Difference between revisions of "BglH"

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=== Database entries ===
 
=== Database entries ===
 +
* '''BsubCyc:''' [http://bsubcyc.org/BSUB/NEW-IMAGE?type=NIL&object=BSU39260&redirect=T BSU39260]
  
 
* '''DBTBS entry:''' [http://dbtbs.hgc.jp/COG/prom/bglPH-yxiE.html]
 
* '''DBTBS entry:''' [http://dbtbs.hgc.jp/COG/prom/bglPH-yxiE.html]
Line 96: Line 97:
  
 
=== Database entries ===
 
=== Database entries ===
 +
* '''BsubCyc:''' [http://bsubcyc.org/BSUB/NEW-IMAGE?type=NIL&object=BSU39260&redirect=T BSU39260]
  
 
* '''Structure:'''
 
* '''Structure:'''

Revision as of 15:11, 2 April 2014

  • Description: phospho-beta-glucosidase

Gene name bglH
Synonyms
Essential no
Product phospho-beta-glucosidase
Function salicin utilization
Gene expression levels in SubtiExpress: bglH
Metabolic function and regulation of this protein in SubtiPathways:
bglH
MW, pI 53 kDa, 4.957
Gene length, protein length 1407 bp, 469 aa
Immediate neighbours yxiE, bglP
Sequences Protein DNA DNA_with_flanks
Genetic context
BglH context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
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Categories containing this gene/protein

utilization of specific carbon sources

This gene is a member of the following regulons

CcpA regulon, LicT regulon

The gene

Basic information

  • Locus tag: BSU39260

Phenotypes of a mutant

Database entries

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

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: 6-phospho-beta-D-glucosyl-(1,4)-D-glucose + H2O = D-glucose + D-glucose 6-phosphate (according to Swiss-Prot)
  • Protein family: glycosyl hydrolase 1 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

  • Structure:
  • KEGG entry: [3]

Additional information

Expression and regulation

  • Regulatory mechanism:
    • CcpA: transcription repression, (CcpA binding site overlaps -35 region) PubMed
    • LicT-dependent RNA switch (antitermination, lack of LicT-dependent antitermination in the presence of gucose due to the requirement of LicT to be phosphorylated by HPr PubMed
  • 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

Juliane Ollinger, Kyung-Bok Song, Haike Antelmann, Michael Hecker, John D Helmann
Role of the Fur regulon in iron transport in Bacillus subtilis.
J Bacteriol: 2006, 188(10);3664-73
[PubMed:16672620] [WorldCat.org] [DOI] (P p)

B Setlow, R-M Cabrera-Martinez, P Setlow
Mechanism of the hydrolysis of 4-methylumbelliferyl-beta-D-glucoside by germinating and outgrowing spores of Bacillus species.
J Appl Microbiol: 2004, 96(6);1245-55
[PubMed:15139916] [WorldCat.org] [DOI] (P p)

Barbara Setlow, Arturo Cabrera-Hernandez, Rosa Martha Cabrera-Martinez, Peter Setlow
Identification of aryl-phospho-beta-D-glucosidases in Bacillus subtilis.
Arch Microbiol: 2004, 181(1);60-7
[PubMed:14652714] [WorldCat.org] [DOI] (P p)

S Krüger, M Hecker
Regulation of the putative bglPH operon for aryl-beta-glucoside utilization in Bacillus subtilis.
J Bacteriol: 1995, 177(19);5590-7
[PubMed:7559347] [WorldCat.org] [DOI] (P p)

D Le Coq, C Lindner, S Krüger, M Steinmetz, J Stülke
New beta-glucoside (bgl) genes in Bacillus subtilis: the bglP gene product has both transport and regulatory functions similar to those of BglF, its Escherichia coli homolog.
J Bacteriol: 1995, 177(6);1527-35
[PubMed:7883710] [WorldCat.org] [DOI] (P p)