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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
Get the DNA and protein sequences
(Barbe et al., 2009)
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:
  • Domains:
  • Modification:
  • Cofactor(s):
  • Effectors of protein activity:

Database entries

  • KEGG entry: [2]

Additional information

Expression and regulation

  • Operon:
  • Sigma factor:
  • Regulation:
  • Regulatory mechanism:
  • Additional information:

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 Stülke lab
    • GP1459 (ywlE::tet), available in Stülke 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:

Labs working on this gene/protein

Your additional remarks


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)