Difference between revisions of "MntR"

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|style="background:#ABCDEF;" align="center"| '''Gene length, protein length''' || 426 bp, 142 aa  
 
|style="background:#ABCDEF;" align="center"| '''Gene length, protein length''' || 426 bp, 142 aa  
 
|-
 
|-
|style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[yqhO]]'', ''[[yqhM]]''
+
|style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[yqhO]]'', ''[[lipM]]''
 
|-
 
|-
 
|colspan="2" style="background:#FAF8CC;" align="center"|'''Get the DNA and protein [http://srs.ebi.ac.uk/srsbin/cgi-bin/wgetz?-e+&#91;EMBLCDS:CAB14383&#93;+-newId sequences] <br/> (Barbe ''et al.'', 2009)'''
 
|colspan="2" style="background:#FAF8CC;" align="center"|'''Get the DNA and protein [http://srs.ebi.ac.uk/srsbin/cgi-bin/wgetz?-e+&#91;EMBLCDS:CAB14383&#93;+-newId sequences] <br/> (Barbe ''et al.'', 2009)'''

Revision as of 15:44, 11 October 2010

  • Description: transcriptional regulator, (repression of mntH and mntA-mntB-mntC-mntD under high Mn(II) conditions)


Gene name mntR
Synonyms yqhN
Essential no
Product transcriptional regulator (DtxR family)
Function regulation of manganese transport
Metabolic function and regulation of this protein in SubtiPathways:
Stress
MW, pI 16 kDa, 5.631
Gene length, protein length 426 bp, 142 aa
Immediate neighbours yqhO, lipM
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
MntR context.gif
This image was kindly provided by SubtiList







The gene

Basic information

  • Locus tag: BSU24520

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): Mn(2+) acts as co-repressor (according to PubMed)
  • Effectors of protein activity:
  • Interactions:
    • active as dimer (according to PubMed)
  • Localization: cell membrane (according to Swiss-Prot)

Database entries

  • Structure: 2F5D (complex with manganese), 2HYG (apo-form)
  • 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

John Helmann, Cornell University, USA Homepage

Richard Brennan, Houston, Texas, USA Homepage

Your additional remarks

References

Reviews

Sabine Brantl, Andreas Licht
Characterisation of Bacillus subtilis transcriptional regulators involved in metabolic processes.
Curr Protein Pept Sci: 2010, 11(4);274-91
[PubMed:20408793] [WorldCat.org] [DOI] (I p)


Original Publications

Misha V Golynskiy, William A Gunderson, Michael P Hendrich, Seth M Cohen
Metal binding studies and EPR spectroscopy of the manganese transport regulator MntR.
Biochemistry: 2006, 45(51);15359-72
[PubMed:17176058] [WorldCat.org] [DOI] (I p)

Mark A DeWitt, Joseph I Kliegman, John D Helmann, Richard G Brennan, David L Farrens, Arthur Glasfeld
The conformations of the manganese transport regulator of Bacillus subtilis in its metal-free state.
J Mol Biol: 2007, 365(5);1257-65
[PubMed:17118401] [WorldCat.org] [DOI] (P p)

Joseph I Kliegman, Sarah L Griner, John D Helmann, Richard G Brennan, Arthur Glasfeld
Structural basis for the metal-selective activation of the manganese transport regulator of Bacillus subtilis.
Biochemistry: 2006, 45(11);3493-505
[PubMed:16533030] [WorldCat.org] [DOI] (P p)

Misha V Golynskiy, Talib C Davis, John D Helmann, Seth M Cohen
Metal-induced structural organization and stabilization of the metalloregulatory protein MntR.
Biochemistry: 2005, 44(9);3380-9
[PubMed:15736948] [WorldCat.org] [DOI] (P p)

Scot A Lieser, Talib C Davis, John D Helmann, Seth M Cohen
DNA-binding and oligomerization studies of the manganese(II) metalloregulatory protein MntR from Bacillus subtilis.
Biochemistry: 2003, 42(43);12634-42
[PubMed:14580210] [WorldCat.org] [DOI] (P p)

Emmanuel Guedon, Charles M Moore, Qiang Que, Tao Wang, Rick W Ye, John D Helmann
The global transcriptional response of Bacillus subtilis to manganese involves the MntR, Fur, TnrA and sigmaB regulons.
Mol Microbiol: 2003, 49(6);1477-91
[PubMed:12950915] [WorldCat.org] [DOI] (P p)

Arthur Glasfeld, Emmanuel Guedon, John D Helmann, Richard G Brennan
Structure of the manganese-bound manganese transport regulator of Bacillus subtilis.
Nat Struct Biol: 2003, 10(8);652-7
[PubMed:12847518] [WorldCat.org] [DOI] (P p)

Emmanuel Guedon, John D Helmann
Origins of metal ion selectivity in the DtxR/MntR family of metalloregulators.
Mol Microbiol: 2003, 48(2);495-506
[PubMed:12675807] [WorldCat.org] [DOI] (P p)

Q Que, J D Helmann
Manganese homeostasis in Bacillus subtilis is regulated by MntR, a bifunctional regulator related to the diphtheria toxin repressor family of proteins.
Mol Microbiol: 2000, 35(6);1454-68
[PubMed:10760146] [WorldCat.org] [DOI] (P p)