FeuA

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
Get the DNA and protein sequences (Barbe et al., 2009)
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)