Difference between revisions of "FeuA"

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(Basic information/ Evolution)
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* '''Locus tag:''' BSU01630
 
* '''Locus tag:''' BSU01630
 
+
[[Link title]]
 
===Phenotypes of a mutant ===
 
===Phenotypes of a mutant ===
  
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* '''Catalyzed reaction/biological activity:'''  
 
* '''Catalyzed reaction/biological activity:'''  
Substrate binding protein for the triscatecholate siderophores ferri-bacillibactin and ferri-enterobactin and part of the FeuABC-YusV ATP-binding cassette-type transporter. Furthermore ferric complexes of L-norepinephrine are bound by this protein.
+
Substrate binding protein for the triscatecholate siderophores ferri-bacillibactin and ferri-enterobactin and part of the [[FeuA]]-[[FeuB]]-[[FeuC]]-[[YusV]] ATP-binding cassette-type transporter. Furthermore ferric complexes of L-norepinephrine are bound by this protein.
  
 
* '''Protein family:''' Fe/B12 periplasmic-binding domain (according to Swiss-Prot)
 
* '''Protein family:''' Fe/B12 periplasmic-binding domain (according to Swiss-Prot)

Revision as of 08:52, 22 January 2010

  • 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

Link title

Phenotypes of a mutant

Database entries

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

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/biological activity:

Substrate binding protein for the triscatecholate siderophores ferri-bacillibactin and ferri-enterobactin and part of the FeuA-FeuB-FeuC-YusV ATP-binding cassette-type transporter. Furthermore ferric complexes of L-norepinephrine are bound by this protein.

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

Extended information on the protein

  • Kinetic information:
  • Domains:

Two independent non-symmetric globular domains, connected by a long alpha-helix (residues 143-164 of the mature protein).

  • 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

Mohamed Marahiel, Marburg University, Germany homepage

Your additional remarks

References

Marcus Miethke, Arne Skerra
Neutrophil gelatinase-associated lipocalin expresses antimicrobial activity by interfering with L-norepinephrine-mediated bacterial iron acquisition.
Antimicrob Agents Chemother: 2010, 54(4);1580-9
[PubMed:20086155] [WorldCat.org] [DOI] (I p)

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)

Rebecca J Abergel, Anna M Zawadzka, Trisha M Hoette, Kenneth N Raymond
Enzymatic hydrolysis of trilactone siderophores: where chiral recognition occurs in enterobactin and bacillibactin iron transport.
J Am Chem Soc: 2009, 131(35);12682-92
[PubMed:19673474] [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)