Difference between revisions of "LonA"

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= [[Categories]] containing this gene/protein =
 
= [[Categories]] containing this gene/protein =
{{SubtiWiki category|[[proteolysis]]}}
+
{{SubtiWiki category|[[proteolysis]]}},
 +
{{SubtiWiki category|[[motility and chemotaxis]]}}
  
 
= This gene is a member of the following [[regulons]] =
 
= This gene is a member of the following [[regulons]] =
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* '''[[SubtInteract|Interactions]]:'''
 
* '''[[SubtInteract|Interactions]]:'''
 
** homohexameric protein {{PubMed|20600124}}
 
** homohexameric protein {{PubMed|20600124}}
 +
** [[LonA]]-[[SmiA]] {{PubMed|25538299}}
 +
** [[LonA]]-[[SwrA]] (degradation) {{PubMed|25538299}}
  
* '''[[Localization]]:''' coincident with the nucleoid during normal growth and localized to the forespore during development {{PubMed|18689473}}
+
* '''[[Localization]]:'''  
 +
** coincident with the nucleoid during normal growth and localized to the forespore during development {{PubMed|18689473}}
  
 
=== Database entries ===
 
=== Database entries ===
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==Original publications==
 
==Original publications==
<pubmed>7961403,7961402, 19542270, 19643080 9852015 18689473 20600124 </pubmed>
+
<pubmed>7961403,7961402, 19542270, 19643080 9852015 18689473 20600124 25538299</pubmed>
  
 
[[Category:Protein-coding genes]]
 
[[Category:Protein-coding genes]]

Revision as of 11:18, 2 January 2015

  • 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
Gene expression levels in SubtiExpress: lonA
Regulation of this protein in SubtiPathways:
lonA
MW, pI 86 kDa, 5.774
Gene length, protein length 2322 bp, 774 aa
Immediate neighbours ysxC, lonB
Sequences Protein DNA DNA_with_flanks
Genetic context
LonA context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
LonA expression.png















Categories containing this gene/protein

proteolysis, motility and chemotaxis

This gene is a member of the following regulons

CtsR regulon

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

Evidence for a specific DNA binding activitity of the α-domain was found 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:
  • Localization:
    • coincident with the nucleoid during normal growth and localized to the forespore during development PubMed

Database entries

  • KEGG entry: [3]
  • E.C. number:

Additional information

Expression and regulation

  • Regulatory mechanism:
  • Additional information:
    • number of protein molecules per cell (minimal medium with glucose and ammonium): 125 PubMed
    • number of protein molecules per cell (complex medium with amino acids, without glucose): 660 PubMed

Biological materials

  • Mutant:
  • Expression vector:
  • lacZ fusion:
  • GFP fusion:
  • two-hybrid system:
  • Antibody:

Labs working on this gene/protein

Your additional remarks

References

Reviews


Original publications

Sampriti Mukherjee, Anna C Bree, Jing Liu, Joyce E Patrick, Peter Chien, Daniel B Kearns
Adaptor-mediated Lon proteolysis restricts Bacillus subtilis hyperflagellation.
Proc Natl Acad Sci U S A: 2015, 112(1);250-5
[PubMed:25538299] [WorldCat.org] [DOI] (I p)

Ramona E Duman, Jan Löwe
Crystal structures of Bacillus subtilis Lon protease.
J Mol Biol: 2010, 401(4);653-70
[PubMed:20600124] [WorldCat.org] [DOI] (I p)

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)

Lyle A Simmons, Alan D Grossman, Graham C Walker
Clp and Lon proteases occupy distinct subcellular positions in Bacillus subtilis.
J Bacteriol: 2008, 190(20);6758-68
[PubMed:18689473] [WorldCat.org] [DOI] (I p)

E Krüger, M Hecker
The first gene of the Bacillus subtilis clpC operon, ctsR, encodes a negative regulator of its own operon and other class III heat shock genes.
J Bacteriol: 1998, 180(24);6681-8
[PubMed:9852015] [WorldCat.org] [DOI] (P 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)