FeuA

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

Gene name	feuA
Synonyms
Essential	no
Product	ABC transporter for the siderophores Fe-enterobactin and Fe-bacillibactin (binding protein)
Function	acquisition of iron
Gene expression levels in SubtiExpress: feuA
Interactions involving this protein in SubtInteract: FeuA
Metabolic function and regulation of this protein in SubtiPathways: Stress, Metal ion homeostasis
MW, pI	34 kDa, 8.018
Gene length, protein length	951 bp, 317 aa
Immediate neighbours	feuB, btr
Sequences	Protein DNA DNA_with_flanks
Genetic context This image was kindly provided by SubtiList
Expression at a glance   PubMed

Categories containing this gene/protein

ABC transporters, acquisition of iron, iron metabolism, membrane proteins

This gene is a member of the following regulons

Btr regulon, CitB regulon, Fur regulon

The gene

Basic information

• Locus tag: BSU01630

Database entries

• DBTBS entry: [1]

• SubtiList entry: [2]

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:
  • FeuA is a lipoprotein with a N-acetyl-S-diacyl-glyceryl-cysteine structure PubMed

• Cofactor(s):

• Effectors of protein activity:

• Interactions:
  • YusV-(FeuB-FeuC)-FeuA PubMed

• Localization:
  • associated to the membrane (lipoprotein) PubMed
  • extracellular (signal peptide) PubMed

Database entries

• Structure: 2PHZ, 2WI8, 2WHY (complex with ferri-bacillibactin), 2XUZ (complex with ferri-enterobactin), 2XV1 (complex with ferric mecam)

• UniProt: P40409

• KEGG entry: [3]

• E.C. number:

Expression and regulation

• Operon: feuA-feuB-feuC-ybbA PubMed

• Expression browser: feuA PubMed

• Sigma factor: SigA PubMed

• 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:

References

Additional publications: PubMed

Kenji Kurokawa, Kyoung-Hwa Ryu, Rie Ichikawa, Akiko Masuda, Min-Su Kim, Hanna Lee, Jun-Ho Chae, Takashi Shimizu, Tatsuya Saitoh, Koichi Kuwano, Shizuo Akira, Naoshi Dohmae, Hiroshi Nakayama, Bok Luel Lee
Novel bacterial lipoprotein structures conserved in low-GC content gram-positive bacteria are recognized by Toll-like receptor 2.
J Biol Chem: 2012, 287(16);13170-81
[PubMed:22303020] [WorldCat.org] [DOI] (I p)

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)