YjbI

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

Categories containing this gene/protein

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

The gene

Basic information

• Locus tag: BSU11560

Database entries

• DBTBS entry: no entry

• SubtiList entry: [1]

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

• Structure: 1UX8

• UniProt: O31607

• KEGG entry: [2]

• E.C. number:

Expression and regulation

• Operon: yjbI-yjbH PubMed

• Expression browser: yjbI PubMed

• Sigma factor:

• Regulation:

• Regulatory mechanism:

• Additional information:

Biological materials

• Mutant:
  • 1A864 ( yjbI::spec), PubMed, available at BGSC

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

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)