WalR

• Description: two-component response regulator, controls cell wall metabolism
  
  

Gene name	walR
Synonyms	yycF
Essential	yes PubMed
Product	two-component response regulator
Function	control of cell wall metabolism
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
Get the DNA and protein sequences (Barbe et al., 2009)
Genetic context This image was kindly provided by SubtiList

Categories containing this gene/protein

cell wall/ other, transcription factors and their control, essential genes, phosphoproteins

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

• DBTBS entry: [1]

• SubtiList entry: [2]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity:

• Protein family: OmpR family of two-component transcription regulators

• Paralogous protein(s):

Extended information on the protein

• Kinetic information:

• Domains:

• Modification: phosphorylated by WalK on an Asp residue

• Cofactor(s):

• Effectors of protein activity: phosphorylation likely affects DNA-binding activity

• Interactions:
  • WalK-WalR

• Localization: cytoplasm (according to Swiss-Prot)

Database entries

• Structure: 2D1V (DNA binding domain), 2ZWM (receiver domain)

• UniProt: P37478

• KEGG entry: [3]

• E.C. number:

Expression and regulation

• Operon: walR-walK-yycH-yycI-walJ-yyxA PubMed

• Sigma factor:

• Regulation: expressed during vegetative growth, repressed during stationary phase PubMed

• Regulatory mechanism:

• Additional information:

Biological materials

• Mutant:

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

Labs working on this gene/protein

• Kevin Devine, Dublin

References

Other original Publications

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)