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
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 This image was kindly provided by SubtiList
Expression at a glance   PubMed

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

Database entries

• BsubCyc: BSU28200

• 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
  • LonA-SmiA PubMed
  • LonA-SwrA (degradation) PubMed

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

Database entries

• BsubCyc: BSU28200

• 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:
  • 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:

References

Reviews

Noël Molière, Kürşad Turgay
General and regulatory proteolysis in Bacillus subtilis.
Subcell Biochem: 2013, 66;73-103
[PubMed:23479438] [WorldCat.org] [DOI] (P p)