AprE

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  • 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
AprE context.gif
This image was kindly provided by SubtiList



Categories containing this gene/protein

utilization of nitrogen sources other than amino acids

This gene is a member of the following regulons

AbrB regulon, ScoC regulon, SinR regulon

The gene

Basic information

  • Locus tag: BSU10300

Phenotypes of a mutant

Database entries

  • DBTBS entry: [1]
  • SubtiList entry: [2]

Additional information

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

Database entries

  • KEGG entry: [3]
  • E.C. number:

Additional information

Expression and regulation

  • Operon: aprE (according to DBTBS)
  • 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:
  • Additional information: The pAPNC213 vector published by Morimoto et al. (2002) is an insertion plasmid for IPTG inducible constructs that can be integrated into the chromosomal aprE locus by replacing the aprE open reading frame via double homologous recombination. PubMed

Labs working on this gene/protein

Your additional remarks

References

Reviews

Massimiliano Marvasi, Pieter T Visscher, Lilliam Casillas Martinez
Exopolymeric substances (EPS) from Bacillus subtilis: polymers and genes encoding their synthesis.
FEMS Microbiol Lett: 2010, 313(1);1-9
[PubMed:20735481] [WorldCat.org] [DOI] (I p)

Original publications