Difference between revisions of "XynC"

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|style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[ynfE]]'', ''[[xynD]]''
 
|style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[ynfE]]'', ''[[xynD]]''
 
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|style="background:#FAF8CC;" align="center"|'''Sequences'''||[http://bsubcyc.org/BSUB/sequence-aa?type=GENE&object=BSU18150 Protein] [http://bsubcyc.org/BSUB/sequence?type=GENE&object=BSU18150 DNA] [http://bsubcyc.org/BSUB/seq-selector?chromosome=CHROM-1&object=BSU18150 Advanced_DNA]
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|style="background:#FAF8CC;" align="center"|'''Sequences'''||[http://bsubcyc.org/BSUB/sequence-aa?type=GENE&object=BSU18150 Protein] [http://bsubcyc.org/BSUB/sequence?type=GENE&object=BSU18150 DNA] [http://bsubcyc.org/BSUB/seq-selector?chromosome=CHROM-1&object=BSU18150 DNA_with_flanks]
 
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|colspan="2" | '''Genetic context''' <br/> [[Image:ynfF_context.gif]]
 
|colspan="2" | '''Genetic context''' <br/> [[Image:ynfF_context.gif]]
 
  <div align="right"> <small>This image was kindly provided by [http://genolist.pasteur.fr/SubtiList/ SubtiList]</small></div>
 
  <div align="right"> <small>This image was kindly provided by [http://genolist.pasteur.fr/SubtiList/ SubtiList]</small></div>
 
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|-
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|colspan="2" |'''[http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=xynC_1942714_1943982_-1 Expression at a glance]'''&#160;&#160;&#160;{{PubMed|22383849}}<br/>[[Image:xynC_expression.png|500px]]
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|colspan="2" |'''[http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=xynC_1942714_1943982_-1 Expression at a glance]'''&#160;&#160;&#160;{{PubMed|22383849}}<br/>[[Image:xynC_expression.png|500px|link=http://subtiwiki.uni-goettingen.de/apps/expression/expression.php?search=BSU18150]]
 
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=== Database entries ===
 
=== Database entries ===
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* '''BsubCyc:''' [http://bsubcyc.org/BSUB/NEW-IMAGE?type=NIL&object=BSU18150&redirect=T BSU18150]
  
 
* '''DBTBS entry:''' no entry
 
* '''DBTBS entry:''' no entry
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=== Database entries ===
 
=== Database entries ===
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* '''BsubCyc:''' [http://bsubcyc.org/BSUB/NEW-IMAGE?type=NIL&object=BSU18150&redirect=T BSU18150]
  
 
* '''Structure:''' [http://www.rcsb.org/pdb/cgi/explore.cgi?pdbId=3GTN 3GTN] {{PubMed|19407387,21256135}}
 
* '''Structure:''' [http://www.rcsb.org/pdb/cgi/explore.cgi?pdbId=3GTN 3GTN] {{PubMed|19407387,21256135}}
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* '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=xynC_1942714_1943982_-1 xynC] {{PubMed|22383849}}
 
* '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=xynC_1942714_1943982_-1 xynC] {{PubMed|22383849}}
  
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* '''Sigma factor:'''  
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* '''[[Sigma factor]]:'''  
  
 
* '''Regulation:'''  
 
* '''Regulation:'''  
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<pubmed>20735481 </pubmed>
 
<pubmed>20735481 </pubmed>
 
==Original publications==
 
==Original publications==
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'''Additional publications:''' {{PubMed|20817675,21256135}}
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<pubmed>19407387, 18957862, 17028274 20817675,21256135 24271172 </pubmed>
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<pubmed>19407387, 18957862, 17028274 </pubmed>
 
  
 
[[Category:Protein-coding genes]]
 
[[Category:Protein-coding genes]]

Latest revision as of 13:51, 2 April 2014

  • Description: endo-xylanase, preference for methylglucurono-xylan

Gene name xynC
Synonyms ynfF
Essential no
Product endo-xylanase
Function xylan degradation
Gene expression levels in SubtiExpress: xynC
MW, pI 47 kDa, 9.078
Gene length, protein length 1266 bp, 422 aa
Immediate neighbours ynfE, xynD
Sequences Protein DNA DNA_with_flanks
Genetic context
YnfF context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
XynC expression.png















Categories containing this gene/protein

utilization of specific carbon sources

This gene is a member of the following regulons

AbrB regulon

The gene

Basic information

  • Locus tag: BSU18150

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 (1->4)-beta-D-xylosyl links in some glucuronoarabinoxylans (according to Swiss-Prot)
  • Protein family: glycosyl hydrolase 30 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

  • KEGG entry: [2]

Additional information

Expression and regulation

  • 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

Reviews

Massimiliano Marvasi, Pieter T Visscher, Lilliam Casillas Martinez
Exopolymeric substances (EPS) from Bacillus subtilis: polymers and genes encoding their synthesis.
FEMS Microbiol Lett: 2010, 313(1);1-9
[PubMed:20735481] [WorldCat.org] [DOI] (I p)

Original publications

Mun Su Rhee, Lusha Wei, Neha Sawhney, John D Rice, Franz J St John, Jason C Hurlbert, James F Preston
Engineering the xylan utilization system in Bacillus subtilis for production of acidic Xylooligosaccharides.
Appl Environ Microbiol: 2014, 80(3);917-27
[PubMed:24271172] [WorldCat.org] [DOI] (I p)

Franz J St John, Jason C Hurlbert, John D Rice, James F Preston, Edwin Pozharski
Ligand bound structures of a glycosyl hydrolase family 30 glucuronoxylan xylanohydrolase.
J Mol Biol: 2011, 407(1);92-109
[PubMed:21256135] [WorldCat.org] [DOI] (I p)

Onuma Chumsakul, Hiroki Takahashi, Taku Oshima, Takahiro Hishimoto, Shigehiko Kanaya, Naotake Ogasawara, Shu Ishikawa
Genome-wide binding profiles of the Bacillus subtilis transition state regulator AbrB and its homolog Abh reveals their interactive role in transcriptional regulation.
Nucleic Acids Res: 2011, 39(2);414-28
[PubMed:20817675] [WorldCat.org] [DOI] (I p)

Franz J St John, David K Godwin, James F Preston, Edwin Pozharski, Jason C Hurlbert
Crystallization and crystallographic analysis of Bacillus subtilis xylanase C.
Acta Crystallogr Sect F Struct Biol Cryst Commun: 2009, 65(Pt 5);499-503
[PubMed:19407387] [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)

Franz J St John, John D Rice, James F Preston
Characterization of XynC from Bacillus subtilis subsp. subtilis strain 168 and analysis of its role in depolymerization of glucuronoxylan.
J Bacteriol: 2006, 188(24);8617-26
[PubMed:17028274] [WorldCat.org] [DOI] (P p)

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