Difference between revisions of "YxeB"
| Line 15: | Line 15: | ||
|style="background:#ABCDEF;" align="center"|'''Function''' || siderophore uptake  | |style="background:#ABCDEF;" align="center"|'''Function''' || siderophore uptake  | ||
|-  | |-  | ||
| − | |colspan="2" style="background:#FAF8CC;" align="center"| '''Gene expression levels in [http://  | + | |colspan="2" style="background:#FAF8CC;" align="center"| '''Gene expression levels in [http://subtiwiki.uni-goettingen.de/apps/expression/ ''Subti''Express]''': [http://subtiwiki.uni-goettingen.de/apps/expression/expression.php?search=BSU39610 yxeB]  | 
|-  | |-  | ||
|colspan="2" style="background:#FAF8CC;" align="center"| '''Interactions involving this protein in [http://cellpublisher.gobics.de/subtinteract/startpage/start/ ''Subt''Interact]''': [http://cellpublisher.gobics.de/subtinteract/interactionList/2/YxeB YxeB]  | |colspan="2" style="background:#FAF8CC;" align="center"| '''Interactions involving this protein in [http://cellpublisher.gobics.de/subtinteract/startpage/start/ ''Subt''Interact]''': [http://cellpublisher.gobics.de/subtinteract/interactionList/2/YxeB YxeB]  | ||
| Line 25: | Line 25: | ||
|style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[yxeC]]'', ''[[yxeA]]''  | |style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[yxeC]]'', ''[[yxeA]]''  | ||
|-  | |-  | ||
| − | |  | + | |style="background:#FAF8CC;" align="center"|'''Sequences'''||[http://bsubcyc.org/BSUB/sequence-aa?type=GENE&object=BSU39610 Protein] [http://bsubcyc.org/BSUB/sequence?type=GENE&object=BSU39610 DNA] [http://bsubcyc.org/BSUB/seq-selector?chromosome=CHROM-1&object=BSU39610 Advanced_DNA]  | 
|-  | |-  | ||
|-  | |-  | ||
Revision as of 14:15, 13 May 2013
-  Description: hydroxamate siderophore ABC transporter (only ferrioxamine) (binding  protein) 
 
| Gene name | yxeB | 
| Synonyms | |
| Essential | no | 
| Product |  hydroxamate siderophore ABC transporter
 
  | 
| Function | siderophore uptake | 
| Gene expression levels in SubtiExpress: yxeB | |
| Interactions involving this protein in SubtInteract: YxeB | |
| MW, pI | 35 kDa, 5.533 | 
| Gene length, protein length | 957 bp, 319 aa | 
| Immediate neighbours | yxeC, yxeA | 
| Sequences | Protein DNA Advanced_DNA | 
 Genetic context  
  This image was kindly provided by SubtiList 
 | |
Expression at a glance   PubMed 
 | |
Contents
Categories containing this gene/protein
ABC transporters, acquisition of iron, iron metabolism
This gene is a member of the following regulons
The gene
Basic information
- Locus tag: BSU39610
 
Phenotypes of a mutant
- no growth with the xenosiderophore ferrioxamine E as single source of iron PubMed
 
Database entries
- DBTBS entry: no entry
 
- SubtiList entry: [1]
 
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity:
 
- Protein family: bacterial solute-binding protein 8 family (according to Swiss-Prot)
 
- Paralogous protein(s):
 
Extended information on the protein
- Kinetic information:
 
- Domains:
 
- Modification:
 
- Cofactor(s):
 
- Effectors of protein activity:
 
Database entries
- Structure:
 
- UniProt: P54941
 
- KEGG entry: [2]
 
- E.C. number:
 
Additional information
Expression and regulation
- Operon: yxeB
 
- 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
Marcus Miethke, Timo Kraushaar, Mohamed A Marahiel  
Uptake of xenosiderophores in Bacillus subtilis occurs with high affinity and enhances the folding stabilities of substrate binding proteins. 
FEBS Lett: 2013, 587(2);206-13 
[PubMed:23220087]
  [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)
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)
Juliane Ollinger, Kyung-Bok Song, Haike Antelmann, Michael Hecker, John D Helmann  
Role of the Fur regulon in iron transport in Bacillus subtilis. 
J Bacteriol: 2006, 188(10);3664-73 
[PubMed:16672620]
  [WorldCat.org]
 [DOI]
 (P p)
Noel Baichoo, Tao Wang, Rick Ye, John D Helmann  
Global analysis of the Bacillus subtilis Fur regulon and the iron starvation stimulon. 
Mol Microbiol: 2002, 45(6);1613-29 
[PubMed:12354229]
  [WorldCat.org]
 [DOI]
 (P p)
Y Quentin, G Fichant, F Denizot  
Inventory, assembly and analysis of Bacillus subtilis ABC transport systems. 
J Mol Biol: 1999, 287(3);467-84 
[PubMed:10092453]
  [WorldCat.org]
 [DOI]
 (P p)

