McsB
- Description: protein arginine kinase, 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
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Contents
Categories containing this gene/protein
protein modification, transcription factors and their control, sporulation proteins, general stress proteins (controlled by SigB), heat shock proteins
This gene is a member of the following regulons
CtsR regulon, SigB regulon, SigF regulon
The gene
Basic information
- Locus tag: BSU00850
Phenotypes of a mutant
Database entries
- DBTBS entry: [1]
- SubtiList entry: [2]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity: targets non-functional CtsR for degradation by ClpP/ClpC PubMed
- Protein family: ATP:guanido phosphotransferase family (according to Swiss-Prot)
- Paralogous protein(s):
Extended information on the protein
- Kinetic information:
- Domains:
- Cofactor(s):
- Effectors of protein activity:
- Interactions:
- Localization:
Database entries
- Structure:
- UniProt: P37570
- KEGG entry: [3]
- E.C. number:
Additional information
Expression and regulation
- Regulation:
- Additional information:
Biological materials
- Mutant:
- Expression vector:
- lacZ fusion:
- GFP fusion:
- two-hybrid system:
- Antibody:
Labs working on this gene/protein
Your additional remarks
References
Reviews
Original Publications
Alexander K W Elsholz, Stephan Michalik, Daniela Zühlke, Michael Hecker, Ulf Gerth
CtsR, the Gram-positive master regulator of protein quality control, feels the heat.
EMBO J: 2010, 29(21);3621-9
[PubMed:20852588]
[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)
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)
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)
Additional publications: PubMed