Difference between revisions of "RacX"

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* '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=racX_3533419_3534102_-1 racX] {{PubMed|22383849}}
 
* '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=racX_3533419_3534102_-1 racX] {{PubMed|22383849}}
  
* '''Sigma factor:''' [[SigW]] {{PubMed|8491712,12207695}}  
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* '''[[Sigma factor]]:''' [[SigW]] {{PubMed|8491712,12207695}}  
  
 
* '''Regulation:'''  
 
* '''Regulation:'''  
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=References=
 
=References=
  
<pubmed>8491712,19063962,9987136, 20431016,7592498, </pubmed>
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<pubmed>8491712,19063962,9987136, 20431016,7592498, 20817675</pubmed>
  
 
[[Category:Protein-coding genes]]
 
[[Category:Protein-coding genes]]

Revision as of 21:14, 18 June 2013

  • Description: amino acid racemase, production of D-amino acids, control of biofilm formation

Gene name racX
Synonyms
Essential no
Product amino acid racemase
Function control of biofilm formation
Gene expression levels in SubtiExpress: racX
MW, pI 25 kDa, 5.396
Gene length, protein length 681 bp, 227 aa
Immediate neighbours yveF, pbpE
Sequences Protein DNA DNA_with_flanks
Genetic context
RacX context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
RacX expression.png















Categories containing this gene/protein

biofilm formation, cell envelope stress proteins (controlled by SigM, V, W, X, Y)

This gene is a member of the following regulons

SigW regulon

The gene

Basic information

  • Locus tag: BSU34430

Phenotypes of a mutant

Database entries

  • DBTBS entry: [1]
  • SubtiList entry: [2]

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity:
  • Protein family: aspartate/glutamate racemases family (according to Swiss-Prot)
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification:
  • Cofactor(s):
  • Effectors of protein activity:

Database entries

  • Structure:
  • KEGG entry: [3]
  • E.C. number:

Additional information

Expression and regulation

  • 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

Onuma Chumsakul, Hiroki Takahashi, Taku Oshima, Takahiro Hishimoto, Shigehiko Kanaya, Naotake Ogasawara, Shu Ishikawa
Genome-wide binding profiles of the Bacillus subtilis transition state regulator AbrB and its homolog Abh reveals their interactive role in transcriptional regulation.
Nucleic Acids Res: 2011, 39(2);414-28
[PubMed:20817675] [WorldCat.org] [DOI] (I p)

Ilana Kolodkin-Gal, Diego Romero, Shugeng Cao, Jon Clardy, Roberto Kolter, Richard Losick
D-amino acids trigger biofilm disassembly.
Science: 2010, 328(5978);627-9
[PubMed:20431016] [WorldCat.org] [DOI] (I p)

María Mercedes Palomino, Carmen Sanchez-Rivas, Sandra M Ruzal
High salt stress in Bacillus subtilis: involvement of PBP4* as a peptidoglycan hydrolase.
Res Microbiol: 2009, 160(2);117-24
[PubMed:19063962] [WorldCat.org] [DOI] (P p)

X Huang, A Gaballa, M Cao, J D Helmann
Identification of target promoters for the Bacillus subtilis extracytoplasmic function sigma factor, sigma W.
Mol Microbiol: 1999, 31(1);361-71
[PubMed:9987136] [WorldCat.org] [DOI] (P p)

M A Strauch
Delineation of AbrB-binding sites on the Bacillus subtilis spo0H, kinB, ftsAZ, and pbpE promoters and use of a derived homology to identify a previously unsuspected binding site in the bsuB1 methylase promote.
J Bacteriol: 1995, 177(23);6999-7002
[PubMed:7592498] [WorldCat.org] [DOI] (P p)

D L Popham, P Setlow
Cloning, nucleotide sequence, and regulation of the Bacillus subtilis pbpE operon, which codes for penicillin-binding protein 4* and an apparent amino acid racemase.
J Bacteriol: 1993, 175(10);2917-25
[PubMed:8491712] [WorldCat.org] [DOI] (P p)