Difference between revisions of "YjbI"
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| + | = [[Categories]] containing this gene/protein = | ||
| + | {{SubtiWiki category|[[resistance against other toxic compounds (nitric oxide, phenolic acids, flavonoids, oxalate)]]}} | ||
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| + | = This gene is a member of the following [[regulons]] = | ||
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=The gene= | =The gene= | ||
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=The protein= | =The protein= | ||
Revision as of 18:30, 8 December 2010
- Description: truncated hemoglobin, NO protection
| Gene name | yjbI |
| Synonyms | |
| Essential | no |
| Product | truncated hemoglobin |
| Function | protection against NO, thiol redox homeostasis |
| 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
| |
Contents
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
- Structure: 1UX8
- UniProt: O31607
- KEGG entry: [2]
- E.C. number:
Additional information
Expression and regulation
- 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
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)
