Difference between revisions of "Fur"

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[[Category:Protein-coding genes]]

Revision as of 11:30, 21 July 2009

  • Description: transcription regulator of iron homoeostasis

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

and transcription of ferri-siderophore uptake genes

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







The gene

Basic information

  • Locus tag: BSU23520

Phenotypes of a mutant

Database entries

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

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity:
  • Protein family: Fur family (according to Swiss-Prot)

Genes controlled by Fur

fsrA

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification:
  • Cofactor(s):
  • Effectors of protein activity:
  • Interactions:
  • Localization: cytoplasm (according to Swiss-Prot)

Database entries

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

Additional information

Expression and regulation

  • Operon: fur
  • Regulation: repressed by PerR
    • repressed in the absence of hydrogen peroxide (PerR) PubMed
  • Regulatory mechanism: PerR: transcription repression
  • Additional information:

Biological materials

  • Mutant:
  • 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

David P Giedroc
Hydrogen peroxide sensing in Bacillus subtilis: it is all about the (metallo)regulator.
Mol Microbiol: 2009, 73(1);1-4
[PubMed:19508286] [WorldCat.org] [DOI] (I p)

L Jacquamet, D A K Traoré, J-L Ferrer, O Proux, D Testemale, J-L Hazemann, E Nazarenko, A El Ghazouani, C Caux-Thang, V Duarte, J-M Latour
Structural characterization of the active form of PerR: insights into the metal-induced activation of PerR and Fur proteins for DNA binding.
Mol Microbiol: 2009, 73(1);20-31
[PubMed:19508285] [WorldCat.org] [DOI] (I p)

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)

Falko Hochgräfe, Carmen Wolf, Stephan Fuchs, Manuel Liebeke, Michael Lalk, Susanne Engelmann, Michael Hecker
Nitric oxide stress induces different responses but mediates comparable protein thiol protection in Bacillus subtilis and Staphylococcus aureus.
J Bacteriol: 2008, 190(14);4997-5008
[PubMed:18487332] [WorldCat.org] [DOI] (I p)

Ahmed Gaballa, John D Helmann
Substrate induction of siderophore transport in Bacillus subtilis mediated by a novel one-component regulator.
Mol Microbiol: 2007, 66(1);164-73
[PubMed:17725565] [WorldCat.org] [DOI] (P p)

Marcus Miethke, Helga Westers, Evert-Jan Blom, Oscar P Kuipers, Mohamed A Marahiel
Iron starvation triggers the stringent response and induces amino acid biosynthesis for bacillibactin production in Bacillus subtilis.
J Bacteriol: 2006, 188(24);8655-7
[PubMed:17012385] [WorldCat.org] [DOI] (P p)

Juliane Ollinger, Kyung-Bok Song, Haike Antelmann, Michael Hecker, John D Helmann
Role of the Fur regulon in iron transport in Bacillus subtilis.
J Bacteriol: 2006, 188(10);3664-73
[PubMed:16672620] [WorldCat.org] [DOI] (P p)

Mayuree Fuangthong, John D Helmann
Recognition of DNA by three ferric uptake regulator (Fur) homologs in Bacillus subtilis.
J Bacteriol: 2003, 185(21);6348-57
[PubMed:14563870] [WorldCat.org] [DOI] (P p)

Emmanuel Guedon, Charles M Moore, Qiang Que, Tao Wang, Rick W Ye, John D Helmann
The global transcriptional response of Bacillus subtilis to manganese involves the MntR, Fur, TnrA and sigmaB regulons.
Mol Microbiol: 2003, 49(6);1477-91
[PubMed:12950915] [WorldCat.org] [DOI] (P p)

Noel Baichoo, John D Helmann
Recognition of DNA by Fur: a reinterpretation of the Fur box consensus sequence.
J Bacteriol: 2002, 184(21);5826-32
[PubMed:12374814] [WorldCat.org] [DOI] (P p)

Noel Baichoo, Tao Wang, Rick Ye, John D Helmann
Global analysis of the Bacillus subtilis Fur regulon and the iron starvation stimulon.
Mol Microbiol: 2002, 45(6);1613-29
[PubMed:12354229] [WorldCat.org] [DOI] (P p)

Min Cao, Tao Wang, Rick Ye, John D Helmann
Antibiotics that inhibit cell wall biosynthesis induce expression of the Bacillus subtilis sigma(W) and sigma(M) regulons.
Mol Microbiol: 2002, 45(5);1267-76
[PubMed:12207695] [WorldCat.org] [DOI] (P p)

Mayuree Fuangthong, Andrew F Herbig, Nada Bsat, John D Helmann
Regulation of the Bacillus subtilis fur and perR genes by PerR: not all members of the PerR regulon are peroxide inducible.
J Bacteriol: 2002, 184(12);3276-86
[PubMed:12029044] [WorldCat.org] [DOI] (P p)

Tamara Hoffmann, Alexandra Schütz, Margot Brosius, Andrea Völker, Uwe Völker, Erhard Bremer
High-salinity-induced iron limitation in Bacillus subtilis.
J Bacteriol: 2002, 184(3);718-27
[PubMed:11790741] [WorldCat.org] [DOI] (P p)

N Bsat, J D Helmann
Interaction of Bacillus subtilis Fur (ferric uptake repressor) with the dhb operator in vitro and in vivo.
J Bacteriol: 1999, 181(14);4299-307
[PubMed:10400588] [WorldCat.org] [DOI] (P p)

N Bsat, A Herbig, L Casillas-Martinez, P Setlow, J D Helmann
Bacillus subtilis contains multiple Fur homologues: identification of the iron uptake (Fur) and peroxide regulon (PerR) repressors.
Mol Microbiol: 1998, 29(1);189-98
[PubMed:9701813] [WorldCat.org] [DOI] (P p)


PubMed