Nos

• 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 This image was kindly provided by SubtiList
Expression at a glance   PubMed

Categories containing this gene/protein

miscellaneous metabolic pathways, biosynthesis of antibacterial compounds

The gene

Basic information

• Locus tag: BSU07630

Database entries

• BsubCyc: BSU07630

• DBTBS entry: [1]

• SubtiList entry: [2]

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:

• Cofactor(s): heme PubMed

• Effectors of protein activity:

• Interactions:

• Localization:

Database entries

• BsubCyc: BSU07630

• Structure: 2AMO (loose dimer), 1M7V (bound to tetrahydrofolate and arginine)

• UniProt: O34453

• KEGG entry: [3]

• E.C. number:

Expression and regulation

• Operon: nos-yflK (according to DBTBS)

• Expression browser: nos PubMed

• 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:

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)