Difference between revisions of "Fur"

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* '''Effectors of protein activity:'''
 
* '''Effectors of protein activity:'''
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** DNA binding activity (repression) is triggered by binding of Fe(II) {{PubMed|23057863}}
  
 
* '''[[SubtInteract|Interactions]]:'''
 
* '''[[SubtInteract|Interactions]]:'''
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<pubmed> 12374814,12354229, 22389480 </pubmed>
 
<pubmed> 12374814,12354229, 22389480 </pubmed>
 
==Other original publications==
 
==Other original publications==
<pubmed>18487332,14563870,18697947,10400588,11790741,16672620,12207695,9701813,12029044,22427629,17725565,17012385,12950915,19508286 , 16672620, </pubmed>
+
<pubmed>18487332,14563870,18697947,10400588,11790741,16672620,12207695,9701813,12029044,22427629,17725565,17012385,12950915,19508286 , 16672620, 23057863</pubmed>
  
 
[http://www.ncbi.nlm.nih.gov/sites/entrez/PMID PubMed]
 
[http://www.ncbi.nlm.nih.gov/sites/entrez/PMID PubMed]
  
 
[[Category:Protein-coding genes]]
 
[[Category:Protein-coding genes]]

Revision as of 19:11, 14 October 2012

  • Description: transcription regulator of iron homoeostasis

Gene name fur
Synonyms yqkL
Essential no
Product transcriptional repressor Fur family
Function regulation of iron homoeostasis

and transcription of ferri-siderophore uptake genes

Gene expression levels in SubtiExpress: fur

and transcription of ferri-siderophore uptake genes

Metabolic function and regulation of this protein in SubtiPathways:
Metal ion homeostasis, Alternative nitrogen sources, Protein secretion
MW, pI 17 kDa, 5.374
Gene length, protein length 447 bp, 149 aa
Immediate neighbours ripX, spoIIM
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
Fur context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
Fur expression.png



















Categories containing this gene/protein

iron metabolism, transcription factors and their control

This gene is a member of the following regulons

PerR regulon

The Fur regulon

The gene

Basic information

  • Locus tag: BSU23520

Phenotypes of a mutant

  • no growth with glucose and ammonium as single sources of carbon and nitrogen, respectively (due to FsrA-mediated repression of the gltA-gltB operon) PubMed
  • poor frowth on lactate as single carbon source (due to overexpression of FsrA-mediated repression of the lutA-lutB-lutC operon, can be suppressed by inactivation of fsrA or fbpB) PubMed
  • transcription profile of a fur mutant strain: GEO PubMed

Database entries

  • DBTBS entry: [1]
  • SubtiList entry: [2]

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity:

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification:
  • Cofactor(s): contains an iron-sulfur cluster
  • Effectors of protein activity:
    • DNA binding activity (repression) is triggered by binding of Fe(II) PubMed

Database entries

  • Structure:
  • KEGG entry: [3]
  • E.C. number:

Additional information

Expression and regulation

  • Regulation:
    • repressed in the absence of hydrogen peroxide (PerR) PubMed
  • Regulatory mechanism:
  • Additional information:

Biological materials

  • Mutant: HB6543 (aphA3), available in the John Helmann lab; also available in the Stülke lab GP879 (fur::mls) and GP868 (fur::mls, perR::spc)
  • Expression vector:
  • lacZ fusion:
  • GFP fusion:
  • two-hybrid system:
  • Antibody:

Labs working on this gene/protein

John Helmann, Cornell University, USA Homepage

Your additional remarks

References

Reviews

Charles M Moore, John D Helmann
Metal ion homeostasis in Bacillus subtilis.
Curr Opin Microbiol: 2005, 8(2);188-95
[PubMed:15802251] [WorldCat.org] [DOI] (P p)

The Fur regulon

Addititonal publications: PubMed

Other original publications


PubMed