EfeB

• Description: elemental iron uptake system, heme peroxidase, converts ferrous iron (Fe(II) to ferric iron (FeIII)) for uptake by EfeO-EfeU, peroxide detoxification under microaerobic conditions
  
  

Gene name	efeB
Synonyms	ipa-29d, ywbN
Essential	no
Product	heme peroxidase in elemental iron uptake
Function	ferrous iron conversion
Gene expression levels in SubtiExpress: efeB
Interactions involving this protein in SubtInteract: EfeB
Metabolic function and regulation of this protein in SubtiPathways: Protein secretion
MW, pI	45 kDa, 8.64
Gene length, protein length	1248 bp, 416 aa
Immediate neighbours	ywbO, efeO
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

acquisition of iron, iron metabolism, cell envelope stress proteins (controlled by SigM, V, W, X, Y), resistance against oxidative and electrophile stress, membrane proteins

This gene is a member of the following regulons

Fur regulon, SigM regulon, SigW regulon, SigX regulon

The gene

Basic information

• Locus tag: BSU38260

Database entries

• DBTBS entry: [1]

• SubtiList entry: [2]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity:
  • oxidizes ferrous iron to ferric iron for uptake by EfeO-EfeU PubMed
  • eliminates reactive oxygen species that accumulate in the presence of ferrous iron PubMed
  • peroxide detoxification under microaerobic conditions PubMed

• Protein family: DyP-type peroxidase family (according to Swiss-Prot)

• Paralogous protein(s):

Extended information on the protein

• Kinetic information:

• Domains:

• Modification:

• Cofactors:
  • protoheme IX PubMed

• Effectors of protein activity:
  • activity is increased in the presence of EfeO due to the displacement of ferric iron PubMed

• Interactions:
  • EfeO-EfeU-EfeB PubMed

• Localization:
  • extracellular, secreted by the TatAY-TatCY complex PubMed
  • TatAY-TatCY-dependent export of EfeB requires a functional WprA PubMed
  • forms a membrane-bound complex with EfeU and EfeO for iron uptake PubMed
  • attached to the membrane via EfeU PubMed

Database entries

• Structure:

• UniProt: P39597

• KEGG entry: [3]

• E.C. number:

Expression and regulation

• Operon:
  • efeU-efeO-efeB PubMed
  • efeB-ywbO PubMed

• Expression browser: efeB PubMed

• Sigma factor:
  • efeU: SigA PubMed
  • efeB: SigM PubMed, SigX, SigW PubMed

• Regulation:
  • induced upon iron starvation (Fur) PubMed

• Regulatory mechanism:
  • Fur: transcription repression PubMed

• Additional information:

Biological materials

• Mutant:

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

Labs working on this gene/protein

Jan Maarten van Dijl, Groningen, Netherlands

References

Original publications

Ruihua Liu, Zhenqiang Zuo, Yingming Xu, Cunjiang Song, Hong Jiang, Chuanling Qiao, Ping Xu, Qixing Zhou, Chao Yang
Twin-arginine signal peptide of Bacillus subtilis YwbN can direct Tat-dependent secretion of methyl parathion hydrolase.
J Agric Food Chem: 2014, 62(13);2913-8
[PubMed:24620988] [WorldCat.org] [DOI] (I p)

Ana Santos, Sónia Mendes, Vânia Brissos, Lígia O Martins
New dye-decolorizing peroxidases from Bacillus subtilis and Pseudomonas putida MET94: towards biotechnological applications.
Appl Microbiol Biotechnol: 2014, 98(5);2053-65
[PubMed:23820555] [WorldCat.org] [DOI] (I p)

Marcus Miethke, Carmine G Monteferrante, Mohamed A Marahiel, Jan Maarten van Dijl
The Bacillus subtilis EfeUOB transporter is essential for high-affinity acquisition of ferrous and ferric iron.
Biochim Biophys Acta: 2013, 1833(10);2267-78
[PubMed:23764491] [WorldCat.org] [DOI] (P p)

