XynA

• Description: endo-1,4-beta-xylanase
  
  

Gene name	xynA
Synonyms
Essential	no
Product	endo-1,4-beta-xylanase
Function	xylan degradation
Gene expression levels in SubtiExpress: xynA
Metabolic function and regulation of this protein in SubtiPathways: Sugar catabolism
MW, pI	23 kDa, 9.644
Gene length, protein length	639 bp, 213 aa
Immediate neighbours	pps, yozV
Sequences	Protein DNA DNA_with_flanks
Genetic context This image was kindly provided by SubtiList
Expression at a glance   PubMed

Categories containing this gene/protein

utilization of specific carbon sources

The gene

Basic information

• Locus tag: BSU18840

Database entries

• DBTBS entry: [1]

• SubtiList entry: [2]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity: Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans (according to Swiss-Prot)

• Protein family:

• 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: 2QZ3 (complex with xylotetraose), 2Z79, 3EXU

• UniProt: P18429

• KEGG entry: [3]

• E.C. number: 3.2.1.8

Expression and regulation

• Operon: xynA PubMed

• Expression browser: xynA PubMed

• Sigma factor: SigA PubMed

• Regulation:
  • constitutively expressed PubMed

• Regulatory mechanism:

• Additional information:
  • A ncRNA is predicted between pps and xynA PubMed

Biological materials

• Mutant:

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

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)

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)

Veronika Szabó, Adél Muskotál, Balázs Tóth, Marko D Mihovilovic, Ferenc Vonderviszt
Construction of a xylanase A variant capable of polymerization.
PLoS One: 2011, 6(9);e25388
[PubMed:21966517] [WorldCat.org] [DOI] (I p)

Sven Cuyvers, Emmie Dornez, Maher Abou Hachem, Birte Svensson, Michael Hothorn, Joanne Chory, Jan A Delcour, Christophe M Courtin
Isothermal titration calorimetry and surface plasmon resonance allow quantifying substrate binding to different binding sites of Bacillus subtilis xylanase.
Anal Biochem: 2012, 420(1);90-2
[PubMed:21964501] [WorldCat.org] [DOI] (I p)

Davi Serradella Vieira, Richard John Ward
Conformation analysis of a surface loop that controls active site access in the GH11 xylanase A from Bacillus subtilis.
J Mol Model: 2012, 18(4);1473-9
[PubMed:21785938] [WorldCat.org] [DOI] (I p)

Sven Cuyvers, Jelle Hendrix, Emmie Dornez, Yves Engelborghs, Jan A Delcour, Christophe M Courtin
Both substrate hydrolysis and secondary substrate binding determine xylanase mobility as assessed by FRAP.
J Phys Chem B: 2011, 115(16);4810-7
[PubMed:21466172] [WorldCat.org] [DOI] (I p)

Irnov Irnov, Cynthia M Sharma, Jörg Vogel, Wade C Winkler
Identification of regulatory RNAs in Bacillus subtilis.
Nucleic Acids Res: 2010, 38(19);6637-51
[PubMed:20525796] [WorldCat.org] [DOI] (I p)

Louise E Rasmussen, Jens F Sørensen, Anne S Meyer
Kinetics and substrate selectivity of a Triticum aestivum xylanase inhibitor (TAXI) resistant D11F/R122D variant of Bacillus subtilis XynA xylanase.
J Biotechnol: 2010, 146(4);207-14
[PubMed:20188130] [WorldCat.org] [DOI] (I p)

Annick Pollet, Stijn Lagaert, Elena Eneyskaya, Anna Kulminskaya, Jan A Delcour, Christophe M Courtin
Mutagenesis and subsite mapping underpin the importance for substrate specificity of the aglycon subsites of glycoside hydrolase family 11 xylanases.
Biochim Biophys Acta: 2010, 1804(4);977-85
[PubMed:20096384] [WorldCat.org] [DOI] (P p)

Louise E Rasmussen, Anne S Meyer
Size exclusion chromatography for the quantitative profiling of the enzyme-catalyzed hydrolysis of Xylo-oligosaccharides.
J Agric Food Chem: 2010, 58(2);762-9
[PubMed:19994888] [WorldCat.org] [DOI] (I p)

Tim Beliën, Iris J Joye, Jan A Delcour, Christophe M Courtin
Computational design-based molecular engineering of the glycosyl hydrolase family 11 B. subtilis XynA endoxylanase improves its acid stability.
Protein Eng Des Sel: 2009, 22(10);587-96
[PubMed:19531602] [WorldCat.org] [DOI] (I p)

Annick Pollet, Elien Vandermarliere, Jeroen Lammertyn, Sergei V Strelkov, Jan A Delcour, Christophe M Courtin
Crystallographic and activity-based evidence for thumb flexibility and its relevance in glycoside hydrolase family 11 xylanases.
Proteins: 2009, 77(2);395-403
[PubMed:19422059] [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)

R Allmansberger
Degradation of the Bacillus subtilis xynA transcript is accelerated in response to stress.
Mol Gen Genet: 1996, 251(1);108-12
[PubMed:8628241] [WorldCat.org] [DOI] (P p)

C Lindner, J Stülke, M Hecker
Regulation of xylanolytic enzymes in Bacillus subtilis.
Microbiology (Reading): 1994, 140 ( Pt 4);753-7
[PubMed:8012596] [WorldCat.org] [DOI] (P p)