AnsB

• Description: L-aspartase
  
  

Gene name	ansB
Synonyms
Essential	no
Product	L-aspartase
Function	aspartate degradation
Gene expression levels in SubtiExpress: ansB
Metabolic function and regulation of this protein in SubtiPathways: Asp, Asn
MW, pI	52 kDa, 5.69
Gene length, protein length	1425 bp, 475 aa
Immediate neighbours	mleN, ansA
Sequences	Protein DNA Advanced_DNA
Genetic context This image was kindly provided by SubtiList
Expression at a glance   PubMed

Categories containing this gene/protein

utilization of amino acids, membrane proteins

This gene is a member of the following regulons

AnsR regulon

The gene

Basic information

• Locus tag: BSU23570

Database entries

• DBTBS entry: [1]

• SubtiList entry: [2]

The protein

Basic information/ Evolution

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

• Protein family: Aspartase subfamily (according to Swiss-Prot)

• Paralogous protein(s): CitG

Extended information on the protein

• Kinetic information:

• Domains:

• Modification:

• Cofactor(s):

• Effectors of protein activity:

• Interactions:

• Localization: cell membrane (according to Swiss-Prot)

Database entries

• Structure: 3R6Q (from Bacillus sp. YM55-1, 72% identity, 92% similarity) PubMed

• UniProt: P26899

• KEGG entry: [3]

• E.C. number: 4.3.1.1

Expression and regulation

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

• Expression browser: ansB 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:

• GFP fusion:

• two-hybrid system:

• Antibody:

References

Additional publications: PubMed

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)

Lope A Flórez, Katrin Gunka, Rafael Polanía, Stefan Tholen, Jörg Stülke
SPABBATS: A pathway-discovery method based on Boolean satisfiability that facilitates the characterization of suppressor mutants.
BMC Syst Biol: 2011, 5;5
[PubMed:21219666] [WorldCat.org] [DOI] (I e)

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)