RsbT

• Description: PP2C activator, protein serine kinase, phosphorylates RsbS, part of the stressosome
  
  

Gene name	rsbT
Synonyms	ycxT
Essential	no
Product	PP2C activator, protein serine kinase
Function	control of SigB activity
Interactions involving this protein in SubtInteract: RsbT
Metabolic function and regulation of this protein in SubtiPathways: Stress
MW, pI	14 kDa, 6.587
Gene length, protein length	399 bp, 133 aa
Immediate neighbours	rsbS, rsbU
Get the DNA and protein sequences (Barbe et al., 2009)
Genetic context This image was kindly provided by SubtiList

Categories containing this gene/protein

protein modification, sigma factors and their control

The gene

Basic information

• Locus tag: BSU04690

Database entries

• DBTBS entry: [1]

• SubtiList entry: [2]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity: phosphorylation of RsbR, RsbRB, RsbRC, and RsbRD PubMed

• Protein family:

• Paralogous protein(s):

Extended information on the protein

• Kinetic information:

• Domains:

• Modification:

• Cofactor(s):

• Effectors of protein activity:

• Interactions:
  • RsbS-RsbT PubMed, RsbR-RsbT PubMed, RsbRB-RsbT PubMed, RsbRC-RsbT PubMed, RsbRD-RsbT PubMed, RsbT-RsbU
  • component of the stressosome

• Localization:

Database entries

• Structure: 3VY9 (complete stressosome)

• UniProt: P42411

• KEGG entry: [3]

• E.C. number:

Expression and regulation

• Operon: rsbR-rsbS-rsbT-rsbU-rsbV-rsbW-sigB-rsbX PubMed

• Sigma factor: SigA PubMed

• Regulation: constitutively expressed PubMed

• Regulatory mechanism:

• Additional information:
  • RsbT is synthesized at the same rate as RsbRA and RsbS, however, the RsbT level in growing B. subtilis is only 10% that of RsbRA, suggesting that the protein is unstable PubMed.

Biological materials

• Mutant:

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

Labs working on this gene/protein

• Bill Haldenwang, San Antonio, USA
• Chet Price, Davis, USA homepage
• Rick Lewis, Newcastle, UK homepage

References

Original Articles

Additional publications: PubMed