Difference between revisions of "YraA"

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=== Database entries ===
 
=== Database entries ===
 +
* '''BsubCyc:''' [http://bsubcyc.org/BSUB/NEW-IMAGE?type=NIL&object=BSU27020&redirect=T BSU27020]
  
 
* '''DBTBS entry:''' [http://dbtbs.hgc.jp/COG/prom/yraA.html]
 
* '''DBTBS entry:''' [http://dbtbs.hgc.jp/COG/prom/yraA.html]
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=== Database entries ===
 
=== Database entries ===
 +
* '''BsubCyc:''' [http://bsubcyc.org/BSUB/NEW-IMAGE?type=NIL&object=BSU27020&redirect=T BSU27020]
  
 
* '''Structure:'''
 
* '''Structure:'''

Revision as of 14:20, 2 April 2014

  • Description: general stress protein, degradation of damaged thiol-containing proteins, glyoxalase III-like enzyme

Gene name yraA
Synonyms
Essential no
Product glyoxalase III-like enzyme
Function detoxification of methylglyoxal
Gene expression levels in SubtiExpress: yraA
MW, pI 18 kDa, 4.729
Gene length, protein length 507 bp, 169 aa
Immediate neighbours adhA, sacC
Sequences Protein DNA DNA_with_flanks
Genetic context
YraA context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
500px















Categories containing this gene/protein

proteolysis, general stress proteins (controlled by SigB), resistance against oxidative and electrophile stress

This gene is a member of the following regulons

AdhR regulon, SigB regulon, SigM regulon

The gene

Basic information

  • Locus tag: BSU27020

Phenotypes of a mutant

Database entries

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

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity:
    • methylglyoxal --> D-lactate PubMed
  • Protein family: peptidase C56 family (according to Swiss-Prot)
  • Paralogous protein(s): YfkM

Extended information on the protein

  • Kinetic information:
  • Modification:
  • Effectors of protein activity:

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

Pete Chandrangsu, Renata Dusi, Chris J Hamilton, John D Helmann
Methylglyoxal resistance in Bacillus subtilis: contributions of bacillithiol-dependent and independent pathways.
Mol Microbiol: 2014, 91(4);706-15
[PubMed:24330391] [WorldCat.org] [DOI] (I p)

Alexander Reder, Dirk Höper, Ulf Gerth, Michael Hecker
Contributions of individual σB-dependent general stress genes to oxidative stress resistance of Bacillus subtilis.
J Bacteriol: 2012, 194(14);3601-10
[PubMed:22582280] [WorldCat.org] [DOI] (I p)

Thi Thu Huyen Nguyen, Warawan Eiamphungporn, Ulrike Mäder, Manuel Liebeke, Michael Lalk, Michael Hecker, John D Helmann, Haike Antelmann
Genome-wide responses to carbonyl electrophiles in Bacillus subtilis: control of the thiol-dependent formaldehyde dehydrogenase AdhA and cysteine proteinase YraA by the MerR-family regulator YraB (AdhR).
Mol Microbiol: 2009, 71(4);876-94
[PubMed:19170879] [WorldCat.org] [DOI] (I p)

Adrian J Jervis, Penny D Thackray, Chris W Houston, Malcolm J Horsburgh, Anne Moir
SigM-responsive genes of Bacillus subtilis and their promoters.
J Bacteriol: 2007, 189(12);4534-8
[PubMed:17434969] [WorldCat.org] [DOI] (P p)

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)