Difference between revisions of "YodF"
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[[Category:Protein-coding genes]] | [[Category:Protein-coding genes]] |
Revision as of 09:23, 30 July 2015
- Description: similar to amino acid permease
Gene name | yodF |
Synonyms | |
Essential | no |
Product | unknown |
Function | unknown |
Gene expression levels in SubtiExpress: yodF | |
Metabolic function and regulation of this protein in SubtiPathways: YodF | |
MW, pI | 53 kDa, 9.682 |
Gene length, protein length | 1488 bp, 496 aa |
Immediate neighbours | yoyD, ctpA |
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
transporters/ other, putative amino acid transporter, membrane proteins
This gene is a member of the following regulons
The gene
Basic information
- Locus tag: BSU19580
Phenotypes of a mutant
Database entries
- BsubCyc: BSU19580
- DBTBS entry: no entry
- SubtiList entry: [1]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity:
- in some database, the protein is annotated as being similar to proline permease, however, it is not involved in proline transport PubMed
- Protein family: solute:sodium symporter family (SSS family)
- Paralogous protein(s): YhjB
Extended information on the protein
- Kinetic information:
- Modification:
- Effectors of protein activity:
- Localization:
- membrane PubMed
Database entries
- BsubCyc: BSU19580
- Structure:
- UniProt: O34745
- KEGG entry: [2]
- E.C. number:
Additional information
Expression and regulation
- Operon:
- Regulation: repressed by casamino acids PubMed
- Additional information:
Biological materials
- Mutant:
- available in Erhard Bremer's lab PubMed
- GP1887 (kan) available in Jörg Stülke's lab
- Expression vector:
- lacZ fusion:
- GFP fusion:
- two-hybrid system:
- Antibody:
Labs working on this gene/protein
Your additional remarks
References
Nicolas Mirouze, Elena Bidnenko, Philippe Noirot, Sandrine Auger
Genome-wide mapping of TnrA-binding sites provides new insights into the TnrA regulon in Bacillus subtilis.
Microbiologyopen: 2015, 4(3);423-35
[PubMed:25755103]
[WorldCat.org]
[DOI]
(I p)
Adrienne Zaprasis, Tamara Hoffmann, Lorena Stannek, Katrin Gunka, Fabian M Commichau, Erhard Bremer
The γ-aminobutyrate permease GabP serves as the third proline transporter of Bacillus subtilis.
J Bacteriol: 2014, 196(3);515-26
[PubMed:24142252]
[WorldCat.org]
[DOI]
(I p)
Hannes Hahne, Susanne Wolff, Michael Hecker, Dörte Becher
From complementarity to comprehensiveness--targeting the membrane proteome of growing Bacillus subtilis by divergent approaches.
Proteomics: 2008, 8(19);4123-36
[PubMed:18763711]
[WorldCat.org]
[DOI]
(I p)
Ken-ichi Yoshida, Hirotake Yamaguchi, Masaki Kinehara, Yo-hei Ohki, Yoshiko Nakaura, Yasutaro Fujita
Identification of additional TnrA-regulated genes of Bacillus subtilis associated with a TnrA box.
Mol Microbiol: 2003, 49(1);157-65
[PubMed:12823818]
[WorldCat.org]
[DOI]
(P p)
Ulrike Mäder, Georg Homuth, Christian Scharf, Knut Büttner, Rüdiger Bode, Michael Hecker
Transcriptome and proteome analysis of Bacillus subtilis gene expression modulated by amino acid availability.
J Bacteriol: 2002, 184(15);4288-95
[PubMed:12107147]
[WorldCat.org]
[DOI]
(P p)