Difference between revisions of "YjbH"
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'''Additional publications:''' {{PubMed|21378193}} | '''Additional publications:''' {{PubMed|21378193}} | ||
− | <pubmed>17293416, 19074380 17908206, 20525796</pubmed> | + | <pubmed>17293416, 19074380 17908206, 20525796 21947404</pubmed> |
[[Category:Protein-coding genes]] | [[Category:Protein-coding genes]] |
Revision as of 19:17, 29 September 2011
- Description: adaptor protein for ClpX-ClpP-catalyzed Spx degradation, confers resistance against nitrosylating agents
Gene name | yjbH |
Synonyms | |
Essential | no |
Product | adaptor protein |
Function | stimulation of Spx degradation |
Interactions involving this protein in SubtInteract: YjbH | |
MW, pI | 31 kDa, 5.206 |
Gene length, protein length | 825 bp, 275 aa |
Immediate neighbours | pepF, yjbI |
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
This gene is a member of the following regulons
The gene
Basic information
- Locus tag: BSU11550
Phenotypes of a mutant
Database entries
- DBTBS entry: no entry
- SubtiList entry: [1]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity: adaptor protein for ClpX-ClpP-catalyzed Spx degradation PubMed
- Protein family: UPF0413 family (according to Swiss-Prot)
- Paralogous protein(s):
Extended information on the protein
- Kinetic information:
- Domains:
- Modification:
- Cofactor(s):contains Zn atoms (coordinated by the N-terminal His-rich region) PubMed
- Effectors of protein activity:
- Localization: cytosolic protein
Database entries
- Structure:
- UniProt: O31606
- KEGG entry: [2]
- E.C. number:
Additional information
Expression and regulation
- Regulation:
- Regulatory mechanism:
Biological materials
- Mutant:
- Expression vector:
- lacZ fusion:
- GFP fusion:
- two-hybrid system:
- Antibody:
Labs working on this gene/protein
Peter Zuber, Oregon Health and Science University, USA Homepage
Claes von Wachenfeldt, Lund University, Sweden Homepage
Your additional remarks
References
Reviews: PubMed
Original Publications
Additional publications: PubMed