Difference between revisions of "YhxA"
| Line 98: | Line 98: | ||
:* subject to Clp-dependent proteolysis upon glucose starvation [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Abstract&list_uids=+17981983 PubMed] | :* subject to Clp-dependent proteolysis upon glucose starvation [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Abstract&list_uids=+17981983 PubMed] | ||
=Expression and regulation= | =Expression and regulation= | ||
| − | |||
* '''Operon:''' ''[[yhxA]]-[[glpP]]'' {{PubMed|2127799}} | * '''Operon:''' ''[[yhxA]]-[[glpP]]'' {{PubMed|2127799}} | ||
| − | * '''[[Sigma factor]]:''' | + | * '''[[Sigma factor]]:''' [[SigA]] {{PubMed|21925382}} |
* '''Regulation:''' | * '''Regulation:''' | ||
| Line 107: | Line 106: | ||
* '''Regulatory mechanism:''' | * '''Regulatory mechanism:''' | ||
| − | * '''Additional information:''' subject to Clp-dependent proteolysis upon glucose starvation {{PubMed|17981983}} | + | * '''Additional information:''' |
| + | ** half-life of the mRNA: 3.7 min {{PubMed|21925382}} | ||
| + | ** the mRNA is stabilized in '' [[rppH]]'' and ''[[rnjA]]'' mutants {{PubMed|21925382}} | ||
| + | ** the mRNA is subject to degradation by [[RNase J1|rnjA]] {{PubMed|21925382}} | ||
| + | ** subject to Clp-dependent proteolysis upon glucose starvation {{PubMed|17981983}} | ||
=Biological materials = | =Biological materials = | ||
| Line 128: | Line 131: | ||
=References= | =References= | ||
| − | <pubmed>17981983 2127799 </pubmed> | + | <pubmed>17981983 2127799 21925382</pubmed> |
[[Category:Protein-coding genes]] | [[Category:Protein-coding genes]] | ||
Revision as of 16:01, 20 September 2011
- Description: similar to adenosylmethionine-8-amino-7-oxononanoate aminotransferase
| Gene name | yhxA |
| Synonyms | |
| Essential | no |
| Product | unknown |
| Function | unknown |
| MW, pI | 49 kDa, 5.644 |
| Gene length, protein length | 1350 bp, 450 aa |
| Immediate neighbours | yhcX, glpP |
| 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
poorly characterized/ putative enzymes
This gene is a member of the following regulons
The gene
Basic information
- Locus tag: BSU09260
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: class-III pyridoxal-phosphate-dependent aminotransferase family (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:
- UniProt: P33189
- KEGG entry: [3]
- E.C. number:
Additional information
- subject to Clp-dependent proteolysis upon glucose starvation PubMed
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
Jamie Richards, Quansheng Liu, Olivier Pellegrini, Helena Celesnik, Shiyi Yao, David H Bechhofer, Ciarán Condon, Joel G Belasco
An RNA pyrophosphohydrolase triggers 5'-exonucleolytic degradation of mRNA in Bacillus subtilis.
Mol Cell: 2011, 43(6);940-9
[PubMed:21925382]
[WorldCat.org]
[DOI]
(I p)
Ulf Gerth, Holger Kock, Ilja Kusters, Stephan Michalik, Robert L Switzer, Michael Hecker
Clp-dependent proteolysis down-regulates central metabolic pathways in glucose-starved Bacillus subtilis.
J Bacteriol: 2008, 190(1);321-31
[PubMed:17981983]
[WorldCat.org]
[DOI]
(I p)
C Holmberg, L Beijer, B Rutberg, L Rutberg
Glycerol catabolism in Bacillus subtilis: nucleotide sequence of the genes encoding glycerol kinase (glpK) and glycerol-3-phosphate dehydrogenase (glpD).
J Gen Microbiol: 1990, 136(12);2367-75
[PubMed:2127799]
[WorldCat.org]
[DOI]
(P p)
