Difference between revisions of "YjbI"

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* '''Mutant:'''
 
* '''Mutant:'''
 +
** 1A864 ( ''yjbI''::''spec''), {{PubMed| }}, available at [http://pasture.asc.ohio-state.edu/BGSC/getdetail.cfm?bgscid=1A864&Search=1A864 BGSC]
  
 
* '''Expression vector:'''
 
* '''Expression vector:'''

Revision as of 12:27, 19 September 2012

  • Description: truncated hemoglobin, NO protection

Gene name yjbI
Synonyms
Essential no
Product truncated hemoglobin
Function protection against NO, thiol redox homeostasis
Gene expression levels in SubtiExpress: yjbI
MW, pI 14 kDa, 5.173
Gene length, protein length 396 bp, 132 aa
Immediate neighbours yjbH, cwlQ
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
YjbI context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
YjbI expression.png
























Categories containing this gene/protein

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

This gene is a member of the following regulons

The gene

Basic information

  • Locus tag: BSU11560

Phenotypes of a mutant

Database entries

  • DBTBS entry: no entry
  • SubtiList entry: [1]

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: binds sulfide with high affinity PubMed
  • Protein family: protozoan/cyanobacterial globin family (according to Swiss-Prot)
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information: K(D) for hydrogen sulfide = 5.0x10(6) M-1 PubMed
  • Domains:
  • Modification:
  • Cofactor(s):
  • Effectors of protein activity:
  • Interactions:
  • Localization:

Database entries

  • KEGG entry: [2]
  • E.C. number:

Additional information

Expression and regulation

  • Sigma factor:
  • Regulation:
  • Regulatory mechanism:
  • Additional information:

Biological materials

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

Labs working on this gene/protein

Your additional remarks

References

Andrea Lapini, Mariangela Di Donato, Barbara Patrizi, Agnese Marcelli, Manuela Lima, Roberto Righini, Paolo Foggi, Natascia Sciamanna, Alberto Boffi
Carbon monoxide recombination dynamics in truncated hemoglobins studied with visible-pump midIR-probe spectroscopy.
J Phys Chem B: 2012, 116(30);8753-61
[PubMed:22759230] [WorldCat.org] [DOI] (I p)

Francesco P Nicoletti, Alessandra Comandini, Alessandra Bonamore, Leonardo Boechi, Fernando Martin Boubeta, Alessandro Feis, Giulietta Smulevich, Alberto Boffi
Sulfide binding properties of truncated hemoglobins.
Biochemistry: 2010, 49(10);2269-78
[PubMed:20102180] [WorldCat.org] [DOI] (I p)

Leonardo Boechi, Pau Arroyo Mañez, F Javier Luque, Marcelo A Marti, Dario A Estrin
Unraveling the molecular basis for ligand binding in truncated hemoglobins: the trHbO Bacillus subtilis case.
Proteins: 2010, 78(4);962-70
[PubMed:19899166] [WorldCat.org] [DOI] (I p)

Annika Rogstam, Jonas T Larsson, Peter Kjelgaard, Claes von Wachenfeldt
Mechanisms of adaptation to nitrosative stress in Bacillus subtilis.
J Bacteriol: 2007, 189(8);3063-71
[PubMed:17293416] [WorldCat.org] [DOI] (P p)