NprE

From SubtiWiki
Revision as of 19:29, 15 September 2010 by Jstuelk (talk | contribs)
Jump to: navigation, search
  • 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
NprE context.gif
This image was kindly provided by SubtiList



The gene

Basic information

  • Locus tag: BSU14700

Phenotypes of a mutant

Database entries

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

Additional information

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

Database entries

  • Structure: 1NPC (of Bacillus cereus)
  • KEGG entry: [3]
  • E.C. number:

Additional information

Expression and regulation

  • Operon: nprE (according to DBTBS)
  • Regulation:
    • repressed during exponential growth (ScoC) PubMed
  • 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

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

Onuma Chumsakul, Hiroki Takahashi, Taku Oshima, Takahiro Hishimoto, Shigehiko Kanaya, Naotake Ogasawara, Shu Ishikawa
Genome-wide binding profiles of the Bacillus subtilis transition state regulator AbrB and its homolog Abh reveals their interactive role in transcriptional regulation.
Nucleic Acids Res: 2011, 39(2);414-28
[PubMed:20817675] [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)

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)