Difference between revisions of "CitB"

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|colspan="2" style="background:#FAF8CC;" align="center"| '''Interactions involving this protein in [http://subtiwiki.uni-goettingen.de/interact/ ''Subt''Interact]''': [http://subtiwiki.uni-goettingen.de/interact/index.php?protein=CitB CitB]
 
|colspan="2" style="background:#FAF8CC;" align="center"| '''Interactions involving this protein in [http://subtiwiki.uni-goettingen.de/interact/ ''Subt''Interact]''': [http://subtiwiki.uni-goettingen.de/interact/index.php?protein=CitB CitB]
 
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|colspan="2" style="background:#FAF8CC;" align="center"| '''Metabolic function and regulation of this protein in [[SubtiPathways|''Subti''Pathways]]: <br/>[http://subtiwiki.uni-goettingen.de/pathways/carbon_flow.html Central C-metabolism]'''
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|colspan="2" style="background:#FAF8CC;" align="center"| '''Metabolic function and regulation of this protein in [[SubtiPathways|''Subti''Pathways]]: <br/>[http://subtiwiki.uni-goettingen.de/subtipathways/search.php?enzyme=citB citB]'''
 
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|style="background:#ABCDEF;" align="center"| '''MW, pI''' || 99 kDa, 4.903   
 
|style="background:#ABCDEF;" align="center"| '''MW, pI''' || 99 kDa, 4.903   

Revision as of 10:53, 7 January 2014

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
CitB context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
CitB expression.png















Categories containing this gene/protein

carbon core metabolism, trigger enzyme, RNA binding regulators

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

  • 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:
  • Domains:
  • Modification:
  • Cofactor(s): FeS cluster
  • Effectors of protein activity:

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
    • part of the iron sparing response (FsrA) PubMed
  • Additional information:

Biological materials

  • 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
  • two-hybrid system: B. pertussis adenylate cyclase-based bacterial two hybrid system (BACTH), available in Jörg Stülke's lab

Labs working on this gene/protein

Your additional remarks

References

Reviews

Original publications