WalR
- Description: two-component response regulator (OmpR family), controls cell wall metabolism
| Gene name | walR |
| Synonyms | yycF |
| Essential | yes PubMed |
| Product | two-component response regulator (OmpR family) |
| Function | control of cell wall metabolism |
| Gene expression levels in SubtiExpress: walR | |
| Interactions involving this protein in SubtInteract: WalR | |
| MW, pI | 27 kDa, 4.876 |
| Gene length, protein length | 705 bp, 235 aa |
| Immediate neighbours | walK, trnY-Phe |
| Sequences | Protein DNA DNA_with_flanks |
Genetic context 
This image was kindly provided by SubtiList
| |
Expression at a glance PubMed
| |
Contents
Categories containing this gene/protein
cell wall/ other, transcription factors and their control, essential genes, phosphoproteins
This gene is a member of the following regulons
The WalR regulon
The gene
Basic information
- Locus tag: BSU40410
Phenotypes of a mutant
- essential PubMed
- a constitutively active form of WalR (WalR-R204C) results in constitutive expression of the WalR regulon, and in combination with a sepF mutation to the formation of cell wall-less L-forms PubMed
Database entries
- BsubCyc: BSU40410
- DBTBS entry: [1]
- SubtiList entry: [2]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity:
- Protein family: OmpR family of two-component response regulators
- Paralogous protein(s):
Extended information on the protein
- Kinetic information:
- Modification: phosphorylated by WalK on an Asp residue
- Effectors of protein activity: phosphorylation likely affects DNA-binding activity
- Localization: cytoplasm (according to Swiss-Prot)
Database entries
- BsubCyc: BSU40410
- UniProt: P37478
- KEGG entry: [3]
- E.C. number:
Additional information
Expression and regulation
- Regulation:
- Regulatory mechanism:
- Additional information:
- number of protein molecules per cell (minimal medium with glucose and ammonium): 176 PubMed
Biological materials
- Mutant:
- Expression vector:
- lacZ fusion:
- GFP fusion:
- two-hybrid system:
- Antibody:
Labs working on this gene/protein
- Kevin Devine, Dublin
Your additional remarks
References
Reviews
The WalR regulon
Other original Publications
Alisha Dhiman, Sonika Bhatnagar, Parul Kulshreshtha, Rakesh Bhatnagar
Functional characterization of WalRK: A two-component signal transduction system from Bacillus anthracis.
FEBS Open Bio: 2014, 4;65-76
[PubMed:24490131]
[WorldCat.org]
[DOI]
(P e)
Wan-Zhen Huang, Jyun-Jhih Wang, Hui-Ju Chen, Jung-Tze Chen, Gwo-Chyuan Shaw
The heat-inducible essential response regulator WalR positively regulates transcription of sigI, mreBH and lytE in Bacillus subtilis under heat stress.
Res Microbiol: 2013, 164(10);998-1008
[PubMed:24125693]
[WorldCat.org]
[DOI]
(I p)
Patricia Domínguez-Cuevas, Romain Mercier, Mark Leaver, Yoshikazu Kawai, Jeff Errington
The rod to L-form transition of Bacillus subtilis is limited by a requirement for the protoplast to escape from the cell wall sacculus.
Mol Microbiol: 2012, 83(1);52-66
[PubMed:22122227]
[WorldCat.org]
[DOI]
(I p)
Akihiro Doi, Toshihide Okajima, Yasuhiro Gotoh, Katsuyuki Tanizawa, Ryutaro Utsumi
X-ray crystal structure of the DNA-binding domain of response regulator WalR essential to the cell viability of staphylococcus aureus and interaction with target DNA.
Biosci Biotechnol Biochem: 2010, 74(9);1901-7
[PubMed:20834167]
[WorldCat.org]
[DOI]
(I p)
Inga Jende, Kottayil I Varughese, Kevin M Devine
Amino acid identity at one position within the alpha1 helix of both the histidine kinase and the response regulator of the WalRK and PhoPR two-component systems plays a crucial role in the specificity of phosphotransfer.
Microbiology (Reading): 2010, 156(Pt 6);1848-1859
[PubMed:20167622]
[WorldCat.org]
[DOI]
(I p)
Yasuhiro Gotoh, Akihiro Doi, Eiji Furuta, Sarah Dubrac, Yoshimasa Ishizaki, Masato Okada, Masayuki Igarashi, Norihiko Misawa, Hirofumi Yoshikawa, Toshihide Okajima, Tarek Msadek, Ryutaro Utsumi
Novel antibacterial compounds specifically targeting the essential WalR response regulator.
J Antibiot (Tokyo): 2010, 63(3);127-34
[PubMed:20111065]
[WorldCat.org]
[DOI]
(I p)
Haiyan Zhao, Annie Heroux, Reuben D Sequeira, Liang Tang
Preliminary crystallographic studies of the regulatory domain of response regulator YycF from an essential two-component signal transduction system.
Acta Crystallogr Sect F Struct Biol Cryst Commun: 2009, 65(Pt 7);719-22
[PubMed:19574649]
[WorldCat.org]
[DOI]
(I p)
Tatsuya Fukushima, Hendrik Szurmant, Eun-Ja Kim, Marta Perego, James A Hoch
A sensor histidine kinase co-ordinates cell wall architecture with cell division in Bacillus subtilis.
Mol Microbiol: 2008, 69(3);621-32
[PubMed:18573169]
[WorldCat.org]
[DOI]
(I p)
Sarah Dubrac, Ivo Gomperts Boneca, Olivier Poupel, Tarek Msadek
New insights into the WalK/WalR (YycG/YycF) essential signal transduction pathway reveal a major role in controlling cell wall metabolism and biofilm formation in Staphylococcus aureus.
J Bacteriol: 2007, 189(22);8257-69
[PubMed:17827301]
[WorldCat.org]
[DOI]
(I p)
Patrick D McLaughlin, Benjamin G Bobay, Erin J Regel, Richele J Thompson, James A Hoch, John Cavanagh
Predominantly buried residues in the response regulator Spo0F influence specific sensor kinase recognition.
FEBS Lett: 2007, 581(7);1425-9
[PubMed:17350627]
[WorldCat.org]
[DOI]
(P p)
Hendrik Szurmant, Kristine Nelson, Eun-Ja Kim, Marta Perego, James A Hoch
YycH regulates the activity of the essential YycFG two-component system in Bacillus subtilis.
J Bacteriol: 2005, 187(15);5419-26
[PubMed:16030236]
[WorldCat.org]
[DOI]
(P p)
C Fabret, V A Feher, J A Hoch
Two-component signal transduction in Bacillus subtilis: how one organism sees its world.
J Bacteriol: 1999, 181(7);1975-83
[PubMed:10094672]
[WorldCat.org]
[DOI]
(P p)
C Fabret, J A Hoch
A two-component signal transduction system essential for growth of Bacillus subtilis: implications for anti-infective therapy.
J Bacteriol: 1998, 180(23);6375-83
[PubMed:9829949]
[WorldCat.org]
[DOI]
(P p)
