Difference between revisions of "YotD"
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|colspan="2" | '''Genetic context''' <br/> [[Image:yotD_context.gif]] | |colspan="2" | '''Genetic context''' <br/> [[Image:yotD_context.gif]] | ||
<div align="right"> <small>This image was kindly provided by [http://genolist.pasteur.fr/SubtiList/ SubtiList]</small></div> | <div align="right"> <small>This image was kindly provided by [http://genolist.pasteur.fr/SubtiList/ SubtiList]</small></div> | ||
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+ | |colspan="2" |'''[http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=yotD_2154887_2155018_-1 Expression at a glance]'''   {{PubMed|22383849}}<br/>[[Image:yotD_expression.png|500px]] | ||
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Revision as of 11:16, 19 April 2012
- Description: similar to acyl-CoA synthetase
Gene name | yotD |
Synonyms | |
Essential | no |
Product | unknown |
Function | unknown |
MW, pI | 4 kDa, 3.816 |
Gene length, protein length | 129 bp, 43 aa |
Immediate neighbours | yotE, yotC |
Get the DNA and protein sequences (Barbe et al., 2009) | |
Genetic context This image was kindly provided by SubtiList
| |
Expression at a glance PubMed |
Contents
Categories containing this gene/protein
SP-beta prophage, poorly characterized/ putative enzymes
This gene is a member of the following regulons
The gene
Basic information
- Locus tag: BSU19920
Phenotypes of a mutant
Database entries
- DBTBS entry: no entry
- SubtiList entry: [1]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity:
- Protein family:
- Paralogous protein(s):
Extended information on the protein
- Kinetic information:
- Domains:
- Modification:
- Cofactor(s): contains an iron-sulfur cluster
- Effectors of protein activity:
- Interactions:
- Localization:
Database entries
- Structure:
- UniProt: O34407
- KEGG entry: [2]
- E.C. number:
Additional information
Expression and regulation
- Operon:
- Sigma factor:
- 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
Shashi Chillappagari, Andreas Seubert, Hein Trip, Oscar P Kuipers, Mohamed A Marahiel, Marcus Miethke
Copper stress affects iron homeostasis by destabilizing iron-sulfur cluster formation in Bacillus subtilis.
J Bacteriol: 2010, 192(10);2512-24
[PubMed:20233928]
[WorldCat.org]
[DOI]
(I p)
Valentina Tosato, Alessandra M Albertini, Michela Zotti, Sabrina Sonda, Carlo V Bruschi
Sequence completion, identification and definition of the fengycin operon in Bacillus subtilis 168.
Microbiology (Reading): 1997, 143 ( Pt 11);3443-3450
[PubMed:9387222]
[WorldCat.org]
[DOI]
(P p)