Difference between revisions of "Phosphoproteins"
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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 | |
| − | + | * [[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=== | ===Phosphorylation on a His residue=== | ||
Revision as of 08:13, 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.
Contents
Phosphoproteins in B. subtilis
Phosphorylation on an Arg residue
Phosphorylation on an Asp residue: Response regulators of two-component systems
- ComA: phosphorylated by ComP
- DegU: phosphorylated by DegS
- DesR: phosphorylated by DesK
- LiaR: phosphorylated by LiaS
- YdfI: phosphorylated by YdfH
- YfiK: phosphorylated by YfiJ
- YhcZ: phosphorylated by YhcY
- YvfU: phosphorylated by YvfT
- YxjL: phosphorylated by YxjM
- BceR: phosphorylated by BceS
- CssR: phosphorylated by CssS
- NatR: phosphorylated by NatK
- PhoP: phosphorylated by PhoR
- ResD: phosphorylated by ResE
- WalR: phosphorylated by WalK
- YbdJ: phosphorylated by YbdK
- YcbL: phosphorylated by YcbM
- YclJ: phosphorylated by YclK
- YkoG: phosphorylated by YkoH
- YrkP: phosphorylated by YrkO
- YvcP: phosphorylated by YvcQ
- YvrHb: phosphorylated by YvrG
- YxdJ: phosphorylated by YxdK
- CheY: phosphorylated by CheA
- CitT: phosphorylated by CitS
- DctR: phosphorylated by DctS
- GlnL: phosphorylated by GlnK
- MalR: phosphorylated by MalK
- LytT: phosphorylated by LytS
- YesN: phosphorylated by YesM
- Spo0F: part of the phosphorelay, phosphorylated by KinA, KinB, KinC, KinD, or KinE
- Spo0A: part of the phosphorelay, phosphorylated by Spo0B
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
- 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
Reviews
