Difference between revisions of "YotD"
(→Extended information on the protein) |
|||
| Line 93: | Line 93: | ||
* '''Regulation:''' | * '''Regulation:''' | ||
| + | ** 11-fold induced by copper stress ([[CsoR]]) {{PubMed|20233928}} | ||
* '''Regulatory mechanism:''' | * '''Regulatory mechanism:''' | ||
| + | ** [[CsoR]]: transcription repression {{PubMed|20233928}} | ||
* '''Additional information:''' | * '''Additional information:''' | ||
| Line 118: | Line 120: | ||
=References= | =References= | ||
| − | <pubmed>,9387222, </pubmed> | + | <pubmed>,9387222, 20233928 </pubmed> |
[[Category:Protein-coding genes]] | [[Category:Protein-coding genes]] | ||
Revision as of 11:54, 18 March 2010
- 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
| |
Contents
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:
- 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)
