Difference between revisions of "TuaD"

From SubtiWiki
Jump to: navigation, search
Line 93: Line 93:
  
 
* '''Regulation:'''  
 
* '''Regulation:'''  
** expressed under conditions of phosphate limitation ([[PhoP]]) [http://www.ncbi.nlm.nih.gov/sites/entrez/9611818 PubMed]
+
** expressed under conditions of phosphate limitation ([[PhoP]]) {{PubMed|9611818,10627039}}
  
 
* '''Regulatory mechanism:'''  
 
* '''Regulatory mechanism:'''  
** [[PhoP]]: transcription activation [http://www.ncbi.nlm.nih.gov/sites/entrez/9611818 PubMed]
+
** [[PhoP]]: transcription activation {{PubMed|9611818,10627039}}
  
 
* '''Additional information:'''
 
* '''Additional information:'''
Line 120: Line 120:
 
=References=
 
=References=
  
<pubmed>10913081,10376820 ,9611818,12970183, 10048024 </pubmed>
+
<pubmed>10913081,10376820 ,9611818,12970183, 10048024 10627039</pubmed>
  
 
[[Category:Protein-coding genes]]
 
[[Category:Protein-coding genes]]

Revision as of 13:07, 28 December 2009

  • Description: UDP glucose 6-dehydrogenase

Gene name tuaD
Synonyms yvhD
Essential no
Product UDP glucose 6-dehydrogenase
Function biosynthesis of teichuronic acid
MW, pI 49 kDa, 6.107
Gene length, protein length 1383 bp, 461 aa
Immediate neighbours tuaE, tuaC
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
TuaD context.gif
This image was kindly provided by SubtiList



The gene

Basic information

  • Locus tag: BSU35580

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:
  • Domains:
  • Modification: phosphorylation on a Tyr residue by PtkA PubMed
  • Cofactor(s):
  • Effectors of protein activity: PtkA-dependent phosphorylation stimulates TuaD activity PubMed
  • Interactions:
  • Localization: cytoplasm (according to Swiss-Prot)

Database entries

  • Structure:
  • KEGG entry: [3]

Additional information

Expression and regulation

  • Regulation:
    • expressed under conditions of phosphate limitation (PhoP) PubMed
  • 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

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)

H Antelmann, C Scharf, M Hecker
Phosphate starvation-inducible proteins of Bacillus subtilis: proteomics and transcriptional analysis.
J Bacteriol: 2000, 182(16);4478-90
[PubMed:10913081] [WorldCat.org] [DOI] (P p)

Maryam Lahooti, Colin R Harwood
Transcriptional analysis of the Bacillus subtilis teichuronic acid operon.
Microbiology (Reading): 1999, 145 ( Pt 12);3409-3417
[PubMed:10627039] [WorldCat.org] [DOI] (P p)

Marco Pagni, Vladimir Lazarevic, Blazenka Soldo, Dimitri Karamata
Assay for UDPglucose 6-dehydrogenase in phosphate-starved cells: gene tuaD of Bacillus subtilis 168 encodes the UDPglucose 6-dehydrogenase involved in teichuronic acid synthesis.
Microbiology (Reading): 1999, 145 ( Pt 5);1049-1053
[PubMed:10376820] [WorldCat.org] [DOI] (P p)

B Soldo, V Lazarevic, M Pagni, D Karamata
Teichuronic acid operon of Bacillus subtilis 168.
Mol Microbiol: 1999, 31(3);795-805
[PubMed:10048024] [WorldCat.org] [DOI] (P p)

Wei Liu, F Marion Hulett
Comparison of PhoP binding to the tuaA promoter with PhoP binding to other Pho-regulon promoters establishes a Bacillus subtilis Pho core binding site.
Microbiology (Reading): 1998, 144 ( Pt 5);1443-1450
[PubMed:9611818] [WorldCat.org] [DOI] (P p)