Difference between revisions of "GmuG"

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(Extended information on the protein)
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* '''Locus tag:''' BSU05880
 
* '''Locus tag:''' BSU05880
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[http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=gmuG_632774_633862_1 Expression]
  
 
===Phenotypes of a mutant ===
 
===Phenotypes of a mutant ===

Revision as of 14:29, 24 January 2012

  • Description: beta-1,4-mannanase

Gene name gmuG
Synonyms ydhT
Essential no
Product beta-1,4-mannanase
Function glucomannan utilization
Metabolic function and regulation of this protein in SubtiPathways:
Sugar catabolism
MW, pI 40 kDa, 5.628
Gene length, protein length 1086 bp, 362 aa
Immediate neighbours gmuF, ydhU/1
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
YdhT context.gif
This image was kindly provided by SubtiList







Categories containing this gene/protein

utilization of specific carbon sources

This gene is a member of the following regulons

AbrB regulon, CcpA regulon, GmuR regulon

The gene

Basic information

  • Locus tag: BSU05880

Expression

Phenotypes of a mutant

Database entries

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

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: Random hydrolysis of (1->4)-beta-D-mannosidic linkages in mannans, galactomannans and glucomannans (according to Swiss-Prot)
  • Protein family: glycosyl hydrolase 26 family (according to Swiss-Prot)
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification:
  • Cofactor(s):
  • Effectors of protein activity:

Database entries

  • KEGG entry: [3]

Additional information

Expression and regulation

  • 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

Additional publications: PubMed

Christian Degering, Thorsten Eggert, Michael Puls, Johannes Bongaerts, Stefan Evers, Karl-Heinz Maurer, Karl-Erich Jaeger
Optimization of protease secretion in Bacillus subtilis and Bacillus licheniformis by screening of homologous and heterologous signal peptides.
Appl Environ Microbiol: 2010, 76(19);6370-6
[PubMed:20709850] [WorldCat.org] [DOI] (I p)

Jiayun Qiao, Zhenghua Rao, Bing Dong, Yunhe Cao
Expression of Bacillus subtilis MA139 beta-mannanase in Pichia pastoris and the enzyme characterization.
Appl Biochem Biotechnol: 2010, 160(5);1362-70
[PubMed:19504356] [WorldCat.org] [DOI] (I p)

Louise E Tailford, Valerie M-A Ducros, James E Flint, Shirley M Roberts, Carl Morland, David L Zechel, Nicola Smith, Mads E Bjørnvad, Torben V Borchert, Keith S Wilson, Gideon J Davies, Harry J Gilbert
Understanding how diverse beta-mannanases recognize heterogeneous substrates.
Biochemistry: 2009, 48(29);7009-18
[PubMed:19441796] [WorldCat.org] [DOI] (I p)

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)

Yoshito Sadaie, Hisashi Nakadate, Reiko Fukui, Lii Mien Yee, Kei Asai
Glucomannan utilization operon of Bacillus subtilis.
FEMS Microbiol Lett: 2008, 279(1);103-9
[PubMed:18177310] [WorldCat.org] [DOI] (P p)