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

• UniProt: 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

Eliel R Romero-García, Alfredo Téllez-Valencia, María F Trujillo, José G Sampedro, Hugo Nájera, Arturo Rojo-Domínguez, Jesús García-Soto, Mario Pedraza-Reyes
Engineering and directed evolution of a Ca2+ binding site A-deficient AprE mutant reveal an essential contribution of the loop Leu75-Leu82 to enzyme activity.
J Biomed Biotechnol: 2009, 2009;201075
[PubMed:19710937] [WorldCat.org] [DOI] (I p)

Sadanobu Abe, Ayako Yasumura, Teruo Tanaka
Regulation of Bacillus subtilis aprE expression by glnA through inhibition of scoC and sigma(D)-dependent degR expression.
J Bacteriol: 2009, 191(9);3050-8
[PubMed:19251843] [WorldCat.org] [DOI] (I p)

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)

Jan-Willem Veening, Oleg A Igoshin, Robyn T Eijlander, Reindert Nijland, Leendert W Hamoen, Oscar P Kuipers
Transient heterogeneity in extracellular protease production by Bacillus subtilis.
Mol Syst Biol: 2008, 4;184
[PubMed:18414485] [WorldCat.org] [DOI] (I p)

Mitsuo Ogura, Atsushi Matsuzawa, Hirofumi Yoshikawa, Teruo Tanaka
Bacillus subtilis SalA (YbaL) negatively regulates expression of scoC, which encodes the repressor for the alkaline exoprotease gene, aprE.
J Bacteriol: 2004, 186(10);3056-64
[PubMed:15126467] [WorldCat.org] [DOI] (P p)

G Hambraeus, C von Wachenfeldt, L Hederstedt
Genome-wide survey of mRNA half-lives in Bacillus subtilis identifies extremely stable mRNAs.
Mol Genet Genomics: 2003, 269(5);706-14
[PubMed:12884008] [WorldCat.org] [DOI] (P 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)

D J Henner, E Ferrari, M Perego, J A Hoch
Location of the targets of the hpr-97, sacU32(Hy), and sacQ36(Hy) mutations in upstream regions of the subtilisin promoter.
J Bacteriol: 1988, 170(1);296-300
[PubMed:2447063] [WorldCat.org] [DOI] (P p)

E Ferrari, D J Henner, M Perego, J A Hoch
Transcription of Bacillus subtilis subtilisin and expression of subtilisin in sporulation mutants.
J Bacteriol: 1988, 170(1);289-95
[PubMed:2447062] [WorldCat.org] [DOI] (P p)

E Ferrari, S M Howard, J A Hoch
Effect of stage 0 sporulation mutations on subtilisin expression.
J Bacteriol: 1986, 166(1);173-9
[PubMed:3082852] [WorldCat.org] [DOI] (P p)

S L Wong, C W Price, D S Goldfarb, R H Doi
The subtilisin E gene of Bacillus subtilis is transcribed from a sigma 37 promoter in vivo.
Proc Natl Acad Sci U S A: 1984, 81(4);1184-8
[PubMed:6322190] [WorldCat.org] [DOI] (P p)