Difference between revisions of "BglS"
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|style="background:#ABCDEF;" align="center"|'''Function''' || lichenan degradation | |style="background:#ABCDEF;" align="center"|'''Function''' || lichenan degradation | ||
|- | |- | ||
− | |colspan="2" style="background:#FAF8CC;" align="center"| '''Gene expression levels in [http:// | + | |colspan="2" style="background:#FAF8CC;" align="center"| '''Gene expression levels in [http://subtiwiki.uni-goettingen.de/apps/expression/ ''Subti''Express]''': [http://subtiwiki.uni-goettingen.de/apps/expression/expression.php?search=BSU39070 bglS] |
|- | |- | ||
|colspan="2" style="background:#FAF8CC;" align="center"| '''Metabolic function and regulation of this protein in [[SubtiPathways|''Subti''Pathways]]: <br/>[http://subtiwiki.uni-goettingen.de/pathways/carbohydrate_metabolic_pathways.html Sugar catabolism]''' | |colspan="2" style="background:#FAF8CC;" align="center"| '''Metabolic function and regulation of this protein in [[SubtiPathways|''Subti''Pathways]]: <br/>[http://subtiwiki.uni-goettingen.de/pathways/carbohydrate_metabolic_pathways.html Sugar catabolism]''' | ||
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|style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[citH]]'', ''[[licT]]'' | |style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[citH]]'', ''[[licT]]'' | ||
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− | | | + | |style="background:#FAF8CC;" align="center"|'''Sequences'''||[http://bsubcyc.org/BSUB/sequence-aa?type=GENE&object=BSU39070 Protein] [http://bsubcyc.org/BSUB/sequence?type=GENE&object=BSU39070 DNA] [http://bsubcyc.org/BSUB/seq-selector?chromosome=CHROM-1&object=BSU39070 Advanced_DNA] |
|- | |- | ||
|colspan="2" | '''Genetic context''' <br/> [[Image:bglS_context.gif]] | |colspan="2" | '''Genetic context''' <br/> [[Image:bglS_context.gif]] |
Revision as of 14:13, 13 May 2013
- 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 |
Gene expression levels in SubtiExpress: bglS | |
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 |
Sequences | Protein DNA Advanced_DNA |
Genetic context This image was kindly provided by SubtiList
| |
Expression at a glance PubMed |
Contents
Categories containing this gene/protein
utilization of specific carbon sources
This gene is a member of the following regulons
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:
- Localization: extracellular (signal peptide) PubMed
Database entries
- Structure: 3O5S
- UniProt: P04957
- KEGG entry: [3]
- E.C. number: 3.2.1.73
Additional information
Expression and regulation
- Regulation:
- Regulatory mechanism:
- CcpA: transcription repression PubMed
- LicT: binding to an RNA switch results in transcriptional antitermination PubMed
- Additional information:
Biological materials
- Mutant: GP427 (licT-bglS, erm), BGW7 (cat), both 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
Junio Cota, Leandro C Oliveira, André R L Damásio, Ana P Citadini, Zaira B Hoffmam, Thabata M Alvarez, Carla A Codima, Vitor B P Leite, Glaucia Pastore, Mario de Oliveira-Neto, Mario T Murakami, Roberto Ruller, Fabio M Squina
Assembling a xylanase-lichenase chimera through all-atom molecular dynamics simulations.
Biochim Biophys Acta: 2013, 1834(8);1492-500
[PubMed:23459129]
[WorldCat.org]
[DOI]
(P 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)
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)