Murat Sezer, Ana Santos, Patrycja Kielb, Tiago Pinto, Ligia O Martins, Smilja Todorovic
Distinct structural and redox properties of the heme active site in bacterial dye decolorizing peroxidase-type peroxidases from two subfamilies: resonance Raman and electrochemical study.
Biochemistry: 2013, 52(18);3074-84
[PubMed:23560556] [WorldCat.org] [DOI] (I p)

Carmine G Monteferrante, Calum MacKichan, Elodie Marchadier, Maria-Victoria Prejean, Rut Carballido-López, Jan Maarten van Dijl
Mapping the twin-arginine protein translocation network of Bacillus subtilis.
Proteomics: 2013, 13(5);800-11
[PubMed:23180473] [WorldCat.org] [DOI] (I p)

Laxmi Krishnappa, Carmine G Monteferrante, Jan Maarten van Dijl
Degradation of the twin-arginine translocation substrate YwbN by extracytoplasmic proteases of Bacillus subtilis.
Appl Environ Microbiol: 2012, 78(21);7801-4
[PubMed:22923395] [WorldCat.org] [DOI] (I p)

René van der Ploeg, Ulrike Mäder, Georg Homuth, Marc Schaffer, Emma L Denham, Carmine G Monteferrante, Marcus Miethke, Mohamed A Marahiel, Colin R Harwood, Theresa Winter, Michael Hecker, Haike Antelmann, Jan Maarten van Dijl
Environmental salinity determines the specificity and need for Tat-dependent secretion of the YwbN protein in Bacillus subtilis.
PLoS One: 2011, 6(3);e18140
[PubMed:21479178] [WorldCat.org] [DOI] (I e)

Robyn T Eijlander, Magdalena A Kolbusz, Erwin M Berendsen, Oscar P Kuipers
Effects of altered TatC proteins on protein secretion efficiency via the twin-arginine translocation pathway of Bacillus subtilis.
Microbiology (Reading): 2009, 155(Pt 6);1776-1785
[PubMed:19383693] [WorldCat.org] [DOI] (P p)

Thijs R H M Kouwen, René van der Ploeg, Haike Antelmann, Michael Hecker, Georg Homuth, Ulrike Mäder, Jan Maarten van Dijl
Overflow of a hyper-produced secretory protein from the Bacillus Sec pathway into the Tat pathway for protein secretion as revealed by proteogenomics.
Proteomics: 2009, 9(4);1018-32
[PubMed:19180538] [WorldCat.org] [DOI] (I p)

Marc A B Kolkman, René van der Ploeg, Michael Bertels, Maurits van Dijk, Joop van der Laan, Jan Maarten van Dijl, Eugenio Ferrari
The twin-arginine signal peptide of Bacillus subtilis YwbN can direct either Tat- or Sec-dependent secretion of different cargo proteins: secretion of active subtilisin via the B. subtilis Tat pathway.
Appl Environ Microbiol: 2008, 74(24);7507-13
[PubMed:18931290] [WorldCat.org] [DOI] (I p)

Warawan Eiamphungporn, John D Helmann
The Bacillus subtilis sigma(M) regulon and its contribution to cell envelope stress responses.
Mol Microbiol: 2008, 67(4);830-48
[PubMed:18179421] [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)

Jan D H Jongbloed, Ulrike Grieger, Haike Antelmann, Michael Hecker, Reindert Nijland, Sierd Bron, Jan Maarten van Dijl
Two minimal Tat translocases in Bacillus.
Mol Microbiol: 2004, 54(5);1319-25
[PubMed:15554971] [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)

X Huang, K L Fredrick, J D Helmann
Promoter recognition by Bacillus subtilis sigmaW: autoregulation and partial overlap with the sigmaX regulon.
J Bacteriol: 1998, 180(15);3765-70
[PubMed:9683469] [WorldCat.org] [DOI] (P p)

E Presecan, I Moszer, L Boursier, H Cruz Ramos, V de la Fuente, M-F Hullo, C Lelong, S Schleich, A Sekowska, B H Song, G Villani, F Kunst, A Danchin, P Glaser
The Bacillus subtilis genome from gerBC (311 degrees) to licR (334 degrees).
Microbiology (Reading): 1997, 143 ( Pt 10);3313-3328
[PubMed:9353933] [WorldCat.org] [DOI] (P p)