Difference between revisions of "YvyD"

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(Categories containing this gene/protein)
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* '''Modification:'''
 
* '''Modification:'''
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** phosphorylated on Arg-6 {{PubMed|22517742}}
  
 
* '''Cofactor(s):'''
 
* '''Cofactor(s):'''
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=References=
 
=References=
  
<pubmed>11948165,9852014,10913081,,12107147 15805528, </pubmed>
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<pubmed>11948165,9852014,10913081,22517742,12107147 15805528, </pubmed>
  
 
[[Category:Protein-coding genes]]
 
[[Category:Protein-coding genes]]

Revision as of 17:59, 21 April 2012

  • Description: general stress protein, required for ribosome dimerization in the stationary phase

Gene name yvyD
Synonyms yviI
Essential no
Product unknown
Function dimerization of ribosomes in the stationary phase
MW, pI 21 kDa, 5.184
Gene length, protein length 567 bp, 189 aa
Immediate neighbours secA, smiA
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
YvyD context.gif
This image was kindly provided by SubtiList



Categories containing this gene/protein

general stress proteins (controlled by SigB), membrane proteins, phosphoproteins

This gene is a member of the following regulons

SigB regulon, SigH regulon

The gene

Basic information

  • Locus tag: BSU35310

Phenotypes of a mutant

  • the mutant is cold-sensitive
  • delayed recovery from stationary phase and delayed germination

Database entries

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

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity:
  • Protein family: ribosomal protein S30Ae family (according to Swiss-Prot)
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification:
    • phosphorylated on Arg-6 PubMed
  • Cofactor(s):
  • Effectors of protein activity:

Database entries

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

Additional information

Expression and 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

Alexander K W Elsholz, Kürsad Turgay, Stephan Michalik, Bernd Hessling, Katrin Gronau, Dan Oertel, Ulrike Mäder, Jörg Bernhardt, Dörte Becher, Michael Hecker, Ulf Gerth
Global impact of protein arginine phosphorylation on the physiology of Bacillus subtilis.
Proc Natl Acad Sci U S A: 2012, 109(19);7451-6
[PubMed:22517742] [WorldCat.org] [DOI] (I 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)

Ulrike Mäder, Georg Homuth, Christian Scharf, Knut Büttner, Rüdiger Bode, Michael Hecker
Transcriptome and proteome analysis of Bacillus subtilis gene expression modulated by amino acid availability.
J Bacteriol: 2002, 184(15);4288-95
[PubMed:12107147] [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)

H Antelmann, C Scharf, M Hecker
Phosphate starvation-inducible proteins of Bacillus subtilis: proteomics and transcriptional analysis.
J Bacteriol: 2000, 182(16);4478-90
[PubMed:10913081] [WorldCat.org] [DOI] (P p)

K Drzewiecki, C Eymann, G Mittenhuber, M Hecker
The yvyD gene of Bacillus subtilis is under dual control of sigmaB and sigmaH.
J Bacteriol: 1998, 180(24);6674-80
[PubMed:9852014] [WorldCat.org] [DOI] (P p)