Difference between revisions of "LonA"

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(Additional information)
(References)
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<pubmed>7961403,7961402, 19542270 </pubmed>
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<pubmed>7961403,7961402, 19542270, 19643080 </pubmed>
  
 
[[Category:Protein-coding genes]]
 
[[Category:Protein-coding genes]]

Revision as of 08:50, 3 August 2009

  • Description: class III heat-shock ATP-dependent protease

Gene name lonA
Synonyms lon
Essential no
Product class III heat-shock ATP-dependent protease
Function protein quality control
Regulation of this protein in SubtiPathways:
Stress
MW, pI 86 kDa, 5.774
Gene length, protein length 2322 bp, 774 aa
Immediate neighbours ysxC, lonB
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
LonA context.gif
This image was kindly provided by SubtiList







The gene

Basic information

  • Locus tag: BSU28200

Phenotypes of a mutant

Database entries

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

Additional information

A mutation in lonA suppresses the motility defect of a lytC mutant PubMed

There is evidence for a specific DNA binding activitity PubMed

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: Hydrolysis of proteins in presence of ATP (according to Swiss-Prot)
  • Protein family: peptidase S16 family (according to Swiss-Prot)
  • Paralogous protein(s):

Extended information on the protein

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

Database entries

  • Structure: 1X37 (Ssd domain)
  • KEGG entry: [3]
  • E.C. number:

Additional information

Expression and regulation

  • Operon:
  • 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

Yu-Ching Lin, Huai-Cheng Lee, Iren Wang, Chun-Hua Hsu, Jiahn-Haur Liao, Alan Yueh-Luen Lee, Chinpan Chen, Shih-Hsiung Wu
DNA-binding specificity of the Lon protease alpha-domain from Brevibacillus thermoruber WR-249.
Biochem Biophys Res Commun: 2009, 388(1);62-6
[PubMed:19643080] [WorldCat.org] [DOI] (I p)

Rui Chen, Sarah B Guttenplan, Kris M Blair, Daniel B Kearns
Role of the sigmaD-dependent autolysins in Bacillus subtilis population heterogeneity.
J Bacteriol: 2009, 191(18);5775-84
[PubMed:19542270] [WorldCat.org] [DOI] (I p)

R Schmidt, A L Decatur, P N Rather, C P Moran, R Losick
Bacillus subtilis lon protease prevents inappropriate transcription of genes under the control of the sporulation transcription factor sigma G.
J Bacteriol: 1994, 176(21);6528-37
[PubMed:7961403] [WorldCat.org] [DOI] (P p)

S Riethdorf, U Völker, U Gerth, A Winkler, S Engelmann, M Hecker
Cloning, nucleotide sequence, and expression of the Bacillus subtilis lon gene.
J Bacteriol: 1994, 176(21);6518-27
[PubMed:7961402] [WorldCat.org] [DOI] (P p)