GmuG

• 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 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

Database entries

• DBTBS entry: [1]

• SubtiList entry: [2]

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:

• Interactions:

• Localization:
  • extracellular (signal peptide) PubMed

Database entries

• Structure: 2QHA, 3CBW mutant variant

• UniProt: O05512

• KEGG entry: [3]

• E.C. number: 3.2.1.78

Expression and regulation

• Operon: gmuB-gmuA-gmuC-gmuD-gmuR-gmuE-gmuF-gmuG PubMed

• Sigma factor: SigA PubMed

• Regulation:
  • induced by conjac glucomannan (requires GmuG) (GmuR) PubMed
  • induced by cellobiose (GmuR) PubMed
  • subject to carbon catabolite repression (CcpA) PubMed

• Regulatory mechanism:
  • GmuR: transcription repression PubMed
  • CcpA: transcription repression PubMed
  • AbrB: transcription activation PubMed

• Additional information:

Biological materials

• Mutant:

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

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)