Difference between revisions of "WalR"
| Line 39: | Line 39: | ||
= This gene is a member of the following [[regulons]] = | = This gene is a member of the following [[regulons]] = | ||
| − | + | =The [[WalR regulon]]= | |
=The gene= | =The gene= | ||
| Line 130: | Line 130: | ||
==Reviews== | ==Reviews== | ||
<pubmed>19019149, 18245295,18792692,</pubmed> | <pubmed>19019149, 18245295,18792692,</pubmed> | ||
| − | + | ==The [[WalR regulon]]== | |
| − | == | + | <pubmed>17581128,10878122,12950927, </pubmed> |
| − | <pubmed>18573169,17350627,10094672,17827301,9829949 | + | ==Other original Publications== |
| + | <pubmed>18573169,17350627,10094672,17827301,9829949,16030236,19574649, 20059685 20111065 20167622 20834167 </pubmed> | ||
[[Category:Protein-coding genes]] | [[Category:Protein-coding genes]] | ||
Revision as of 20:21, 4 January 2011
- 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 |
| 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
| |
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
Database entries
- DBTBS entry: [1]
- SubtiList entry: [2]
Additional information
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
- Localization: cytoplasm (according to Swiss-Prot)
Database entries
- UniProt: P37478
- KEGG entry: [3]
- E.C. number:
Additional information
Expression and regulation
- 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
Your additional remarks
References
Reviews
The WalR regulon
Other original Publications
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)
