CzrA

• Description: transcriptional repressor of cadA and czcD
  
  

Gene name	czrA
Synonyms	yozA
Essential	no
Product	transcriptional repressor (ArsR family)
Function	regulation of resistance against toxic metal cations
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
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, resistance against toxic metals

The CzrA regulon:

• cadA, czcD-trkA

The gene

Basic information

• Locus tag: BSU19120

Database entries

• DBTBS entry: no entry

• SubtiList entry: [1]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity:

• Protein family:

• 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)

• Interactions:

• Localization:

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:

Expression and regulation

• Operon:

• Expression browser: czrA PubMed

• Sigma factor:

• Regulation:

• Regulatory mechanism:

• Additional information:

Biological materials

• Mutant:

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

References

Additional publications: PubMed

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] [DOI] (P p)