YwlE

• Description: protein arginine phosphatase
  
  

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 This image was kindly provided by SubtiList
Expression at a glance   PubMed

Categories containing this gene/protein

protein modification

The gene

Basic information

• Locus tag: BSU36930

Database entries

• BsubCyc: BSU36930

• DBTBS entry: no entry

• SubtiList entry: [1]

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:

• Domains:

• Modification:

• Cofactors:

• Effectors of protein activity:

• Interactions:
  • McsB-YwlE (dephosphorylation of McsB) PubMed

• Localization: weak oligomerization, results in inactivation of YwlE PubMed

Database entries

• BsubCyc: BSU36930

• Structure: 1ZGG

• UniProt: P39155

• KEGG entry: [2]

• E.C. number: 3.1.3.48

Expression and regulation

• Operon:

• Expression browser: ywlE PubMed

• Sigma factor:

• 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

• Mutant:
  • ywlE::aphA3 available from Ulf Gerth's lab
  • ywlE::tet available from Ulf Gerth's lab
  • ywlE::spec available from Ulf Gerth's lab
  • GP1458 (ywlE::aphA3), available in Jörg Stülke's lab
  • GP1459 (ywlE::tet), available in Jörg Stülke's lab

• 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:

• Antibody: available in Ulf Gerth's lab

Labs working on this gene/protein

• Ulf Gerth, Greifswald, Germany

• Fabian Commichau Göttingen, Germany

References

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)