Fur

• 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 This image was kindly provided by SubtiList

The gene

Basic information

• Locus tag: BSU23520

Database entries

• DBTBS entry: [1]

• SubtiList entry: [2]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity:

• Protein family: Fur family (according to Swiss-Prot)

• Paralogous protein(s): PerR, Zur

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:

• Swiss prot entry: P54574

• KEGG entry: [3]

• E.C. number:

Expression and regulation

• Operon: fur

• Sigma factor: SigA

• Regulation: repressed by PerR
  • repressed in the absence of hydrogen peroxide (PerR) PubMed

• Regulatory mechanism: PerR: transcription repression
  • PerR: transcription repression PubMed

• 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

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)

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)

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)

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)

PubMed