LonA

• 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 This image was kindly provided by SubtiList

Categories containing this gene/protein

proteolysis

This gene is a member of the following regulons

CtsR regulon

The gene

Basic information

• Locus tag: BSU28200

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:

• Interactions:
  • homohexameric protein PubMed

• Localization: coincident with the nucleoid during normal growth and localized to the forespore during development PubMed

Database entries

• Structure: 3M65 (N-terminal domain) PubMed, 3M6A (C-terminal domain) PubMed, 1X37 (Ssd domain)

• UniProt: P37945

• KEGG entry: [3]

• E.C. number:

Expression and regulation

• Operon: lonA-ysxC PubMed

• Expression browser: lonA PubMed

• Sigma factor: SigA PubMed

• Regulation:
  • induced by heat stress (CtsR) PubMed

• Regulatory mechanism:
  • CtsR: transcription repression PubMed

• Additional information:

Biological materials

• Mutant:

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

References

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)