Zur

• Description: transcriptional repressor, regulates zinc homeostasis
  
  

Gene name	zur
Synonyms	yqfV
Essential	no
Product	transcriptional repressor
Function	regulation of zinc homeostasis (yciC, znuA-znuC-znuB)
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
Get the DNA and protein sequences (Barbe et al., 2009)
Genetic context This image was kindly provided by SubtiList

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 (according to Swiss-Prot)

• 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:

• 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)