Difference between revisions of "YwlE"

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(References)
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**''ywlE::tet'' available from [[Ulf Gerth]]'s lab
 
**''ywlE::tet'' available from [[Ulf Gerth]]'s lab
 
**''ywlE::spec'' available from [[Ulf Gerth]]'s lab
 
**''ywlE::spec'' available from [[Ulf Gerth]]'s lab
**GP1458 (''ywlE''::''aphA3''), available in [[Jörg Stülke]]'s lab
+
** GP1458 (''ywlE''::''aphA3''), available in [[Jörg Stülke]]'s lab
**GP1459 (''ywlE''::''tet''), available in [[Jörg Stülke]]'s lab
+
** GP1459 (''ywlE''::''tet''), available in [[Jörg Stülke]]'s and [[Fabian Commichau]]'s labs {{PubMed|25610436}}
  
 
* '''Expression vector:''' for expression, purification in E. coli with N-terminal His-tag, pRSETA available in [[Ulf Gerth]]'s lab
 
* '''Expression vector:''' for expression, purification in E. coli with N-terminal His-tag, pRSETA available in [[Ulf Gerth]]'s lab
Line 140: Line 140:
 
=Labs working on this gene/protein=
 
=Labs working on this gene/protein=
 
* [[Ulf Gerth]], Greifswald, Germany
 
* [[Ulf Gerth]], Greifswald, Germany
 
 
* [[Fabian Commichau]] Göttingen, Germany
 
* [[Fabian Commichau]] Göttingen, Germany
  
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=References=
 
=References=
  
<pubmed>16452434,15866923,15995210,19678837 21622759, 20852588 22517742 23770242 23838530 24263382 24825175 </pubmed>
+
<pubmed>16452434,15866923,15995210,19678837 21622759, 20852588 22517742 23770242 23838530 24263382 24825175 25610436</pubmed>
  
 
[[Category:Protein-coding genes]]
 
[[Category:Protein-coding genes]]

Revision as of 09:06, 23 January 2015

Gene name ywlE
Synonyms ipc-31d
Essential no
Product protein arginine phosphatase
Function dephosphorylation of McsB
Gene expression levels in SubtiExpress: ywlE
MW, pI 16 kDa, 6.681
Gene length, protein length 450 bp, 150 aa
Immediate neighbours ywlF, ywlD
Sequences Protein DNA DNA_with_flanks
Genetic context
YwlE context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
YwlE expression.png















Categories containing this gene/protein

protein modification

This gene is a member of the following regulons

The gene

Basic information

  • Locus tag: BSU36930

Phenotypes of a mutant

Database entries

  • DBTBS entry: no entry
  • SubtiList entry: [1]

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: Protein arginine phosphate + H2O = protein arginine + phosphate PubMed
  • Protein family:
  • Paralogous protein(s): YfkJ

Extended information on the protein

  • Kinetic information:
  • Modification:
  • Effectors of protein activity:

Database entries

  • KEGG entry: [2]

Additional information

Expression and regulation

  • Operon:
  • Regulation:
  • Regulatory mechanism:
  • Additional information:
    • number of protein molecules per cell (minimal medium with glucose and ammonium): 91 PubMed
    • number of protein molecules per cell (complex medium with amino acids, without glucose): 272 PubMed

Biological materials

  • Expression vector: for expression, purification in E. coli with N-terminal His-tag, pRSETA available in Ulf Gerth's lab
  • lacZ fusion:
  • GFP fusion:
  • two-hybrid system:

Labs working on this gene/protein

Your additional remarks

References

Lorena Stannek, Katrin Gunka, Rachel A Care, Ulf Gerth, Fabian M Commichau
Factors that mediate and prevent degradation of the inactive and unstable GudB protein in Bacillus subtilis.
Front Microbiol: 2014, 5;758
[PubMed:25610436] [WorldCat.org] [DOI] (P e)

