CitB
- Description: trigger enzyme: aconitase and RNA binding protein
| Gene name | citB |
| Synonyms | |
| Essential | no |
| Product | trigger enzyme: aconitate hydratase (aconitase) |
| Function | TCA cycle |
| Metabolic function and regulation of this protein in SubtiPathways: Central C-metabolism | |
| MW, pI | 99 kDa, 4.903 |
| Gene length, protein length | 2727 bp, 909 aa |
| Immediate neighbours | sspO, yneN |
| Get the DNA and protein sequences (Barbe et al., 2009) | |
Genetic context 
This image was kindly provided by SubtiList
| |
Contents
The gene
Basic information
- Locus tag: BSU18000
Phenotypes of a mutant
glutamate auxotrophy and a defect in sporulation PubMed
Database entries
- DBTBS entry: [1]
- SubtiList entry: [2]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity: Citrate = isocitrate (according to Swiss-Prot)
- Binding to iron responsive elements (IRE RNA) in the absence of the FeS cluster PubMed
- Protein family:
- Paralogous protein(s):
Extended information on the protein
- Kinetic information:
- Domains:
- Modification:
- Cofactor(s): FeS cluster
- Effectors of protein activity:
- Interactions:
- Localization:
Database entries
- Structure: 1L5J (E. coli)
- UniProt: P09339
- KEGG entry: [3]
- E.C. number: 4.2.1.3
Additional information
B. subtilis aconitase is both an enzyme and an RNA binding protein PubMed
Expression and regulation
- Regulation:
- repressed during growth in the presence of branched chain amino acids (CodY) PubMed
- repressed in the presence of glucose and glutamate (CcpC) PubMed
- expressed upon transition into the stationary phase (AbrB) PubMed
- repressed by glucose (3.7-fold) (CcpA) PubMed
- repression by glucose + arginine (CcpC) PubMed
- less expressed under conditions of extreme iron limitation (FsrA) PubMed
- Regulatory mechanism:
- Additional information:
Biological materials
- Mutant: GP683 (erm), available in Stülke lab
- Expression vector:
- GFP fusion:
- two-hybrid system: B. pertussis adenylate cyclase-based bacterial two hybrid system (BACTH), available in Stülke lab
- Antibody: available in Linc Sonenshein lab
Labs working on this gene/protein
Linc Sonenshein, Tufts University, Boston, MA, USA Homepage
Jörg Stülke, University of Göttingen, Germany Homepage
Your additional remarks
References
Reviews
Karl Volz
The functional duality of iron regulatory protein 1.
Curr Opin Struct Biol: 2008, 18(1);106-11
[PubMed:18261896]
[WorldCat.org]
[DOI]
(P p)
Fabian M Commichau, Jörg Stülke
Trigger enzymes: bifunctional proteins active in metabolism and in controlling gene expression.
Mol Microbiol: 2008, 67(4);692-702
[PubMed:18086213]
[WorldCat.org]
[DOI]
(P p)
Patricia J Kiley, Helmut Beinert
The role of Fe-S proteins in sensing and regulation in bacteria.
Curr Opin Microbiol: 2003, 6(2);181-5
[PubMed:12732309]
[WorldCat.org]
[DOI]
(P p)
R L Switzer
Non-redox roles for iron-sulfur clusters in enzymes.
Biofactors: 1989, 2(2);77-86
[PubMed:2696478]
[WorldCat.org]
(P p)
Original publications
Ahmed Gaballa, Haike Antelmann, Claudio Aguilar, Sukhjit K Khakh, Kyung-Bok Song, Gregory T Smaldone, John D Helmann
The Bacillus subtilis iron-sparing response is mediated by a Fur-regulated small RNA and three small, basic proteins.
Proc Natl Acad Sci U S A: 2008, 105(33);11927-32
[PubMed:18697947]
[WorldCat.org]
[DOI]
(I p)
Alisa W Serio, Kieran B Pechter, Abraham L Sonenshein
Bacillus subtilis aconitase is required for efficient late-sporulation gene expression.
J Bacteriol: 2006, 188(17);6396-405
[PubMed:16923907]
[WorldCat.org]
[DOI]
(P p)
Hans-Matti Blencke, Irene Reif, Fabian M Commichau, Christian Detsch, Ingrid Wacker, Holger Ludwig, Jörg Stülke
Regulation of citB expression in Bacillus subtilis: integration of multiple metabolic signals in the citrate pool and by the general nitrogen regulatory system.
Arch Microbiol: 2006, 185(2);136-46
[PubMed:16395550]
[WorldCat.org]
[DOI]
(P p)
Hans-Matti Blencke, Georg Homuth, Holger Ludwig, Ulrike Mäder, Michael Hecker, Jörg Stülke
Transcriptional profiling of gene expression in response to glucose in Bacillus subtilis: regulation of the central metabolic pathways.
Metab Eng: 2003, 5(2);133-49
[PubMed:12850135]
[WorldCat.org]
[DOI]
(P p)
Hyun-Jin Kim, Sam-In Kim, Manoja Ratnayake-Lecamwasam, Kiyoshi Tachikawa, Abraham L Sonenshein, Mark Strauch
Complex regulation of the Bacillus subtilis aconitase gene.
J Bacteriol: 2003, 185(5);1672-80
[PubMed:12591885]
[WorldCat.org]
[DOI]
(P p)
C Jourlin-Castelli, N Mani, M M Nakano, A L Sonenshein
CcpC, a novel regulator of the LysR family required for glucose repression of the citB gene in Bacillus subtilis.
J Mol Biol: 2000, 295(4);865-78
[PubMed:10656796]
[WorldCat.org]
[DOI]
(P p)
C Alén, A L Sonenshein
Bacillus subtilis aconitase is an RNA-binding protein.
Proc Natl Acad Sci U S A: 1999, 96(18);10412-7
[PubMed:10468622]
[WorldCat.org]
[DOI]
(P p)
M M Nakano, P Zuber, A L Sonenshein
Anaerobic regulation of Bacillus subtilis Krebs cycle genes.
J Bacteriol: 1998, 180(13);3304-11
[PubMed:9642180]
[WorldCat.org]
[DOI]
(P p)
J E Craig, M J Ford, D C Blaydon, A L Sonenshein
A null mutation in the Bacillus subtilis aconitase gene causes a block in Spo0A-phosphate-dependent gene expression.
J Bacteriol: 1997, 179(23);7351-9
[PubMed:9393699]
[WorldCat.org]
[DOI]
(P p)
A Fouet, S F Jin, G Raffel, A L Sonenshein
Multiple regulatory sites in the Bacillus subtilis citB promoter region.
J Bacteriol: 1990, 172(9);5408-15
[PubMed:2118511]
[WorldCat.org]
[DOI]
(P p)
A Fouet, A L Sonenshein
A target for carbon source-dependent negative regulation of the citB promoter of Bacillus subtilis.
J Bacteriol: 1990, 172(2);835-44
[PubMed:2105305]
[WorldCat.org]
[DOI]
(P p)
M S Rosenkrantz, D W Dingman, A L Sonenshein
Bacillus subtilis citB gene is regulated synergistically by glucose and glutamine.
J Bacteriol: 1985, 164(1);155-64
[PubMed:2413006]
[WorldCat.org]
[DOI]
(P p)
S H Fisher, B Magasanik
2-Ketoglutarate and the regulation of aconitase and histidase formation in Bacillus subtilis.
J Bacteriol: 1984, 158(1);379-82
[PubMed:6143742]
[WorldCat.org]
[DOI]
(P p)
