Difference between revisions of "YoaW"
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| − | |colspan="2" |'''[http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=yoaW_2046980_2047411_-1 Expression at a glance]'''   {{PubMed|22383849}}<br/>[[Image:yoaW_expression.png|500px]] | + | |colspan="2" |'''[http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=yoaW_2046980_2047411_-1 Expression at a glance]'''   {{PubMed|22383849}}<br/>[[Image:yoaW_expression.png|500px|link=http://subtiwiki.uni-goettingen.de/apps/expression/expression.php?search=BSU18780]] |
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Revision as of 13:32, 16 May 2013
- Description: unknown
| Gene name | yoaW |
| Synonyms | |
| Essential | no |
| Product | unknown |
| Function | unknown |
| Gene expression levels in SubtiExpress: yoaW | |
| MW, pI | 16 kDa, 5.159 |
| Gene length, protein length | 429 bp, 143 aa |
| Immediate neighbours | yoaV, yoaZ |
| Sequences | Protein DNA DNA_with_flanks |
Genetic context 
This image was kindly provided by SubtiList
| |
Expression at a glance PubMed
| |
Contents
Categories containing this gene/protein
This gene is a member of the following regulons
The gene
Basic information
- Locus tag: BSU18780
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: eamA transporter family (according to Swiss-Prot)
- Paralogous protein(s):
Extended information on the protein
- Kinetic information:
- Domains:
- Modification:
- Cofactor(s):
- Effectors of protein activity:
- Localization:
- cell membrane (according to Swiss-Prot)
- extracellular (signal peptide) PubMed
Database entries
- Structure:
- UniProt: O34541
- KEGG entry: [3]
- E.C. number:
Additional information
Expression and regulation
- Regulation:
- Additional information:
Biological materials
- Expression vector:
- lacZ fusion:
- GFP fusion:
- two-hybrid system:
- Antibody:
Labs working on this gene/protein
Your additional remarks
References
Christian Degering, Thorsten Eggert, Michael Puls, Johannes Bongaerts, Stefan Evers, Karl-Heinz Maurer, Karl-Erich Jaeger
Optimization of protease secretion in Bacillus subtilis and Bacillus licheniformis by screening of homologous and heterologous signal peptides.
Appl Environ Microbiol: 2010, 76(19);6370-6
[PubMed:20709850]
[WorldCat.org]
[DOI]
(I p)
Birgit Voigt, Haike Antelmann, Dirk Albrecht, Armin Ehrenreich, Karl-Heinz Maurer, Stefan Evers, Gerhard Gottschalk, Jan Maarten van Dijl, Thomas Schweder, Michael Hecker
Cell physiology and protein secretion of Bacillus licheniformis compared to Bacillus subtilis.
J Mol Microbiol Biotechnol: 2009, 16(1-2);53-68
[PubMed:18957862]
[WorldCat.org]
[DOI]
(I p)
Mélanie A Hamon, Nicola R Stanley, Robert A Britton, Alan D Grossman, Beth A Lazazzera
Identification of AbrB-regulated genes involved in biofilm formation by Bacillus subtilis.
Mol Microbiol: 2004, 52(3);847-60
[PubMed:15101989]
[WorldCat.org]
[DOI]
(P p)
P N Rather, R E Hay, G L Ray, W G Haldenwang, C P Moran
Nucleotide sequences that define promoters that are used by Bacillus subtilis sigma-29 RNA polymerase.
J Mol Biol: 1986, 192(3);557-65
[PubMed:3104598]
[WorldCat.org]
[DOI]
(P p)