Débora Broch Trentini, Jakob Fuhrmann, Karl Mechtler, Tim Clausen
Chasing Phosphoarginine Proteins: Development of a Selective Enrichment Method Using a Phosphatase Trap.
Mol Cell Proteomics: 2014, 13(8);1953-64
[PubMed:24825175] [WorldCat.org] [DOI] (I p)

Andreas Schmidt, Débora Broch Trentini, Silvia Spiess, Jakob Fuhrmann, Gustav Ammerer, Karl Mechtler, Tim Clausen
Quantitative phosphoproteomics reveals the role of protein arginine phosphorylation in the bacterial stress response.
Mol Cell Proteomics: 2014, 13(2);537-50
[PubMed:24263382] [WorldCat.org] [DOI] (I p)

Jakob Fuhrmann, Venkataraman Subramanian, Paul R Thompson
Targeting the arginine phosphatase YwlE with a catalytic redox-based inhibitor.
ACS Chem Biol: 2013, 8(9);2024-32
[PubMed:23838530] [WorldCat.org] [DOI] (I p)

Jakob Fuhrmann, Beata Mierzwa, Débora B Trentini, Silvia Spiess, Anita Lehner, Emmanuelle Charpentier, Tim Clausen
Structural basis for recognizing phosphoarginine and evolving residue-specific protein phosphatases in gram-positive bacteria.
Cell Rep: 2013, 3(6);1832-9
[PubMed:23770242] [WorldCat.org] [DOI] (I p)

Alexander K W Elsholz, Kürsad Turgay, Stephan Michalik, Bernd Hessling, Katrin Gronau, Dan Oertel, Ulrike Mäder, Jörg Bernhardt, Dörte Becher, Michael Hecker, Ulf Gerth
Global impact of protein arginine phosphorylation on the physiology of Bacillus subtilis.
Proc Natl Acad Sci U S A: 2012, 109(19);7451-6
[PubMed:22517742] [WorldCat.org] [DOI] (I p)

A K W Elsholz, K Hempel, S Michalik, K Gronau, D Becher, M Hecker, U Gerth
Activity control of the ClpC adaptor McsB in Bacillus subtilis.
J Bacteriol: 2011, 193(15);3887-93
[PubMed:21622759] [WorldCat.org] [DOI] (I p)

Alexander K W Elsholz, Stephan Michalik, Daniela Zühlke, Michael Hecker, Ulf Gerth
CtsR, the Gram-positive master regulator of protein quality control, feels the heat.
EMBO J: 2010, 29(21);3621-9
[PubMed:20852588] [WorldCat.org] [DOI] (I p)

Jascha Blobel, Pau Bernadó, Huimin Xu, Changwen Jin, Miquel Pons
Weak oligomerization of low-molecular-weight protein tyrosine phosphatase is conserved from mammals to bacteria.
FEBS J: 2009, 276(16);4346-57
[PubMed:19678837] [WorldCat.org] [DOI] (I p)

Huimin Xu, Bin Xia, Changwen Jin
Solution structure of a low-molecular-weight protein tyrosine phosphatase from Bacillus subtilis.
J Bacteriol: 2006, 188(4);1509-17
[PubMed:16452434] [WorldCat.org] [DOI] (P p)

Lucia Musumeci, Cristina Bongiorni, Lutz Tautz, Robert A Edwards, Andrei Osterman, Marta Perego, Tomas Mustelin, Nunzio Bottini
Low-molecular-weight protein tyrosine phosphatases of Bacillus subtilis.
J Bacteriol: 2005, 187(14);4945-56
[PubMed:15995210] [WorldCat.org] [DOI] (P p)

Ivan Mijakovic, Lucia Musumeci, Lutz Tautz, Dina Petranovic, Robert A Edwards, Peter Ruhdal Jensen, Tomas Mustelin, Josef Deutscher, Nunzio Bottini
In vitro characterization of the Bacillus subtilis protein tyrosine phosphatase YwqE.
J Bacteriol: 2005, 187(10);3384-90
[PubMed:15866923] [WorldCat.org] [DOI] (P p)