Difference between revisions of "Csn"
| Line 14: | Line 14: | ||
|style="background:#ABCDEF;" align="center"|'''Function''' || chitin degradation | |style="background:#ABCDEF;" align="center"|'''Function''' || chitin 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=BSU26890 csn] |
|- | |- | ||
|style="background:#ABCDEF;" align="center"| '''MW, pI''' || 31 kDa, 8.892 | |style="background:#ABCDEF;" align="center"| '''MW, pI''' || 31 kDa, 8.892 | ||
| Line 22: | Line 22: | ||
|style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[yraM]]'', ''[[yraL]]'' | |style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[yraM]]'', ''[[yraL]]'' | ||
|- | |- | ||
| − | | | + | |style="background:#FAF8CC;" align="center"|'''Sequences'''||[http://bsubcyc.org/BSUB/sequence-aa?type=GENE&object=BSU26890 Protein] [http://bsubcyc.org/BSUB/sequence?type=GENE&object=BSU26890 DNA] [http://bsubcyc.org/BSUB/seq-selector?chromosome=CHROM-1&object=BSU26890 Advanced_DNA] |
|- | |- | ||
|colspan="2" | '''Genetic context''' <br/> [[Image:csn_context.gif]] | |colspan="2" | '''Genetic context''' <br/> [[Image:csn_context.gif]] | ||
Revision as of 13:25, 13 May 2013
- Description: chitosanase
| Gene name | csn |
| Synonyms | |
| Essential | no |
| Product | chitosanase |
| Function | chitin degradation |
| Gene expression levels in SubtiExpress: csn | |
| MW, pI | 31 kDa, 8.892 |
| Gene length, protein length | 831 bp, 277 aa |
| Immediate neighbours | yraM, yraL |
| 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: BSU26890
Phenotypes of a mutant
Database entries
- DBTBS entry: no entry
- SubtiList entry: [1]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity: Endohydrolysis of beta-(1->4)-linkages between D-glucosamine residues in a partly acetylated chitosan (according to Swiss-Prot)
- Protein family: glycosyl hydrolase 46 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), major constituent of the secretome PubMed
Database entries
- Structure:
- UniProt: O07921
- KEGG entry: [2]
- E.C. number: 3.2.1.132
Additional information
Expression and regulation
- Operon:
- Sigma factor:
- Regulation:
- 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
Additional publications: PubMed
Chulhong Oh, Mahanama De Zoysa, Do-Hyung Kang, Youngdeuk Lee, Ilson Whang, Chamilani Nikapitiya, Soo-Jin Heo, Kon-Tak Yoon, Abu Affan, Jehee Lee
Isolation, purification, and enzymatic characterization of extracellular chitosanase from marine bacterium Bacillus subtilis CH2.
J Microbiol Biotechnol: 2011, 21(10);1021-5
[PubMed:22031025]
[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)
Luis A Rivas, Vı Ctor Parro, Mercedes Moreno-Paz, Rafael P Mellado
The Bacillus subtilis 168 csn gene encodes a chitosanase with similar properties to a streptomyces enzyme.
Microbiology (Reading): 2000, 146 ( Pt 11);2929-2936
[PubMed:11065371]
[WorldCat.org]
[DOI]
(P p)
