Nos

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  • Description: nitric-oxide synthase

Gene name nos
Synonyms yflM
Essential no
Product nitric-oxide synthase
Function production of nitric oxide
Gene expression levels in SubtiExpress: nos
Interactions involving this protein in SubtInteract: Nos
MW, pI 38 kDa, 5.528
Gene length, protein length 1008 bp, 336 aa
Immediate neighbours yflN, yflL
Sequences Protein DNA DNA_with_flanks
Genetic context
YflM context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
Nos expression.png
























Categories containing this gene/protein

miscellaneous metabolic pathways, biosynthesis of antibacterial compounds

This gene is a member of the following regulons

The gene

Basic information

  • Locus tag: BSU07630

Phenotypes of a mutant

Database entries

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

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity:
  • Protein family: Bacterial NOS oxygenase subfamily (according to Swiss-Prot)
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification:
  • Effectors of protein activity:

Database entries

  • Structure: 2AMO (loose dimer), 1M7V (bound to tetrahydrofolate and arginine)
  • KEGG entry: [3]
  • E.C. number:

Additional information

Expression and regulation

  • Sigma factor:
  • Regulation:
  • Regulatory mechanism:
  • Additional information: Note that the gene yflL is located between nos and yflK, but on the opposite strand.
    • number of protein molecules per cell (minimal medium with glucose and ammonium): 18 PubMed

Biological materials

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

Labs working on this gene/protein

Your additional remarks

References

Jérôme Santolini, Amandine Maréchal, Alain Boussac, Pierre Dorlet
EPR characterisation of the ferrous nitrosyl complex formed within the oxygenase domain of NO synthase.
Chembiochem: 2013, 14(14);1852-7
[PubMed:23943262] [WorldCat.org] [DOI] (I p)

Isabelle Salard-Arnaud, Dennis Stuehr, Jean-Luc Boucher, Daniel Mansuy
Spectroscopic, catalytic and binding properties of Bacillus subtilis NO synthase-like protein: comparison with other bacterial and mammalian NO synthases.
J Inorg Biochem: 2012, 106(1);164-71
[PubMed:22119809] [WorldCat.org] [DOI] (I p)

Luciana Hannibal, Ramasamy Somasundaram, Jesús Tejero, Adjele Wilson, Dennis J Stuehr
Influence of heme-thiolate in shaping the catalytic properties of a bacterial nitric-oxide synthase.
J Biol Chem: 2011, 286(45);39224-35
[PubMed:21921039] [WorldCat.org] [DOI] (I p)

Frank Schreiber, Martin Beutler, Dennis Enning, María Lamprecht-Grandio, Olga Zafra, José Eduardo González-Pastor, Dirk de Beer
The role of nitric-oxide-synthase-derived nitric oxide in multicellular traits of Bacillus subtilis 3610: biofilm formation, swarming, and dispersal.
BMC Microbiol: 2011, 11;111
[PubMed:21599925] [WorldCat.org] [DOI] (I e)

Albane Brunel, Adjélé Wilson, Laura Henry, Pierre Dorlet, Jérôme Santolini
The proximal hydrogen bond network modulates Bacillus subtilis nitric-oxide synthase electronic and structural properties.
J Biol Chem: 2011, 286(14);11997-2005
[PubMed:21310962] [WorldCat.org] [DOI] (I p)

Zhi-Qiang Wang, Chin-Chuan Wei, Dennis J Stuehr
How does a valine residue that modulates heme-NO binding kinetics in inducible NO synthase regulate enzyme catalysis?
J Inorg Biochem: 2010, 104(3);349-56
[PubMed:20006999] [WorldCat.org] [DOI] (I p)

Kartikeya Pant, Alexandrine M Bilwes, Subrata Adak, Dennis J Stuehr, Brian R Crane
Structure of a nitric oxide synthase heme protein from Bacillus subtilis.
Biochemistry: 2002, 41(37);11071-9
[PubMed:12220171] [WorldCat.org] [DOI] (P p)

Subrata Adak, Kulwant S Aulak, Dennis J Stuehr
Direct evidence for nitric oxide production by a nitric-oxide synthase-like protein from Bacillus subtilis.
J Biol Chem: 2002, 277(18);16167-71
[PubMed:11856757] [WorldCat.org] [DOI] (P p)