Difference between revisions of "CitB"
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** number of protein molecules per cell (minimal medium with glucose and ammonium): 5049 {{PubMed|24696501}} | ** number of protein molecules per cell (minimal medium with glucose and ammonium): 5049 {{PubMed|24696501}} | ||
** number of protein molecules per cell (complex medium with amino acids, without glucose): 24371 {{PubMed|24696501}} | ** number of protein molecules per cell (complex medium with amino acids, without glucose): 24371 {{PubMed|24696501}} | ||
+ | ** number of protein molecules per cell (minimal medium with glucose and ammonium, exponential phase): 5745 {{PubMed|21395229}} | ||
+ | ** number of protein molecules per cell (minimal medium with glucose and ammonium, early stationary phase after glucose exhaustion): 3428 {{PubMed|21395229}} | ||
+ | ** number of protein molecules per cell (minimal medium with glucose and ammonium, late stationary phase after glucose exhaustion): 5655 {{PubMed|21395229}} | ||
=Biological materials = | =Biological materials = | ||
− | |||
* '''Mutant:''' | * '''Mutant:''' | ||
** GP1275 (erm), available in [[Jörg Stülke]]'s lab | ** GP1275 (erm), available in [[Jörg Stülke]]'s lab |
Revision as of 14:04, 17 April 2014
- Description: trigger enzyme: aconitase and RNA binding protein
Gene name | citB |
Synonyms | |
Essential | no |
Product | trigger enzyme: aconitate hydratase (aconitase) |
Function | TCA cycle |
Gene expression levels in SubtiExpress: citB | |
Interactions involving this protein in SubtInteract: CitB | |
Metabolic function and regulation of this protein in SubtiPathways: citB | |
MW, pI | 99 kDa, 4.903 |
Gene length, protein length | 2727 bp, 909 aa |
Immediate neighbours | sspO, yneN |
Sequences | Protein DNA DNA_with_flanks |
Genetic context This image was kindly provided by SubtiList
| |
Expression at a glance PubMed |
Contents
Categories containing this gene/protein
carbon core metabolism, trigger enzyme, RNA binding regulators, most abundant proteins
This gene is a member of the following regulons
CcpA regulon, CcpC regulon, CodY regulon, FsrA regulon
The CitB regulon: feuA-feuB-feuC-ybbA, citZ
The gene
Basic information
- Locus tag: BSU18000
Phenotypes of a mutant
- glutamate auxotrophy and a defect in sporulation PubMed
Database entries
- BsubCyc: BSU18000
- DBTBS entry: [1]
- SubtiList entry: [2]
Additional information
- A mutation was found in this gene after evolution under relaxed selection for sporulation PubMed
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity:
- Citrate <=> isocitrate
- 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:
- Modification:
- Cofactors: FeS cluster
- Effectors of protein activity:
Database entries
- BsubCyc: BSU18000
- 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 (moonlighting protein) PubMed
- extensive information on the structure and enzymatic properties of CitB can be found at Proteopedia
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, indirect negative regulation by 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
- part of the iron sparing response (FsrA) PubMed
- Regulatory mechanism:
- Additional information:
- belongs to the 100 most abundant proteins PubMed
- number of protein molecules per cell (minimal medium with glucose and ammonium): 5049 PubMed
- number of protein molecules per cell (complex medium with amino acids, without glucose): 24371 PubMed
- number of protein molecules per cell (minimal medium with glucose and ammonium, exponential phase): 5745 PubMed
- number of protein molecules per cell (minimal medium with glucose and ammonium, early stationary phase after glucose exhaustion): 3428 PubMed
- number of protein molecules per cell (minimal medium with glucose and ammonium, late stationary phase after glucose exhaustion): 5655 PubMed
Biological materials
- Mutant:
- GP1275 (erm), available in Jörg Stülke's lab
- GP1441 (spc), available in Jörg Stülke's lab
- 1A999 ( citB::spec), PubMed, available at BGSC
- Expression vector:
- GP1439 (citB-Strep (spc)), purification from B. subtilis, for SPINE, available in Jörg Stülke's lab
- pGP1810 (for expression, purification in E. coli with N-terminal Strep-tag, in pGP172, available in Jörg Stülke's lab
- lacZ fusion:
- pGP700 (in pAC5), available in Jörg Stülke's lab
- GFP fusion: GP1434 (spc, based on pGP1870), available in Jörg Stülke's lab
- two-hybrid system: B. pertussis adenylate cyclase-based bacterial two hybrid system (BACTH), available in Jörg Stülke's lab
- Antibody: available in Linc Sonenshein's lab
- FLAG-tag construct:
- GP1144 (spc, based on pGP1331), available in Jörg Stülke's lab
- GP1145 (kan), available in Jörg Stülke's 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