Difference between revisions of "YlxP"

From SubtiWiki
Jump to: navigation, search
(Extended information on the protein)
Line 43: Line 43:
  
 
* '''Locus tag:''' BSU16640
 
* '''Locus tag:''' BSU16640
 +
 +
[http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=ylxP_1736156_1736434_1 Expression]
  
 
===Phenotypes of a mutant ===
 
===Phenotypes of a mutant ===

Revision as of 09:49, 25 January 2012

  • Description: general stress protein

Gene name ylxP
Synonyms ymxD
Essential no
Product unknown
Function unknown
MW, pI 10 kDa, 7.895
Gene length, protein length 276 bp, 92 aa
Immediate neighbours infB, rbfA
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
YlxP context.gif
This image was kindly provided by SubtiList



Categories containing this gene/protein

general stress proteins (controlled by SigB)

This gene is a member of the following regulons

SigB regulon, stringent response

The gene

Basic information

  • Locus tag: BSU16640

Expression

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:
  • 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

  • Regulation:
    • RelA dependent downregulation (Class I) during stringent response PubMed
    • induced by stress (SigB) 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

Dirk Höper, Uwe Völker, Michael Hecker
Comprehensive characterization of the contribution of individual SigB-dependent general stress genes to stress resistance of Bacillus subtilis.
J Bacteriol: 2005, 187(8);2810-26
[PubMed:15805528] [WorldCat.org] [DOI] (P p)

Christine Eymann, Georg Homuth, Christian Scharf, Michael Hecker
Bacillus subtilis functional genomics: global characterization of the stringent response by proteome and transcriptome analysis.
J Bacteriol: 2002, 184(9);2500-20
[PubMed:11948165] [WorldCat.org] [DOI] (P p)

K Shazand, J Tucker, M Grunberg-Manago, J C Rabinowitz, T Leighton
Similar organization of the nusA-infB operon in Bacillus subtilis and Escherichia coli.
J Bacteriol: 1993, 175(10);2880-7
[PubMed:8491709] [WorldCat.org] [DOI] (P p)