NprE

• Description: extracellular neutral protease B
  
  

Gene name	nprE
Synonyms
Essential	no
Product	extracellular neutral protease B
Function	degradation of proteins
MW, pI	56 kDa, 7.481
Gene length, protein length	1563 bp, 521 aa
Immediate neighbours	yktD, ylaA
Get the DNA and protein sequences (Barbe et al., 2009)
Genetic context 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

The gene

Basic information

• Locus tag: BSU14700

Expression

Database entries

• DBTBS entry: [1]

• SubtiList entry: [2]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity: Similar, but not identical, to that of thermolysin (according to Swiss-Prot)

• Protein family: peptidase M4 family (according to Swiss-Prot)

• Paralogous protein(s): NprB

Extended information on the protein

• Kinetic information:

• Domains:

• Modification:

• Cofactor(s):

• Effectors of protein activity:

• Interactions:

• Localization:
  • extracellular (signal peptide) PubMed

Database entries

• Structure: 1NPC (of Bacillus cereus)

• UniProt: P68736

• KEGG entry: [3]

• E.C. number:

Expression and regulation

• Operon: nprE (according to DBTBS)

• Sigma factor:

• Regulation:
  • repressed during exponential growth (ScoC) PubMed

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

• Additional information:

Biological materials

• Mutant:

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

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

Additional publications: PubMed

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)

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)