Difference between revisions of "Ugd"

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= [[Categories]] containing this gene/protein =
 
= [[Categories]] containing this gene/protein =
{{SubtiWiki category|[[phosphoproteins]]}}
+
{{SubtiWiki category|[[phosphoproteins]]}},
 +
{{SubtiWiki category|[[sporulation/ other]]}}
  
 
= This gene is a member of the following [[regulons]] =
 
= This gene is a member of the following [[regulons]] =

Revision as of 08:03, 22 April 2014

  • Description: UDP-glucose dehydrogenase

Gene name ugd
Synonyms ywqF
Essential no
Product UDP-glucose dehydrogenase
Function unknown
Gene expression levels in SubtiExpress: ugd
Interactions involving this protein in SubtInteract: Ugd
MW, pI 47 kDa, 5.03
Gene length, protein length 1320 bp, 440 aa
Immediate neighbours ywqG, ptpZ
Sequences Protein DNA DNA_with_flanks
Genetic context
YwqF context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
Ugd expression.png















Categories containing this gene/protein

phosphoproteins, sporulation/ other

This gene is a member of the following regulons

The gene

Basic information

  • Locus tag: BSU36230

Phenotypes of a mutant

Database entries

  • DBTBS entry: [1]
  • SubtiList entry: [2]

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: UDP-glucose + 2 NAD+ + H2O = UDP-glucuronate + 2 NADH (according to Swiss-Prot)
  • Protein family: UDP-glucose/GDP-mannose dehydrogenase family (according to Swiss-Prot)

Extended information on the protein

  • Kinetic information:
  • Effectors of protein activity: phosphorylation by PtkA stimulates activity of Ugd PubMed

Database entries

  • Structure:
  • KEGG entry: [3]

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

Your additional remarks

References

Lei Shi, Boyang Ji, Lorena Kolar-Znika, Ana Boskovic, Fanny Jadeau, Christophe Combet, Christophe Grangeasse, Damjan Franjevic, Emmanuel Talla, Ivan Mijakovic
Evolution of bacterial protein-tyrosine kinases and their relaxed specificity toward substrates.
Genome Biol Evol: 2014, 6(4);800-17
[PubMed:24728941] [WorldCat.org] [DOI] (I p)

Taryn B Kiley, Nicola R Stanley-Wall
Post-translational control of Bacillus subtilis biofilm formation mediated by tyrosine phosphorylation.
Mol Microbiol: 2010, 78(4);947-63
[PubMed:20815827] [WorldCat.org] [DOI] (I p)

Dina Petranovic, Christophe Grangeasse, Boris Macek, Mohammad Abdillatef, Virginie Gueguen-Chaignon, Sylvie Nessler, Josef Deutscher, Ivan Mijakovic
Activation of Bacillus subtilis Ugd by the BY-kinase PtkA proceeds via phosphorylation of its residue tyrosine 70.
J Mol Microbiol Biotechnol: 2009, 17(2);83-9
[PubMed:19258708] [WorldCat.org] [DOI] (I 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)

Ivan Mijakovic, Dina Petranovic, Josef Deutscher
How tyrosine phosphorylation affects the UDP-glucose dehydrogenase activity of Bacillus subtilis YwqF.
J Mol Microbiol Biotechnol: 2004, 8(1);19-25
[PubMed:15741737] [WorldCat.org] [DOI] (P p)

Ivan Mijakovic, Sandrine Poncet, Grégory Boël, Alain Mazé, Sylvie Gillet, Emmanuel Jamet, Paulette Decottignies, Christophe Grangeasse, Patricia Doublet, Pierre Le Maréchal, Josef Deutscher
Transmembrane modulator-dependent bacterial tyrosine kinase activates UDP-glucose dehydrogenases.
EMBO J: 2003, 22(18);4709-18
[PubMed:12970183] [WorldCat.org] [DOI] (P p)