Difference between revisions of "EfeB"

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=References=
 
=References=
 
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<pubmed>16672620,19180538,12354229, 19383693 9353933 9683469 15554971 21479178 18179421 22923395 23180473 23560556 </pubmed>
<pubmed>16672620,19180538,12354229, 19383693 9353933 9683469 15554971 21479178 18179421 22923395 23180473</pubmed>
 
  
 
[[Category:Protein-coding genes]]
 
[[Category:Protein-coding genes]]

Revision as of 12:51, 15 April 2013

  • Description: elemental iron uptake system (binding protein)

Gene name ywbN
Synonyms ipa-29d
Essential no
Product elemental iron uptake system (binding protein)
Function iron uptake
Gene expression levels in SubtiExpress: ywbN
Interactions involving this protein in SubtInteract: YwbN
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, ywbM
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
YwbN context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
YwbN expression.png















Categories containing this gene/protein

transporters/ other, acquisition of iron, iron metabolism, cell envelope stress proteins (controlled by SigM, V, W, X, Y), 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

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: DyP-type peroxidase family (according to Swiss-Prot)
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification:
  • Cofactor(s):
  • Effectors of protein activity:

Database entries

  • Structure:
  • KEGG entry: [3]
  • E.C. number:

Additional information

Expression and regulation

  • Regulation:
  • Regulatory mechanism:
  • 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

Your additional remarks

References

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)

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)