Difference between revisions of "YlxQ"
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=Expression and regulation= | =Expression and regulation= | ||
− | * '''Operon:''' | + | * '''Operon:''' ''[[ylxS]]-[[nusA]]-[[ylxR]]-[[ylxQ]]-[[infB]]-[[ylxP]]-[[rbfA]]'' {{PubMed|8491709}} |
− | * '''[[Sigma factor]]:''' | + | * '''[[Sigma factor]]:''' [[SigA]] {{PubMed|8491709}} |
* '''Regulation:''' | * '''Regulation:''' | ||
Line 118: | Line 118: | ||
=References= | =References= | ||
− | + | <pubmed>11948165 8491709 </pubmed> | |
[[Category:Protein-coding genes]] | [[Category:Protein-coding genes]] |
Revision as of 19:14, 16 October 2009
- Description: similar to ribosomal protein, L7AE family
Gene name | ylxQ |
Synonyms | ymxC |
Essential | no |
Product | unknown |
Function | unknown |
MW, pI | 10 kDa, 10.166 |
Gene length, protein length | 300 bp, 100 aa |
Immediate neighbours | ylxR, infB |
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: BSU16620
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: ribosomal protein L7Ae 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: P32729
- KEGG entry: [3]
- E.C. number:
Additional information
Expression and 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
Christine Eymann, Georg Homuth, Christian Scharf, Michael Hecker
Bacillus subtilis functional genomics: global characterization of the stringent response by proteome and transcriptome analysis.
J Bacteriol: 2002, 184(9);2500-20
[PubMed:11948165]
[WorldCat.org]
[DOI]
(P p)
K Shazand, J Tucker, M Grunberg-Manago, J C Rabinowitz, T Leighton
Similar organization of the nusA-infB operon in Bacillus subtilis and Escherichia coli.
J Bacteriol: 1993, 175(10);2880-7
[PubMed:8491709]
[WorldCat.org]
[DOI]
(P p)