Difference between revisions of "YmdB"

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<pubmed> 19376879 </pubmed>
 
<pubmed> 19376879 </pubmed>
 
# Author1, Author2 & Author3 (year) Title ''Journal'' '''volume:''' page-page. [http://www.ncbi.nlm.nih.gov/sites/entrez/PMID PubMed]
 

Revision as of 21:12, 15 June 2009

  • Description: unknown function

Gene name ymdB
Synonyms
Essential no
Product YmdB protein
Function unknown function
MW, pI 29,1 kDa, 6.50
Gene length, protein length 792 bp, 264 amino acids
Immediate neighbours rny, spoVS
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
YmdB context.gif
This image was kindly provided by SubtiList



The gene

Basic information

  • Locus tag: BSU16970

Phenotypes of a mutant

strong overexpression of Hag

Database entries

  • DBTBS entry: no entry
  • SubtiList entry: [1]

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: negative effector of the expression of hag and other members of the SigD regulon
  • Protein family:
  • Paralogous protein(s): similar to unknown proteins

Extended information on the protein

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

Database entries

  • Structure:
  • KEGG entry: [2]
  • E.C. number:

Additional information

has a negative effect on hag expression

Expression and regulation

  • Sigma factor:
  • Regulation: constitutive
  • Regulatory mechanism:
  • Additional information: there is a terminator between rny and ymdB, most transcripts terminate there

Biological materials

  • Mutant: GP583 (spc), available in Stülke lab
  • Expression vector: pGP1040 (N-terminal His-tag, in pWH844), pGP1041 (N-terminal Strep-tag, for SPINE, expression in B. subtilis, in pGP380), available in Stülke lab
  • lacZ fusion:
  • GFP fusion:
  • two-hybrid system: B. pertussis adenylate cyclase-based bacterial two hybrid system (BACTH), available in Stülke lab
  • Antibody:

Labs working on this gene/protein

Jörg Stülke, University of Göttingen, Germany Homepage

Your additional remarks

References

Jason Zemansky, Benjamin C Kline, Joshua J Woodward, Jess H Leber, Hélène Marquis, Daniel A Portnoy
Development of a mariner-based transposon and identification of Listeria monocytogenes determinants, including the peptidyl-prolyl isomerase PrsA2, that contribute to its hemolytic phenotype.
J Bacteriol: 2009, 191(12);3950-64
[PubMed:19376879] [WorldCat.org] [DOI] (I p)