McsB

• Description: protein arginine kinase, phosphorylates CtsR, modulator of CtsR-dependent repression
  
  

Gene name	mcsB
Synonyms	yacI
Essential	no
Product	protein arginine kinase
Function	control of CtsR activity
Metabolic function and regulation of this protein in SubtiPathways: Stress
MW, pI	40 kDa, 5.068
Gene length, protein length	1089 bp, 363 aa
Immediate neighbours	mcsA, clpC
Get the DNA and protein sequences (Barbe et al., 2009)
Genetic context This image was kindly provided by SubtiList

The gene

Basic information

• Locus tag: BSU00850

Database entries

• DBTBS entry: [1]

• SubtiList entry: [2]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity: phosphorylation of CtsR on Arg-62 PubMed

• Protein family: ATP:guanido phosphotransferase family (according to Swiss-Prot)

• Paralogous protein(s):

Extended information on the protein

• Kinetic information:

• Domains:

• Modification:

• Cofactor(s):

• Effectors of protein activity:

• Interactions: McsA-McsB-CtsR, McsB-CtsR, McsB-ClpC, McsA-McsB

• Localization:

Database entries

• Structure:

• UniProt: P37570

• KEGG entry: [3]

• E.C. number:

Expression and regulation

• Operon: ctsR-mcsA-mcsB-clpC-radA-disA PubMed

• Sigma factor: SigA PubMed, SigB PubMed1 PubMed2, SigF PubMed

• Regulation:
  • expressed early during sporulation in the forespore (SigF) PubMed
  • induced by stress (SigB) PubMed
  • induced by heat (CtsR) PubMed

• Regulatory mechanism:
  • CtsR: transcription repression PubMed

• Additional information:

Biological materials

• Mutant:

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

References

Reviews

Janine Kirstein, Noël Molière, David A Dougan, Kürşad Turgay
Adapting the machine: adaptor proteins for Hsp100/Clp and AAA+ proteases.
Nat Rev Microbiol: 2009, 7(8);589-99
[PubMed:19609260] [WorldCat.org] [DOI] (I p)

Original Publications

Jakob Fuhrmann, Andreas Schmidt, Silvia Spiess, Anita Lehner, Kürsad Turgay, Karl Mechtler, Emmanuelle Charpentier, Tim Clausen
McsB is a protein arginine kinase that phosphorylates and inhibits the heat-shock regulator CtsR.
Science: 2009, 324(5932);1323-7
[PubMed:19498169] [WorldCat.org] [DOI] (I p)

Jeanette Hahn, Naomi Kramer, Kenneth Briley, David Dubnau
McsA and B mediate the delocalization of competence proteins from the cell poles of Bacillus subtilis.
Mol Microbiol: 2009, 72(1);202-15
[PubMed:19226326] [WorldCat.org] [DOI] (I p)

Janine Kirstein, David A Dougan, Ulf Gerth, Michael Hecker, Kürşad Turgay
The tyrosine kinase McsB is a regulated adaptor protein for ClpCP.
EMBO J: 2007, 26(8);2061-70
[PubMed:17380125] [WorldCat.org] [DOI] (P p)

Stephanie T Wang, Barbara Setlow, Erin M Conlon, Jessica L Lyon, Daisuke Imamura, Tsutomu Sato, Peter Setlow, Richard Losick, Patrick Eichenberger
The forespore line of gene expression in Bacillus subtilis.
J Mol Biol: 2006, 358(1);16-37
[PubMed:16497325] [WorldCat.org] [DOI] (P p)

Janine Kirstein, Daniela Zühlke, Ulf Gerth, Kürşad Turgay, Michael Hecker
A tyrosine kinase and its activator control the activity of the CtsR heat shock repressor in B. subtilis.
EMBO J: 2005, 24(19);3435-45
[PubMed:16163393] [WorldCat.org] [DOI] (P p)

A Petersohn, M Brigulla, S Haas, J D Hoheisel, U Völker, M Hecker
Global analysis of the general stress response of Bacillus subtilis.
J Bacteriol: 2001, 183(19);5617-31
[PubMed:11544224] [WorldCat.org] [DOI] (P p)

E Krüger, D Zühlke, E Witt, H Ludwig, M Hecker
Clp-mediated proteolysis in Gram-positive bacteria is autoregulated by the stability of a repressor.
EMBO J: 2001, 20(4);852-63
[PubMed:11179229] [WorldCat.org] [DOI] (P p)

I Derré, G Rapoport, T Msadek
CtsR, a novel regulator of stress and heat shock response, controls clp and molecular chaperone gene expression in gram-positive bacteria.
Mol Microbiol: 1999, 31(1);117-31
[PubMed:9987115] [WorldCat.org] [DOI] (P p)

E Krüger, T Msadek, M Hecker
Alternate promoters direct stress-induced transcription of the Bacillus subtilis clpC operon.
Mol Microbiol: 1996, 20(4);713-23
[PubMed:8793870] [WorldCat.org] [DOI] (P p)