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: ansB | |
| MW, pI | 52 kDa, 5.69 |
| Gene length, protein length | 1425 bp, 475 aa |
| Immediate neighbours | mleN, ansA |
| Sequences | Protein DNA DNA_with_flanks |
Genetic context 
This image was kindly provided by SubtiList
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Expression at a glance PubMed
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Contents
Categories containing this gene/protein
utilization of amino acids, membrane proteins
This gene is a member of the following regulons
The gene
Basic information
- Locus tag: BSU23570
Phenotypes of a mutant
Database entries
- BsubCyc: BSU23570
- DBTBS entry: [1]
- SubtiList entry: [2]
Additional information
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:
- Localization: cell membrane (according to Swiss-Prot)
Database entries
- BsubCyc: BSU23570
- UniProt: P26899
- KEGG entry: [3]
- E.C. number: 4.3.1.1
Additional information
Expression and regulation
- Additional information:
- number of protein molecules per cell (minimal medium with glucose and ammonium, late stationary phase after glucose exhaustion): 35 PubMed
Biological materials
- Mutant: GP1153 (del ansAB::ermC) available in the Stülke lab
- Expression vector:
- lacZ fusion:
- GFP fusion:
- two-hybrid system:
- Antibody:
Labs working on this gene/protein
Your additional remarks
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)
