Difference between revisions of "MlpA"

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* '''Operon:''' ''[[mlpA]]'' {{PubMed|8098035}}
 
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* '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=mlpA_1742617_1743846_1 mlpA] {{PubMed|22383849}}
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=Biological materials =
 
=Biological materials =

Revision as of 09:16, 13 April 2012

  • Description: mitochondrial processing peptidase-like, involved in regulation of protease gene expression

Gene name mlpA
Synonyms ymxG
Essential no
Product specific processing protease
Function control of proteolyticc activity
MW, pI 45 kDa, 5.275
Gene length, protein length 1227 bp, 409 aa
Immediate neighbours ylxY, ymxH
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
MlpA context.gif
This image was kindly provided by SubtiList



Categories containing this gene/protein

proteolysis

This gene is a member of the following regulons

The gene

Basic information

  • Locus tag: BSU16710

Phenotypes of a mutant

fivefold increased levels of proteolytic activity in their growth medium PubMed

Database entries

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

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity:
  • Protein family: peptidase M16 family (according to Swiss-Prot)
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification:
  • Cofactor(s):
  • Effectors of protein activity:

Database entries

  • Structure:
  • KEGG entry: [3]
  • E.C. number:

Additional information

Expression and regulation

  • Sigma factor:
  • Regulation:
  • Regulatory mechanism:
  • Additional information:

Biological materials

  • Mutant: deletion mutant, available in van Dijl lab
  • Expression vector:
  • lacZ fusion:
  • GFP fusion:
  • two-hybrid system:
  • Antibody:

Labs working on this gene/protein

Jan Maarten van Dijl, Groningen, Netherlands

Your additional remarks

References

H Tjalsma, A Bolhuis, J D Jongbloed, S Bron, J M van Dijl
Signal peptide-dependent protein transport in Bacillus subtilis: a genome-based survey of the secretome.
Microbiol Mol Biol Rev: 2000, 64(3);515-47
[PubMed:10974125] [WorldCat.org] [DOI] (P p)

A Bolhuis, E Koetje, J Y Dubois, J Vehmaanperä, G Venema, S Bron, J M van Dijl
Did the mitochondrial processing peptidase evolve from a eubacterial regulator of gene expression?
Mol Biol Evol: 2000, 17(1);198-201
[PubMed:10666719] [WorldCat.org] [DOI] (P p)

N Y Chen, S Q Jiang, D A Klein, H Paulus
Organization and nucleotide sequence of the Bacillus subtilis diaminopimelate operon, a cluster of genes encoding the first three enzymes of diaminopimelate synthesis and dipicolinate synthase.
J Biol Chem: 1993, 268(13);9448-65
[PubMed:8098035] [WorldCat.org] (P p)