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
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

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: secreted (according to Swiss-Prot), 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)