Difference between revisions of "BglC"
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=== Database entries === | === Database entries === | ||
− | * '''Structure:''' [http://www.rcsb.org/pdb/explore.do?structureId= | + | * '''Structure:''' [http://www.rcsb.org/pdb/explore.do?structureId=3PZT 3PZT] {{PubMed|21880019}} |
* '''UniProt:''' [http://www.uniprot.org/uniprot/P10475 P10475] | * '''UniProt:''' [http://www.uniprot.org/uniprot/P10475 P10475] | ||
Line 128: | Line 128: | ||
=References= | =References= | ||
− | <pubmed>18957862,3024130 | + | <pubmed>18957862,3024130 21880019 3106328 </pubmed> |
[[Category:Protein-coding genes]] | [[Category:Protein-coding genes]] |
Revision as of 12:22, 27 December 2011
- Description: endo-1,4-beta-glucanase
Gene name | bglC |
Synonyms | eglS |
Essential | no |
Product | endo-1,4-beta-glucanase) |
Function | beta-1,4-glucan degradation |
MW, pI | 55 kDa, 8.619 |
Gene length, protein length | 1497 bp, 499 aa |
Immediate neighbours | alsT, ynfE |
Get the DNA and protein sequences (Barbe et al., 2009) | |
Genetic context This image was kindly provided by SubtiList
|
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: BSU18130
Phenotypes of a mutant
Database entries
- DBTBS entry: [1]
- SubtiList entry: [2]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity: Endohydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans (according to Swiss-Prot)
- Protein family: glycosyl hydrolase 5 (cellulase A) 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
- UniProt: P10475
- KEGG entry: [3]
- E.C. number: 3.2.1.4
Additional information
Expression and regulation
- Operon: bglC (according to DBTBS)
- Regulation:
- Regulatory mechanism:
- 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
Camila R Santos, Joice H Paiva, Maurício L Sforça, Jorge L Neves, Rodrigo Z Navarro, Júnio Cota, Patrícia K Akao, Zaira B Hoffmam, Andréia N Meza, Juliana H Smetana, Maria L Nogueira, Igor Polikarpov, José Xavier-Neto, Fábio M Squina, Richard J Ward, Roberto Ruller, Ana C Zeri, Mário T Murakami
Dissecting structure-function-stability relationships of a thermostable GH5-CBM3 cellulase from Bacillus subtilis 168.
Biochem J: 2012, 441(1);95-104
[PubMed:21880019]
[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)
L M Robson, G H Chambliss
Endo-beta-1,4-glucanase gene of Bacillus subtilis DLG.
J Bacteriol: 1987, 169(5);2017-25
[PubMed:3106328]
[WorldCat.org]
[DOI]
(P p)
R M MacKay, A Lo, G Willick, M Zuker, S Baird, M Dove, F Moranelli, V Seligy
Structure of a Bacillus subtilis endo-beta-1,4-glucanase gene.
Nucleic Acids Res: 1986, 14(22);9159-70
[PubMed:3024130]
[WorldCat.org]
[DOI]
(P p)