AnsA

• Description: L-asparaginase
  
  

Gene name	ansA
Synonyms
Essential	no
Product	L-asparaginase
Function	asparagine degradation
Gene expression levels in SubtiExpress: ansA
Metabolic function and regulation of this protein in SubtiPathways: Asp, Asn
MW, pI	36 kDa, 4.455
Gene length, protein length	987 bp, 329 aa
Immediate neighbours	ansB, ansR
Get the DNA and protein sequences (Barbe et al., 2009)
Genetic context This image was kindly provided by SubtiList
Expression at a glance   PubMed

Categories containing this gene/protein

utilization of amino acids

This gene is a member of the following regulons

AnsR regulon

The gene

Basic information

• Locus tag: BSU23580

Database entries

• DBTBS entry: [1]

• SubtiList entry: [2]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity: L-asparagine + H₂O = L-aspartate + NH₃ (according to Swiss-Prot)

• Protein family: asparaginase 1 family (according to Swiss-Prot)

• Paralogous protein(s): AnsZ

Extended information on the protein

• Kinetic information:

• Domains:

• Modification:

• Cofactor(s):

• Effectors of protein activity:

• Interactions:

• Localization:

Database entries

• Structure:

• UniProt: P26900

• KEGG entry: [3]

• E.C. number: 3.5.1.1

Expression and regulation

• Operon:
  • ansA-ansB PubMed
  • ansA-ansB-mleN-mleA PubMed

• Expression browser: ansA PubMed

• Sigma factor: SigA PubMed

• Regulation:
  • expressed in the presence of asparagine (AnsR) PubMed

• Regulatory mechanism:
  • AnsR: transcription repression PubMed

• Additional information:

Biological materials

• Mutant: GP1153 (del ansAB::ermC) available in the Stülke lab

• Expression vector:

• lacZ fusion: pGP872 (in pAC5), available in Stülke lab

• GFP fusion:

• two-hybrid system:

• Antibody:

References

Pierre Nicolas, Ulrike Mäder, Etienne Dervyn, Tatiana Rochat, Aurélie Leduc, Nathalie Pigeonneau, Elena Bidnenko, Elodie Marchadier, Mark Hoebeke, Stéphane Aymerich, Dörte Becher, Paola Bisicchia, Eric Botella, Olivier Delumeau, Geoff Doherty, Emma L Denham, Mark J Fogg, Vincent Fromion, Anne Goelzer, Annette Hansen, Elisabeth Härtig, Colin R Harwood, Georg Homuth, Hanne Jarmer, Matthieu Jules, Edda Klipp, Ludovic Le Chat, François Lecointe, Peter Lewis, Wolfram Liebermeister, Anika March, Ruben A T Mars, Priyanka Nannapaneni, David Noone, Susanne Pohl, Bernd Rinn, Frank Rügheimer, Praveen K Sappa, Franck Samson, Marc Schaffer, Benno Schwikowski, Leif Steil, Jörg Stülke, Thomas Wiegert, Kevin M Devine, Anthony J Wilkinson, Jan Maarten van Dijl, Michael Hecker, Uwe Völker, Philippe Bessières, Philippe Noirot
Condition-dependent transcriptome reveals high-level regulatory architecture in Bacillus subtilis.
Science: 2012, 335(6072);1103-6
[PubMed:22383849] [WorldCat.org] [DOI] (I p)

Susan H Fisher, Lewis V Wray
Bacillus subtilis 168 contains two differentially regulated genes encoding L-asparaginase.
J Bacteriol: 2002, 184(8);2148-54
[PubMed:11914346] [WorldCat.org] [DOI] (P p)

D Sun, P Setlow
Cloning and nucleotide sequence of the Bacillus subtilis ansR gene, which encodes a repressor of the ans operon coding for L-asparaginase and L-aspartase.
J Bacteriol: 1993, 175(9);2501-6
[PubMed:8478318] [WorldCat.org] [DOI] (P p)

D X Sun, P Setlow
Cloning, nucleotide sequence, and expression of the Bacillus subtilis ans operon, which codes for L-asparaginase and L-aspartase.
J Bacteriol: 1991, 173(12);3831-45
[PubMed:1711029] [WorldCat.org] [DOI] (P p)