AprE

• Description: extracellular alkaline serine protease (subtilisin E)
  
  

Gene name	aprE
Synonyms	sprE
Essential	no
Product	extracellular alkaline serine protease (subtilisin E))
Function	protein degradation
MW, pI	39 kDa, 9.342
Gene length, protein length	1143 bp, 381 aa
Immediate neighbours	yhfN, yhfO
Get the DNA and protein sequences (Barbe et al., 2009)
Genetic context This image was kindly provided by SubtiList

The gene

Basic information

• Locus tag: BSU10300

Database entries

• DBTBS entry: [1]

• SubtiList entry: [2]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity: Hydrolysis of proteins with broad specificity for peptide bonds, and a preference for a large uncharged residue in P1 (according to Swiss-Prot)

• Protein family: peptidase S8 family (according to Swiss-Prot)

• Paralogous protein(s):

Extended information on the protein

• Kinetic information:

• Domains:

• Modification:

• Cofactor(s):

• Effectors of protein activity:

• Interactions: AprE-PaiA

• Localization: secreted (according to Swiss-Prot), extracellular (signal peptide) PubMed

Database entries

• Structure: 1SBC

• Swiss prot entry: P04189

• KEGG entry: [3]

• E.C. number:

Expression and regulation

• Operon:

• Sigma factor:

• Regulation:
  • repressed by SinR PubMed
  • repressed during exponential growth (ScoC) PubMed
  • repressed during logrithmic growth (AbrB) PubMed

• Regulatory mechanism:
  • SinR: transcription repression PubMed
  • ScoC: transcription repression PubMed
  • AbrB: transcription repression PubMed

• Additional information: the mRNA is extremely stable (more than 25 min) PubMed

Biological materials

• Mutant:

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

References

Birgit Voigt, Haike Antelmann, Dirk Albrecht, Armin Ehrenreich, Karl-Heinz Maurer, Stefan Evers, Gerhard Gottschalk, Jan Maarten van Dijl, Thomas Schweder, Michael Hecker
Cell physiology and protein secretion of Bacillus licheniformis compared to Bacillus subtilis.
J Mol Microbiol Biotechnol: 2009, 16(1-2);53-68
[PubMed:18957862] [WorldCat.org] [DOI] (I p)

Gustav Hambraeus, Kaisa Karhumaa, Blanka Rutberg
A 5' stem-loop and ribosome binding but not translation are important for the stability of Bacillus subtilis aprE leader mRNA.
Microbiology (Reading): 2002, 148(Pt 6);1795-1803
[PubMed:12055299] [WorldCat.org] [DOI] (P p)

Gustav Hambraeus, Martin Persson, Blanka Rutberg
The aprE leader is a determinant of extreme mRNA stability in Bacillus subtilis.
Microbiology (Reading): 2000, 146 Pt 12;3051-3059
[PubMed:11101663] [WorldCat.org] [DOI] (P p)

P T Kallio, J E Fagelson, J A Hoch, M A Strauch
The transition state regulator Hpr of Bacillus subtilis is a DNA-binding protein.
J Biol Chem: 1991, 266(20);13411-7
[PubMed:1906467] [WorldCat.org] (P p)

N K Gaur, J Oppenheim, I Smith
The Bacillus subtilis sin gene, a regulator of alternate developmental processes, codes for a DNA-binding protein.
J Bacteriol: 1991, 173(2);678-86
[PubMed:1898931] [WorldCat.org] [DOI] (P p)

M A Strauch, G B Spiegelman, M Perego, W C Johnson, D Burbulys, J A Hoch
The transition state transcription regulator abrB of Bacillus subtilis is a DNA binding protein.
EMBO J: 1989, 8(5);1615-21
[PubMed:2504584] [WorldCat.org] [DOI] (P p)

1. Voigt et al. (2009) Cell physiology and protein secretion of Bacillus licheniformis compared to Bacillus subtilis. J Mol Microbiol Biotechnol. 16: 53-68 PubMed
2. Hambraeus, G., Persson, M. & Rutberg, B. (2000). The aprE leader is a determinant of extreme mRNA stability in Bacillus subtilis. Microbiology 146, 3051-3059. PubMed
3. Hambraeus, G., Karhumaa, K. & Rutberg, B. (2002). A 5' stem-loop and ribosome binding but not translation are important for the stability of Bacillus subtilis aprE leader mRNA. Microbiology 148, 1795-1803. PubMed
4. Author1, Author2 & Author3 (year) Title Journal volume: page-page. PubMed