Difference between revisions of "FeuA"

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(Database entries)
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=== Database entries ===
 
=== Database entries ===
  
* '''Structure:''' [http://www.rcsb.org/pdb/explore.do?structureId=2PHZ 2PHZ], [http://www.rcsb.org/pdb/explore.do?structureId=2WHY 2WHY] (complex with ferri-bacillibactin)
+
* '''Structure:''' [http://www.rcsb.org/pdb/explore.do?structureId=2PHZ 2PHZ], [http://www.rcsb.org/pdb/explore.do?structureId=2WI8 2WI8], [http://www.rcsb.org/pdb/explore.do?structureId=2WHY 2WHY] (complex with ferri-bacillibactin)
  
 
* '''UniProt:''' [http://www.uniprot.org/uniprot/P40409 P40409]
 
* '''UniProt:''' [http://www.uniprot.org/uniprot/P40409 P40409]
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=References=
 
=References=
  
<pubmed>14563870,16672620,10092453,16889643,17725565,12354229,18957862 18763711, </pubmed>
+
<pubmed>19746494,14563870,16672620,10092453,16889643,17725565,12354229,18957862 18763711, </pubmed>
  
 
[[Category:Protein-coding genes]]
 
[[Category:Protein-coding genes]]

Revision as of 09:54, 14 October 2009

  • Description: ABC-transporter for the siderophores enterobactin and bacillibactin (binding protein), with YusV as ATPase

Gene name feuA
Synonyms
Essential no
Product ABC-transporter for the siderophores enterobactin
and bacillibactin (binding protein)
Function iron acquisition
Metabolic function and regulation of this protein in SubtiPathways:
Stress
MW, pI 34 kDa, 8.018
Gene length, protein length 951 bp, 317 aa
Immediate neighbours feuB, btr
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
FeuA context.gif
This image was kindly provided by SubtiList







The gene

Basic information

  • Locus tag: BSU01630

Phenotypes of a mutant

Database entries

  • DBTBS entry: [1]
  • SubtiList entry: [2]

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity:
  • Protein family: Fe/B12 periplasmic-binding domain (according to Swiss-Prot)
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification:
  • Cofactor(s):
  • Effectors of protein activity:
  • Interactions:
  • Localization: cell membrane (according to Swiss-Prot), extracellular (signal peptide) PubMed, membrane PubMed

Database entries

  • Structure: 2PHZ, 2WI8, 2WHY (complex with ferri-bacillibactin)
  • KEGG entry: [3]
  • E.C. number:

Additional information

Expression and regulation

  • Regulation:
    • repressed in the presence of iron (Fur, CitB) PubMed
    • induced in the presence of iron chelators bacillibactin or enterobactin (Btr) PubMed
  • Regulatory mechanism:
    • Fur: transcription repression PubMed
    • CitB: binding to the iron responsive element in the absence of iron
    • Btr: transcription activation in the presence of the co-activators bacillibactin or enterobactin PubMed
  • 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

Florian Peuckert, Marcus Miethke, Alexander G Albrecht, Lars-Oliver Essen, Mohamed A Marahiel
Structural basis and stereochemistry of triscatecholate siderophore binding by FeuA.
Angew Chem Int Ed Engl: 2009, 48(42);7924-7
[PubMed:19746494] [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)

Ahmed Gaballa, John D Helmann
Substrate induction of siderophore transport in Bacillus subtilis mediated by a novel one-component regulator.
Mol Microbiol: 2007, 66(1);164-73
[PubMed:17725565] [WorldCat.org] [DOI] (P p)

Marcus Miethke, Oliver Klotz, Uwe Linne, Jürgen J May, Carsten L Beckering, Mohamed A Marahiel
Ferri-bacillibactin uptake and hydrolysis in Bacillus subtilis.
Mol Microbiol: 2006, 61(6);1413-27
[PubMed:16889643] [WorldCat.org] [DOI] (P 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)

Mayuree Fuangthong, John D Helmann
Recognition of DNA by three ferric uptake regulator (Fur) homologs in Bacillus subtilis.
J Bacteriol: 2003, 185(21);6348-57
[PubMed:14563870] [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)