Difference between revisions of "LonA"
(→References) |
(→Additional information) |
||
Line 51: | Line 51: | ||
A mutation in ''lonA'' suppresses the motility defect of a ''[[lytC]]'' mutant [http://www.ncbi.nlm.nih.gov/sites/entrez/19542270 PubMed] | A mutation in ''lonA'' suppresses the motility defect of a ''[[lytC]]'' mutant [http://www.ncbi.nlm.nih.gov/sites/entrez/19542270 PubMed] | ||
− | + | Evidence for a specific DNA binding activitity was found [http://www.ncbi.nlm.nih.gov/sites/entrez/19643080 PubMed] | |
=The protein= | =The protein= |
Revision as of 08:51, 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 This image was kindly provided by SubtiList
|
Contents
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 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:
- Localization:
Database entries
- Structure: 1X37 (Ssd domain)
- UniProt: P37945
- 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)