Difference between revisions of "Mpr"

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= Categories containing this gene/protein =
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{{SubtiWiki category|[[utilization of nitrogen sources other than amino acids]]}}
 
=The protein=
 
=The protein=
  

Revision as of 18:06, 30 November 2010

  • Description: extracellular metalloprotease

Gene name mpr
Synonyms
Essential no
Product extracellular metalloprotease
Function protein degradation
MW, pI 33 kDa, 8.967
Gene length, protein length 939 bp, 313 aa
Immediate neighbours purT, ybfJ
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
Mpr context.gif
This image was kindly provided by SubtiList



The gene

Basic information

  • Locus tag: BSU02240

Phenotypes of a mutant

Database entries

  • DBTBS entry: no entry
  • SubtiList entry: [1]

Additional information

Categories containing this gene/protein

utilization of nitrogen sources other than amino acids

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity:
  • Protein family: peptidase S1B family (according to Swiss-Prot)
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification:
  • Cofactor(s):
  • Effectors of protein activity:
  • Interactions:
  • Localization: extracellular (signal peptide) PubMed

Database entries

  • Structure:
  • KEGG entry: [2]
  • E.C. number:

Additional information

Expression and regulation

  • Regulation: repressed by casamino acids 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

Reviews

Massimiliano Marvasi, Pieter T Visscher, Lilliam Casillas Martinez
Exopolymeric substances (EPS) from Bacillus subtilis: polymers and genes encoding their synthesis.
FEMS Microbiol Lett: 2010, 313(1);1-9
[PubMed:20735481] [WorldCat.org] [DOI] (I p)

Original publications

Birgit Voigt, Haike Antelmann, Dirk Albrecht, Armin Ehrenreich, Karl-Heinz Maurer, Stefan Evers, Gerhard Gottschalk, Jan Maarten van Dijl, Thomas Schweder, Michael Hecker
Cell physiology and protein secretion of Bacillus licheniformis compared to Bacillus subtilis.
J Mol Microbiol Biotechnol: 2009, 16(1-2);53-68
[PubMed:18957862] [WorldCat.org] [DOI] (I p)

Chi Hye Park, Sang Jun Lee, Sung Gu Lee, Weon Sup Lee, Si Myung Byun
Hetero- and autoprocessing of the extracellular metalloprotease (Mpr) in Bacillus subtilis.
J Bacteriol: 2004, 186(19);6457-64
[PubMed:15375126] [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)