Functional and Structural Characterization of RsbU, a Stress Signaling Protein Phosphatase 2C

RsbU is a positive regulator of the activity of σB, the general stress-response σ factor of Gram+ microorganisms. The N-terminal domain of this protein has no significant sequence homology with proteins of known function, whereas the C-terminal domain is similar to the catalytic domains of PP2C-type...

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Veröffentlicht in:	The Journal of biological chemistry 2004-09, Vol.279 (39), p.40927-40937
Hauptverfasser:	Delumeau, Olivier, Dutta, Sujit, Brigulla, Matthias, Kuhnke, Grit, Hardwick, Steven W., Völker, Uwe, Yudkin, Michael D., Lewis, Richard J.
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence Bacillus subtilis Bacillus subtilis - metabolism Bacterial Proteins - chemistry Bacterial Proteins - physiology Crystallography, X-Ray Dose-Response Relationship, Drug Electrophoresis, Polyacrylamide Gel Hydrogen Bonding Models, Biological Models, Molecular Molecular Sequence Data Phenotype Phosphoprotein Phosphatases - chemistry Phosphoric Monoester Hydrolases - chemistry Phosphoric Monoester Hydrolases - metabolism Phosphoric Monoester Hydrolases - physiology Plasmids - metabolism Protein Binding Protein Conformation Protein Phosphatase 2C Protein Structure, Secondary Protein Structure, Tertiary Protein-Serine-Threonine Kinases - chemistry Sequence Homology, Amino Acid Signal Transduction Time Factors
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