Difference between revisions of "Hmp"

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=== Additional information===
 
=== Additional information===
 
 
 
  
 
=The protein=
 
=The protein=
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=Expression and regulation=
 
=Expression and regulation=
  
* '''Operon:''' ''hmp'' {{PubMed|8682784}}
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* '''Operon:'''  
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** ''hmp'' {{PubMed|8682784}}
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** ''[[hmp]]-[[ykjA]]'' {{PubMed|22383849}}
  
 
* '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=hmp_1372792_1373991_1 hmp] {{PubMed|22383849}}
 
* '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=hmp_1372792_1373991_1 hmp] {{PubMed|22383849}}
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=References=
 
=References=
  
<pubmed>8682784,15231799,,10972836,16885456,18487332, 16923910 </pubmed>
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<pubmed>8682784,15231799,,10972836,16885456,18487332, 16923910 22383849</pubmed>
  
 
[[Category:Protein-coding genes]]
 
[[Category:Protein-coding genes]]

Revision as of 15:47, 26 May 2014

  • Description: flavohemoglobin, involved in resistance to nitric oxide (NO), essential for long-term survival under anaerobic conditions

Gene name hmp
Synonyms ykiA
Essential no
Product flavohemoglobin
Function resistance to NO
Gene expression levels in SubtiExpress: hmp
Metabolic function and regulation of this protein in SubtiPathways:
hmp
MW, pI 44 kDa, 5.705
Gene length, protein length 1197 bp, 399 aa
Immediate neighbours ykhA, ykzH
Sequences Protein DNA DNA_with_flanks
Genetic context
Hmp context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
Hmp expression.png




























Categories containing this gene/protein

electron transport/ other, resistance against other toxic compounds (nitric oxide, phenolic acids, flavonoids, oxalate)

This gene is a member of the following regulons

NsrR regulon, ResD regulon

The gene

Basic information

  • Locus tag: BSU13040

Phenotypes of a mutant

Database entries

  • DBTBS entry: [1]
  • SubtiList entry: [2]

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: 2 NO + 2 O2 + NAD(P)H = 2 NO3- + NAD(P)+ (according to Swiss-Prot)
  • Protein family: FAD-binding FR-type domain (according to Swiss-Prot)
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification:
  • Cofactor(s):
  • Effectors of protein activity:

Database entries

  • Structure:
  • KEGG entry: [3]
  • E.C. number:

Additional information

Expression and regulation

  • Regulation:
    • expressed under anaerobic conditions (ResD) PubMed
    • induced by nitric oxide under anaerobic conditions (NsrR) PubMed
  • Additional information:
    • number of protein molecules per cell (minimal medium with glucose and ammonium): 27 PubMed
    • number of protein molecules per cell (complex medium with amino acids, without glucose): 346 PubMed

Biological materials

  • Mutant:
  • Expression vector:
  • lacZ fusion:
  • GFP fusion:
  • two-hybrid system:
  • Antibody:

Labs working on this gene/protein

Your additional remarks

References

Pierre Nicolas, Ulrike Mäder, Etienne Dervyn, Tatiana Rochat, Aurélie Leduc, Nathalie Pigeonneau, Elena Bidnenko, Elodie Marchadier, Mark Hoebeke, Stéphane Aymerich, Dörte Becher, Paola Bisicchia, Eric Botella, Olivier Delumeau, Geoff Doherty, Emma L Denham, Mark J Fogg, Vincent Fromion, Anne Goelzer, Annette Hansen, Elisabeth Härtig, Colin R Harwood, Georg Homuth, Hanne Jarmer, Matthieu Jules, Edda Klipp, Ludovic Le Chat, François Lecointe, Peter Lewis, Wolfram Liebermeister, Anika March, Ruben A T Mars, Priyanka Nannapaneni, David Noone, Susanne Pohl, Bernd Rinn, Frank Rügheimer, Praveen K Sappa, Franck Samson, Marc Schaffer, Benno Schwikowski, Leif Steil, Jörg Stülke, Thomas Wiegert, Kevin M Devine, Anthony J Wilkinson, Jan Maarten van Dijl, Michael Hecker, Uwe Völker, Philippe Bessières, Philippe Noirot
Condition-dependent transcriptome reveals high-level regulatory architecture in Bacillus subtilis.
Science: 2012, 335(6072);1103-6
[PubMed:22383849] [WorldCat.org] [DOI] (I p)

Falko Hochgräfe, Carmen Wolf, Stephan Fuchs, Manuel Liebeke, Michael Lalk, Susanne Engelmann, Michael Hecker
Nitric oxide stress induces different responses but mediates comparable protein thiol protection in Bacillus subtilis and Staphylococcus aureus.
J Bacteriol: 2008, 190(14);4997-5008
[PubMed:18487332] [WorldCat.org] [DOI] (I p)

Michiko M Nakano
Essential role of flavohemoglobin in long-term anaerobic survival of Bacillus subtilis.
J Bacteriol: 2006, 188(17);6415-8
[PubMed:16923910] [WorldCat.org] [DOI] (P p)

Michiko M Nakano, Hao Geng, Shunji Nakano, Kazuo Kobayashi
The nitric oxide-responsive regulator NsrR controls ResDE-dependent gene expression.
J Bacteriol: 2006, 188(16);5878-87
[PubMed:16885456] [WorldCat.org] [DOI] (P p)

Charles M Moore, Michiko M Nakano, Tao Wang, Rick W Ye, John D Helmann
Response of Bacillus subtilis to nitric oxide and the nitrosating agent sodium nitroprusside.
J Bacteriol: 2004, 186(14);4655-64
[PubMed:15231799] [WorldCat.org] [DOI] (P p)

M M Nakano, Y Zhu, M Lacelle, X Zhang, F M Hulett
Interaction of ResD with regulatory regions of anaerobically induced genes in Bacillus subtilis.
Mol Microbiol: 2000, 37(5);1198-207
[PubMed:10972836] [WorldCat.org] [DOI] (P p)

M LaCelle, M Kumano, K Kurita, K Yamane, P Zuber, M M Nakano
Oxygen-controlled regulation of the flavohemoglobin gene in Bacillus subtilis.
J Bacteriol: 1996, 178(13);3803-8
[PubMed:8682784] [WorldCat.org] [DOI] (P p)