Zur

• Description: transcriptional repressor, regulates zinc homeostasis
  
  

Gene name	zur
Synonyms	yqfV
Essential	no
Product	transcriptional repressor (Fur family)
Function	regulation of zinc homeostasis (yciC, znuA-znuC-znuB)
Gene expression levels in SubtiExpress: zur
Regulatory function of this protein in SubtiPathways: Stress
MW, pI	16 kDa, 4.856
Gene length, protein length	435 bp, 145 aa
Immediate neighbours	yqfW, yqfU
Sequences	Protein DNA DNA_with_flanks
Genetic context This image was kindly provided by SubtiList
Expression at a glance   PubMed

Categories containing this gene/protein

trace metal homeostasis (Cu, Zn, Ni, Mn, Mo), transcription factors and their control, phosphoproteins

The gene

Basic information

• Locus tag: BSU25100

Database entries

• DBTBS entry: no entry

• SubtiList entry: [1]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity:

• Protein family: Fur family

• Paralogous protein(s): PerR, Fur

Extended information on the protein

• Kinetic information:

• Domains:

• Modification: phosphorylated on ser/ thr/ tyr PubMed

• Cofactor(s):

• Effectors of protein activity:
  • sequential binding of zinc (two atoms per monomer) results in the activation of Zur and thus in repression of the genes of the Zur regulon PubMed

• Interactions:
  • forms dimers PubMed

• Localization:

Database entries

• Structure:

• UniProt: P54479

• KEGG entry: [2]

• E.C. number:

Expression and regulation

• Operon:

• Expression browser: zur PubMed

• Sigma factor:

• Regulation:

• Regulatory mechanism:

• Additional information:

Biological materials

• Mutant:
  • 1A904 ( zur::spec), PubMed, available at BGSC

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

Labs working on this gene/protein

John Helmann, Cornell University, USA Homepage

References

Zhen Ma, Scott E Gabriel, John D Helmann
Sequential binding and sensing of Zn(II) by Bacillus subtilis Zur.
Nucleic Acids Res: 2011, 39(21);9130-8
[PubMed:21821657] [WorldCat.org] [DOI] (I p)

Scott E Gabriel, John D Helmann
Contributions of Zur-controlled ribosomal proteins to growth under zinc starvation conditions.
J Bacteriol: 2009, 191(19);6116-22
[PubMed:19648245] [WorldCat.org] [DOI] (I p)

Scott E Gabriel, Faith Miyagi, Ahmed Gaballa, John D Helmann
Regulation of the Bacillus subtilis yciC gene and insights into the DNA-binding specificity of the zinc-sensing metalloregulator Zur.
J Bacteriol: 2008, 190(10);3482-8
[PubMed:18344368] [WorldCat.org] [DOI] (I p)

Alain Lévine, Françoise Vannier, Cédric Absalon, Lauriane Kuhn, Peter Jackson, Elaine Scrivener, Valérie Labas, Joëlle Vinh, Patrick Courtney, Jérôme Garin, Simone J Séror
Analysis of the dynamic Bacillus subtilis Ser/Thr/Tyr phosphoproteome implicated in a wide variety of cellular processes.
Proteomics: 2006, 6(7);2157-73
[PubMed:16493705] [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)

Ekaterina M Panina, Andrey A Mironov, Mikhail S Gelfand
Comparative genomics of bacterial zinc regulons: enhanced ion transport, pathogenesis, and rearrangement of ribosomal proteins.
Proc Natl Acad Sci U S A: 2003, 100(17);9912-7
[PubMed:12904577] [WorldCat.org] [DOI] (P p)

Ahmed Gaballa, Tao Wang, Rick W Ye, John D Helmann
Functional analysis of the Bacillus subtilis Zur regulon.
J Bacteriol: 2002, 184(23);6508-14
[PubMed:12426338] [WorldCat.org] [DOI] (P p)

A Gaballa, J D Helmann
Identification of a zinc-specific metalloregulatory protein, Zur, controlling zinc transport operons in Bacillus subtilis.
J Bacteriol: 1998, 180(22);5815-21
[PubMed:9811636] [WorldCat.org] [DOI] (P p)