Difference between revisions of "YxeB"

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* no growth with the xenosiderophore ferrioxamine E as single source of iron {{PubMed|23220087}}  
 
* no growth with the xenosiderophore ferrioxamine E as single source of iron {{PubMed|23220087}}  
 
=== Database entries ===
 
=== Database entries ===
 +
* '''BsubCyc:''' [http://bsubcyc.org/BSUB/NEW-IMAGE?type=NIL&object=BSU39610&redirect=T BSU39610]
  
 
* '''DBTBS entry:''' no entry
 
* '''DBTBS entry:''' no entry
Line 99: Line 100:
  
 
=== Database entries ===
 
=== Database entries ===
 +
* '''BsubCyc:''' [http://bsubcyc.org/BSUB/NEW-IMAGE?type=NIL&object=BSU39610&redirect=T BSU39610]
  
 
* '''Structure:'''
 
* '''Structure:'''

Revision as of 15:13, 2 April 2014

  • Description: hydroxamate siderophore ABC transporter (only ferrioxamine) (binding protein)

Gene name yxeB
Synonyms
Essential no
Product hydroxamate siderophore ABC transporter


(only ferrioxamine) (binding protein)

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 DNA_with_flanks
Genetic context
YxeB context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
YxeB expression.png















Categories containing this gene/protein

ABC transporters, acquisition of iron, iron metabolism

This gene is a member of the following regulons

Fur regulon

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:
  • KEGG entry: [2]
  • E.C. number:

Additional information

Expression and regulation

  • Sigma factor:
  • Regulation:
    • repressed unless the cells enter an iron starvation (Fur) PubMed
  • Regulatory mechanism:
  • 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)