Difference between revisions of "CzrA"

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(References)
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* '''Structure:'''
 
* '''Structure:'''
 
+
** [http://www.rcsb.org/pdb/explore/explore.do?structureId=1R1U 1R1U] (the apo-repressor from ''Staph. aureus'', 49% identity, 82% similarity) {{PubMed|14568530}}
 +
** [http://www.rcsb.org/pdb/explore/explore.do?structureId=1R1V 1R1V] (the Zn(II) form from ''Staph. aureus'', 49% identity, 82% similarity) {{PubMed|14568530}}
 +
** [http://www.rcsb.org/pdb/explore/explore.do?structureId=2KJB 2KJB] (the DNA-bound form from ''Staph. aureus'', 49% identity, 82% similarity) {{PubMed|19822742}}
 
* '''UniProt:''' [http://www.uniprot.org/uniprot/O31844 O31844]
 
* '''UniProt:''' [http://www.uniprot.org/uniprot/O31844 O31844]
  
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=References=
 
=References=
 
'''Additional publications:'''  {{PubMed|22007899}}
 
'''Additional publications:'''  {{PubMed|22007899}}
<pubmed>15948947, 16430705, </pubmed>
+
<pubmed>15948947, 16430705, 14568530 19822742 </pubmed>
  
 
[[Category:Protein-coding genes]]
 
[[Category:Protein-coding genes]]

Revision as of 11:42, 25 November 2011

  • 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
YozA context.gif
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

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:
  • 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)

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:
  • 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

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)