Difference between revisions of "Phosphoproteins"

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(Phosphorylation on an Arg residue)
(Phosphorylation on an Arg residue)
 
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Line 72: Line 72:
 
* [[IolE]] (R216)
 
* [[IolE]] (R216)
 
* [[KatA]]
 
* [[KatA]]
 +
* [[Kre]] (R26)
 
* [[LeuB]]
 
* [[LeuB]]
 
* [[LeuC]]
 
* [[LeuC]]
Line 80: Line 81:
 
* [[MelA]] (R56)
 
* [[MelA]] (R56)
 
* [[MenB]]
 
* [[MenB]]
 +
* [[MntB]] (R132)
 
* [[MtnA]]
 
* [[MtnA]]
  
Line 86: Line 88:
 
* [[Nin]]
 
* [[Nin]]
 
* [[OdhA]]
 
* [[OdhA]]
* [[OdhB]]
+
* [[OdhB]] (R300)
 
* [[OxdC]]
 
* [[OxdC]]
 
* [[PdxS]]
 
* [[PdxS]]
Line 94: Line 96:
 
* [[RecA]]
 
* [[RecA]]
 
* [[RplK]]
 
* [[RplK]]
* [[RplN]]
+
* [[RplN]] (R17)
 +
* [[RplV]] (R11)
 
* [[RplW]]
 
* [[RplW]]
 
* [[RpmEB]]
 
* [[RpmEB]]
Line 101: Line 104:
 
* [[RpoC]]
 
* [[RpoC]]
 
* [[RpsG]]
 
* [[RpsG]]
* [[RpsH]]
+
* [[RpsH]] (R47, R72)
 
* [[RpsI]]
 
* [[RpsI]]
 
* [[RpsL]]
 
* [[RpsL]]
Line 107: Line 110:
 
* [[RpsN]]
 
* [[RpsN]]
 
* [[ScoC]]
 
* [[ScoC]]
 +
* [[SrfAA]] (R226)
 
* [[SrfAB]]
 
* [[SrfAB]]
 
* [[SsbA]]
 
* [[SsbA]]
Line 113: Line 117:
 
* [[ThyB]]
 
* [[ThyB]]
 
* [[Tig]]
 
* [[Tig]]
* [[TufA]]
+
* [[TufA]] (R384)
 
* [[YceE]]
 
* [[YceE]]
 
* [[YciC]]
 
* [[YciC]]
 
* [[YdcI]]
 
* [[YdcI]]
 
* [[YdjO]]
 
* [[YdjO]]
 +
* [[YerA]] (R14)
 
* [[YfmG]]
 
* [[YfmG]]
 
* [[YheA]]
 
* [[YheA]]
 +
* [[YkoM]] (R89)
 +
 
* [[YlbN]]
 
* [[YlbN]]
 
* [[YloV]]
 
* [[YloV]]
 +
* [[YpiF]] (R4)
 
* [[YrvO]]
 
* [[YrvO]]
  
 
* [[YtxH]]
 
* [[YtxH]]
 +
* [[YvfU]] (R116, R143)
 
* [[YvrO]]
 
* [[YvrO]]
  

Latest revision as of 11:12, 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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