YraA

• 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
Metabolic function and regulation of this protein in SubtiPathways: 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 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

Database entries

• BsubCyc: BSU27020

• DBTBS entry: [1]

• SubtiList entry: [2]

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:

• Domains:

• Modification:

• Cofactors:

• Effectors of protein activity:

• Interactions:

• Localization:

Database entries

• BsubCyc: BSU27020

• Structure:

• UniProt: O06006

• KEGG entry: [3]

• E.C. number:

Expression and regulation

• Operon:
  • adhA-yraA PubMed
  • yraA

• Expression browser: yraA PubMed

• Sigma factor:
  • yraA: SigB PubMed, SigM PubMed

• Regulation:
  • adhA: induced in the presence of the toxic carbonyls methylglyoxal and formaldehyde (AdhR) PubMed
  • yraA: induced by stress (SigB) PubMed

• Regulatory mechanism:
  • AdhR: transcription activation PubMed

• Additional information:
  • number of protein molecules per cell (minimal medium with glucose and ammonium): 1006 PubMed
  • number of protein molecules per cell (complex medium with amino acids, without glucose): 871 PubMed

Biological materials

• Mutant:

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

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)