Difference between revisions of "YlxQ"
Line 1: | Line 1: | ||
− | * '''Description:''' similar to ribosomal protein, L7AE family <br/><br/> | + | * '''Description:''' similar to [[ribosomal protein]], L7AE family <br/><br/> |
{| align="right" border="1" cellpadding="2" | {| align="right" border="1" cellpadding="2" | ||
Line 54: | Line 54: | ||
* '''Catalyzed reaction/ biological activity:''' | * '''Catalyzed reaction/ biological activity:''' | ||
− | * '''Protein family:''' ribosomal protein L7Ae family (according to Swiss-Prot) | + | * '''Protein family:''' [[ribosomal protein]] L7Ae family (according to Swiss-Prot) |
* '''Paralogous protein(s):''' | * '''Paralogous protein(s):''' |
Revision as of 17:55, 3 November 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)