YlxP

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  • Description: general stress protein

Gene name ylxP
Synonyms ymxD
Essential no
Product unknown
Function unknown
Gene expression levels in SubtiExpress: ylxP
MW, pI 10 kDa, 7.895
Gene length, protein length 276 bp, 92 aa
Immediate neighbours infB, rbfA
Sequences Protein DNA DNA_with_flanks
Genetic context
YlxP context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
YlxP expression.png
























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

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)