MlpA

• 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 This image was kindly provided by SubtiList

Categories containing this gene/protein

proteolysis

The gene

Basic information

• Locus tag: BSU16710

Expression

Phenotypes of a mutant

fivefold increased levels of proteolytic activity in their growth medium PubMed

Database entries

• DBTBS entry: [1]

• SubtiList entry: [2]

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:

• Interactions:

• Localization:

Database entries

• Structure:

• UniProt: Q04805

• KEGG entry: [3]

• E.C. number:

Expression and regulation

• Operon: mlpA PubMed

• 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

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)