Difference between revisions of "Phosphoproteins"

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(Phosphorylation on an Arg 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]]
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* [[ComGA]]
 
* [[ComGA]]
 
* [[ComK]]
 
* [[ComK]]
 
+
* [[CsoR]] (R24)
 
* [[DivIVA]]
 
* [[DivIVA]]
 
* [[FadB]]
 
* [[FadB]]
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* [[IlvB]]
 
* [[IlvB]]
 
* [[IlvC]]
 
* [[IlvC]]
 +
* [[IolE]] (R216)
 
* [[KatA]]
 
* [[KatA]]
 
* [[LeuB]]
 
* [[LeuB]]
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* [[McsA]]
 
* [[McsA]]
 
* [[Mdh]]
 
* [[Mdh]]
 +
* [[MelA]] (R56)
 
* [[MenB]]
 
* [[MenB]]
 
* [[MtnA]]
 
* [[MtnA]]

Revision as of 09:36, 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


Reviews


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