Difference between revisions of "BglS"
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− | * '''Mutant:''' | + | * '''Mutant:''' GP427 (licT-bglS, erm), available in the [[Stülke]] lab |
* '''Expression vector:''' | * '''Expression vector:''' |
Revision as of 17:41, 30 September 2009
- Description: endo-beta-1,3-1,4 glucanase
Gene name | bglS |
Synonyms | bgl, licS |
Essential | no |
Product | endo-beta-1,3-1,4 glucanase |
Function | lichenan degradation |
Metabolic function and regulation of this protein in SubtiPathways: Sugar catabolism | |
MW, pI | 27 kDa, 6.482 |
Gene length, protein length | 726 bp, 242 aa |
Immediate neighbours | citH, licT |
Get the DNA and protein sequences (Barbe et al., 2009) | |
Genetic context This image was kindly provided by SubtiList
|
Contents
The gene
Basic information
- Locus tag: BSU39070
Phenotypes of a mutant
Database entries
- DBTBS entry: [1]
- SubtiList entry: [2]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity: Hydrolysis of (1->4)-beta-D-glucosidic linkages in beta-D-glucans containing (1->3)- and (1->4)-bonds (according to Swiss-Prot)
- Protein family: glycosyl hydrolase 16 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:
- UniProt: P04957
- KEGG entry: [3]
- E.C. number: 3.2.1.73 3
Additional information
Expression and regulation
- Regulation: repressed by glucose (3.1-fold) (CcpA) PubMed1 PubMed2, expressed in the stationary phase (temporal activation), weak induction by ß-glucosides (LicT) PubMed
- Regulatory mechanism:
- Additional information:
Biological materials
- Mutant: GP427 (licT-bglS, erm), available in the Stülke lab
- Expression vector:
- lacZ fusion:
- GFP fusion:
- two-hybrid system:
- Antibody:
Labs working on this gene/protein
Your additional remarks
References
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)
Hans-Matti Blencke, Georg Homuth, Holger Ludwig, Ulrike Mäder, Michael Hecker, Jörg Stülke
Transcriptional profiling of gene expression in response to glucose in Bacillus subtilis: regulation of the central metabolic pathways.
Metab Eng: 2003, 5(2);133-49
[PubMed:12850135]
[WorldCat.org]
[DOI]
(P p)
K Schnetz, J Stülke, S Gertz, S Krüger, M Krieg, M Hecker, B Rak
LicT, a Bacillus subtilis transcriptional antiterminator protein of the BglG family.
J Bacteriol: 1996, 178(7);1971-9
[PubMed:8606172]
[WorldCat.org]
[DOI]
(P p)
S Krüger, J Stülke, M Hecker
Catabolite repression of beta-glucanase synthesis in Bacillus subtilis.
J Gen Microbiol: 1993, 139(9);2047-54
[PubMed:8245831]
[WorldCat.org]
[DOI]
(P p)
J Stülke, R Hanschke, M Hecker
Temporal activation of beta-glucanase synthesis in Bacillus subtilis is mediated by the GTP pool.
J Gen Microbiol: 1993, 139(9);2041-5
[PubMed:8245830]
[WorldCat.org]
[DOI]
(P p)
N Murphy, D J McConnell, B A Cantwell
The DNA sequence of the gene and genetic control sites for the excreted B. subtilis enzyme beta-glucanase.
Nucleic Acids Res: 1984, 12(13);5355-67
[PubMed:6087283]
[WorldCat.org]
[DOI]
(P p)