CzrA

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Gene name czrA
Synonyms yozA
Essential no
Product transcriptional repressor (ArsR family)
Function regulation of resistance against toxic metal cations
Gene expression levels in SubtiExpress: czrA
Metabolic function and regulation of this protein in SubtiPathways:
metal ion homeostasis
MW, pI 12 kDa, 5.719
Gene length, protein length 321 bp, 107 aa
Immediate neighbours yobW, yocA
Sequences Protein DNA DNA_with_flanks
Genetic context
YozA context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
CzrA expression.png

Contents















Categories containing this gene/protein

trace metal homeostasis (Cu, Zn, Ni, Mn, Mo), transcription factors and their control, resistance against toxic metals

This gene is a member of the following regulons

The CzrA regulon:

The gene

Basic information

  • Locus tag: BSU19120

Phenotypes of a mutant

Database entries

  • DBTBS entry: no entry
  • SubtiList entry: [1]

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity:
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification:
  • Cofactor(s):
  • Effectors of protein activity:
    • DNA-binding activity of CzrA is inactivated by high concentrations of toxic metal ions (induction)

Database entries

  • Structure:
    • 1R1U (the apo-repressor from Staph. aureus, 49% identity, 82% similarity) PubMed
    • 1R1V (the Zn(II) form from Staph. aureus, 49% identity, 82% similarity) PubMed
    • 2KJB (the DNA-bound form from Staph. aureus, 49% identity, 82% similarity) PubMed
  • UniProt: O31844
  • KEGG entry: [2]
  • E.C. number:

Additional information

Expression and regulation

  • Operon:
  • 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

Your additional remarks

References

Zhen Ma, Pete Chandrangsu, Tyler C Helmann, Adisak Romsang, Ahmed Gaballa, John D Helmann
Bacillithiol is a major buffer of the labile zinc pool in Bacillus subtilis.
Mol. Microbiol.: 2014, 94(4);756-70
[PubMed:25213752] [WorldCat.org] [DOI] (I p)

Dhruva K Chakravorty, Bing Wang, Chul Won Lee, David P Giedroc, Kenneth M Merz
Simulations of allosteric motions in the zinc sensor CzrA.
J. Am. Chem. Soc.: 2012, 134(7);3367-76
[PubMed:22007899] [WorldCat.org] [DOI] (I p)

Alphonse I Arunkumar, Gregory C Campanello, David P Giedroc
Solution structure of a paradigm ArsR family zinc sensor in the DNA-bound state.
Proc. Natl. Acad. Sci. U.S.A.: 2009, 106(43);18177-82
[PubMed:19822742] [WorldCat.org] [DOI] (I p)

Duncan R Harvie, Claudia Andreini, Gabriele Cavallaro, Wenmao Meng, Bernard A Connolly, Ken-ichi Yoshida, Yasutaro Fujita, Colin R Harwood, David S Radford, Stephen Tottey, Jennifer S Cavet, Nigel J Robinson
Predicting metals sensed by ArsR-SmtB repressors: allosteric interference by a non-effector metal.
Mol. Microbiol.: 2006, 59(4);1341-56
[PubMed:16430705] [WorldCat.org] [DOI] (P p)

Charles M Moore, Ahmed Gaballa, Monica Hui, Rick W Ye, John D Helmann
Genetic and physiological responses of Bacillus subtilis to metal ion stress.
Mol. Microbiol.: 2005, 57(1);27-40
[PubMed:15948947] [WorldCat.org] [DOI] (P p)

Christoph Eicken, Mario A Pennella, Xiaohua Chen, Karl M Koshlap, Michael L VanZile, James C Sacchettini, David P Giedroc
A metal-ligand-mediated intersubunit allosteric switch in related SmtB/ArsR zinc sensor proteins.
J. Mol. Biol.: 2003, 333(4);683-95
[PubMed:14568530] [WorldCat.org] (P p)

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