Difference between revisions of "PapB"

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<pubmed> 23144141 </pubmed>
 
[[Category:Protein-coding genes]]
 
[[Category:Protein-coding genes]]

Revision as of 19:56, 13 November 2012

  • Description: similar to Xaa-Pro dipeptidase

Gene name ykvY
Synonyms
Essential no
Product unknown
Function unknown
Gene expression levels in SubtiExpress: ykvY
Metabolic function and regulation of this protein in SubtiPathways:
Alternative nitrogen sources
MW, pI 40 kDa, 5.171
Gene length, protein length 1089 bp, 363 aa
Immediate neighbours zosA, ykvZ
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
YkvY context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
YkvY expression.png
























Categories containing this gene/protein

utilization of nitrogen sources other than amino acids

This gene is a member of the following regulons

The gene

Basic information

  • Locus tag: BSU13860

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 family: peptidase M24B family (according to Swiss-Prot)
  • Paralogous protein(s): YqhT

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification:
  • Cofactor(s):
  • Effectors of protein activity:

Database entries

  • Structure: 3Q6D (B. anthracis Xaa-Pro dipeptidase, 35% identity, 55% similarity)
  • KEGG entry: [2]
  • E.C. number:

Additional information

Expression and regulation

  • Operon:
  • Sigma factor:
  • 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

Adrienne Zaprasis, Jeanette Brill, Marietta Thüring, Guido Wünsche, Magnus Heun, Helena Barzantny, Tamara Hoffmann, Erhard Bremer
Osmoprotection of Bacillus subtilis through import and proteolysis of proline-containing peptides.
Appl Environ Microbiol: 2013, 79(2);576-87
[PubMed:23144141] [WorldCat.org] [DOI] (I p)