MntR

• 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
Gene expression levels in SubtiExpress: mntR
Metabolic function and regulation of this protein in SubtiPathways: mntR
MW, pI	16 kDa, 5.631
Gene length, protein length	426 bp, 142 aa
Immediate neighbours	yqhO, lipM
Sequences	Protein DNA DNA_with_flanks
Genetic context This image was kindly provided by SubtiList
Expression at a glance   PubMed

Categories containing this gene/protein

trace metal homeostasis (Cu, Zn, Ni, Mn, Mo), transcription factors and their control, membrane proteins

The MntR regulon:

• mntA-mntB-mntC-mntD, mntH

The gene

Basic information

• Locus tag: BSU24520

Database entries

• BsubCyc: BSU24520

• 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): 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

• BsubCyc: BSU24520

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

• UniProt: P54512

• KEGG entry: [2]

• E.C. number:

Expression and regulation

• Operon:

• Expression browser: mntR PubMed

• Sigma factor:

• Regulation:

• Regulatory mechanism:

• Additional information:
  • number of protein molecules per cell (minimal medium with glucose and ammonium): 376 PubMed
  • number of protein molecules per cell (complex medium with amino acids, without glucose): 790 PubMed
  • number of protein molecules per cell (minimal medium with glucose and ammonium, exponential phase): 900 PubMed
  • number of protein molecules per cell (minimal medium with glucose and ammonium, early stationary phase after glucose exhaustion): 300 PubMed
  • number of protein molecules per cell (minimal medium with glucose and ammonium, late stationary phase after glucose exhaustion): 488 PubMed

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

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

Amanda M McGuire, Bonnie J Cuthbert, Zhen Ma, Kristen D Grauer-Gray, Megan Brunjes Brophy, Kayce A Spear, Sumarin Soonsanga, Joseph I Kliegman, Sarah L Griner, John D Helmann, Arthur Glasfeld
Roles of the A and C sites in the manganese-specific activation of MntR.
Biochemistry: 2013, 52(4);701-13
[PubMed:23298157] [WorldCat.org] [DOI] (I p)

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)