ||
** [[MtlR]]: phosphorylated by [[ptsH|HPr]] and likely by [[MtlA]] | ** [[MtlR]]: phosphorylated by [[ptsH|HPr]] and likely by [[MtlA]] | ||
| + | |||
| + | * Protein kinases of [[two-component systems]] | ||
| + | These kinases are dimeric proteins. Phosphorylation occurs from one subunit to the other (not quite an autophosphorylation). | ||
| + | ** [[ComP]] | ||
| + | ** [[DegS]] | ||
| + | ** [[DesK]] | ||
| + | ** [[LiaS]] | ||
| + | ** [[YdfH]] | ||
| + | ** [[YfiJ]] | ||
| + | ** [[YhcY]] | ||
| + | ** [[YvfT]] | ||
| + | ** [[YxjM]] | ||
| + | ** [[BceS]] | ||
| + | ** [[CssS]] | ||
| + | ** [[NatK]] | ||
| + | ** [[PhoR]] | ||
| + | ** [[ResE]] | ||
| + | ** [[WalK]] | ||
| + | ** [[YbdK]] | ||
| + | ** [[YcbM]] | ||
| + | ** [[YclK]] | ||
| + | ** [[YkoH]] | ||
| + | ** [[YrkO]] | ||
| + | ** [[YvcQ]] | ||
| + | ** [[YvrG]] | ||
| + | ** [[YxdK]] | ||
| + | ** [[CheA]] | ||
| + | ** [[CitS]] | ||
| + | ** [[DctS]] | ||
| + | ** [[GlnK]] | ||
| + | ** [[MalK]] | ||
| + | ** [[LytS]] | ||
| + | ** [[YesM]] | ||
| + | ** [[YwpD]] | ||
| + | ** [[KinA]] | ||
| + | ** [[KinB]] | ||
| + | ** [[KinC]] | ||
| + | ** [[KinD]] | ||
| + | ** [[KinE]] | ||
| + | ** [[Spo0B]]: part of the [[phosphorelay]], phosphorylated by [[Spo0F]] | ||
==Proteins closely related to the PTS== | ==Proteins closely related to the PTS== | ||
Revision as of 19:08, 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
- Non-PTS proteins controlled by PTS-dependent phosphorylation
- GlpK: phosphorylated by HPr
- GlcT: phosphorylated by HPr and by PtsG
- LicT: phosphorylated by HPr and likely by BglP
- SacT: phosphorylated by HPr and likely by SacP
- SacY: phosphorylated by HPr and likely by SacY
- LevR: phosphorylated by HPr and by LevE
- LicR: phosphorylated by HPr and likely by LicB
- ManR: phosphorylated by HPr and likely by ManP
- MtlR: phosphorylated by HPr and likely by MtlA
- Protein kinases of two-component systems
These kinases are dimeric proteins. Phosphorylation occurs from one subunit to the other (not quite an autophosphorylation).
- 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
