Difference between revisions of "CitB"

From SubtiWiki
Jump to: navigation, search
(Expression and regulation)
(Expression and regulation)
Line 118: Line 118:
 
** repressed during growth in the presence of branched chain amino acids ([[CodY]]) [http://www.ncbi.nlm.nih.gov/sites/entrez/12591885 PubMed]
 
** repressed during growth in the presence of branched chain amino acids ([[CodY]]) [http://www.ncbi.nlm.nih.gov/sites/entrez/12591885 PubMed]
 
** repressed in the presence of glucose and glutamate ([[CcpC]]) [http://www.ncbi.nlm.nih.gov/sites/entrez/10656796 PubMed]
 
** repressed in the presence of glucose and glutamate ([[CcpC]]) [http://www.ncbi.nlm.nih.gov/sites/entrez/10656796 PubMed]
** expressed upon transition into the stationary phase ([[AbrB]]) [http://www.ncbi.nlm.nih.gov/sites/entrez/12591885 PubMed], probably indirect negative regulation by [[AbrB]] {{PubMed|20817675}}
+
** expressed upon transition into the stationary phase ([[AbrB]]) [http://www.ncbi.nlm.nih.gov/sites/entrez/12591885 PubMed], indirect negative regulation by [[AbrB]] {{PubMed|20817675}}
 
** repressed by glucose (3.7-fold) ([[CcpA]]) [http://www.ncbi.nlm.nih.gov/pubmed/12850135 PubMed]
 
** repressed by glucose (3.7-fold) ([[CcpA]]) [http://www.ncbi.nlm.nih.gov/pubmed/12850135 PubMed]
 
** repression by glucose + arginine ([[CcpC]]) [http://www.ncbi.nlm.nih.gov/sites/entrez/16395550 PubMed]
 
** repression by glucose + arginine ([[CcpC]]) [http://www.ncbi.nlm.nih.gov/sites/entrez/16395550 PubMed]

Revision as of 17:12, 30 May 2011

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
CitB context.gif
This image was kindly provided by SubtiList







Categories containing this gene/protein

carbon core metabolism, trigger enzyme, RNA binding regulators

This gene is a member of the following regulons

AbrB regulon, CcpC regulon, CodY regulon, FsrA regulon

The CitB regulon: feuA-feuB-feuC-ybbA

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:
  • Localization:

Database entries

  • Structure: 1L5J (E. coli)
  • KEGG entry: [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
  • Additional information:

Biological materials

  • Mutant: GP683 (erm), available in Stülke lab
  • Expression vector:
  • lacZ fusion: pGP700 (in pAC5), available in Stülke lab
  • GFP fusion:
  • two-hybrid system: B. pertussis adenylate cyclase-based bacterial two hybrid system (BACTH), available in Stülke 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