Difference between revisions of "YfhM"
Line 119: | Line 119: | ||
=References= | =References= | ||
− | <pubmed>15805528, </pubmed> | + | <pubmed>9987136,10913081,,15805528, </pubmed> |
# Höper et al. (2005) Comprehensive Characterization of the Contribution of Individual [[SigB]]-Dependent General Stress Genes to Stress Resistance of ''Bacillus subtilis''. J. Bact. '''187:''' 2810-2826 [http://www.ncbi.nlm.nih.gov/pubmed/15805528 PubMed] | # Höper et al. (2005) Comprehensive Characterization of the Contribution of Individual [[SigB]]-Dependent General Stress Genes to Stress Resistance of ''Bacillus subtilis''. J. Bact. '''187:''' 2810-2826 [http://www.ncbi.nlm.nih.gov/pubmed/15805528 PubMed] | ||
# Gerth et al. (2008) Clp-dependent proteolysis down-regulates central metabolic pathways in glucose-starved Bacillus subtilis. J Bacteriol 190:321-331 [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Abstract&list_uids=+17981983 PubMed] | # Gerth et al. (2008) Clp-dependent proteolysis down-regulates central metabolic pathways in glucose-starved Bacillus subtilis. J Bacteriol 190:321-331 [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Abstract&list_uids=+17981983 PubMed] | ||
# Author1, Author2 & Author3 (year) Title ''Journal'' '''volume:''' page-page. [http://www.ncbi.nlm.nih.gov/sites/entrez/PMID PubMed] | # Author1, Author2 & Author3 (year) Title ''Journal'' '''volume:''' page-page. [http://www.ncbi.nlm.nih.gov/sites/entrez/PMID PubMed] |
Revision as of 19:31, 13 June 2009
- Description: general stress protein, similar to epoxide hydrolase
Gene name | yfhM |
Synonyms | |
Essential | no |
Product | unknown |
Function | survival of ethanol stress |
MW, pI | 32 kDa, 6.064 |
Gene length, protein length | 858 bp, 286 aa |
Immediate neighbours | yfhL, csbB |
Get the DNA and protein sequences (Barbe et al., 2009) | |
Genetic context This image was kindly provided by SubtiList
|
Contents
The gene
Basic information
- Locus tag: BSU08590
Phenotypes of a mutant
Database entries
- DBTBS entry: [1]
- SubtiList entry: [2]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity:
- Protein family: AB hydrolase superfamily (according to Swiss-Prot)
- Paralogous protein(s):
Extended information on the protein
- Kinetic information:
- Domains:
- Modification:
- Cofactor(s):
- Effectors of protein activity:
- Interactions:
- Localization:
Database entries
- Structure:
- Swiss prot entry: O31581
- KEGG entry: [3]
- E.C. number:
Additional information
- subject to Clp-dependent proteolysis upon glucose starvation PubMed
Expression and regulation
- Operon:
- Regulatory mechanism:
- Additional information: subject to Clp-dependent proteolysis upon glucose starvation PubMed
Biological materials
- Mutant:
- Expression vector:
- lacZ fusion:
- GFP fusion:
- two-hybrid system:
- Antibody:
Labs working on this gene/protein
Your additional remarks
References
Dirk Höper, Uwe Völker, Michael Hecker
Comprehensive characterization of the contribution of individual SigB-dependent general stress genes to stress resistance of Bacillus subtilis.
J Bacteriol: 2005, 187(8);2810-26
[PubMed:15805528]
[WorldCat.org]
[DOI]
(P p)
H Antelmann, C Scharf, M Hecker
Phosphate starvation-inducible proteins of Bacillus subtilis: proteomics and transcriptional analysis.
J Bacteriol: 2000, 182(16);4478-90
[PubMed:10913081]
[WorldCat.org]
[DOI]
(P p)
X Huang, A Gaballa, M Cao, J D Helmann
Identification of target promoters for the Bacillus subtilis extracytoplasmic function sigma factor, sigma W.
Mol Microbiol: 1999, 31(1);361-71
[PubMed:9987136]
[WorldCat.org]
[DOI]
(P p)
- Höper et al. (2005) Comprehensive Characterization of the Contribution of Individual SigB-Dependent General Stress Genes to Stress Resistance of Bacillus subtilis. J. Bact. 187: 2810-2826 PubMed
- Gerth et al. (2008) Clp-dependent proteolysis down-regulates central metabolic pathways in glucose-starved Bacillus subtilis. J Bacteriol 190:321-331 PubMed
- Author1, Author2 & Author3 (year) Title Journal volume: page-page. PubMed