Difference between revisions of "RacX"

From SubtiWiki
Jump to: navigation, search
(Expression and regulation)
Line 102: Line 102:
  
 
* '''Regulation:'''  
 
* '''Regulation:'''  
** repressed during logrithmic growth ([[AbrB]]) [http://www.ncbi.nlm.nih.gov/sites/entrez/7592498 PubMed]
+
** repressed during logrithmic growth ([[AbrB]]) [http://www.ncbi.nlm.nih.gov/sites/entrez/7592498 PubMed], probably indirect regulation by [[AbrB]] {{PubMed|20817675}}
 +
 
 
** induced by cell wall stress ([[SigW]]) {{PubMed|8491712,12207695}}  
 
** induced by cell wall stress ([[SigW]]) {{PubMed|8491712,12207695}}  
  
 
* '''Regulatory mechanism:'''  
 
* '''Regulatory mechanism:'''  
** [[AbrB]]:  transcription repression [http://www.ncbi.nlm.nih.gov/sites/entrez/7592498 PubMed]
 
  
 
* '''Additional information:'''
 
* '''Additional information:'''

Revision as of 17:04, 30 May 2011

  • 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
MW, pI 25 kDa, 5.396
Gene length, protein length 681 bp, 227 aa
Immediate neighbours yveF, pbpE
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
RacX context.gif
This image was kindly provided by SubtiList



Categories containing this gene/protein

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

This gene is a member of the following regulons

AbrB regulon, 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:
  • Interactions:
  • Localization:

Database entries

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

Additional information

Expression and regulation

  • 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

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)