SppA

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  • Description: signal peptide peptidase required for efficient processing of pre-proteins, cleaves remnant signal peptides within the cellular membrane

Gene name sppA
Synonyms yteI
Essential no
Product signal peptide peptidase
Function protein secretion
Gene expression levels in SubtiExpress: sppA
Metabolic function and regulation of this protein in SubtiPathways:
SppA
MW, pI 36 kDa, 7.314
Gene length, protein length 1005 bp, 335 aa
Immediate neighbours yteJ, ytdI
Sequences Protein DNA DNA_with_flanks
Genetic context
SppA context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
SppA expression.png















Categories containing this gene/protein

protein secretion, cell envelope stress proteins (controlled by SigM, V, W, X, Y), membrane proteins

This gene is a member of the following regulons

SigW regulon

The gene

Basic information

  • Locus tag: BSU29530

Phenotypes of a mutant

  • more sensitive to nisin PubMed

Database entries

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

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity:
    • serine protease that functions to cleave the remnant signal peptides left behind after protein secretion and cleavage by signal peptidases
  • Protein family: peptidase S49 family (according to Swiss-Prot)
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Modification:
  • Effectors of protein activity:

Database entries

  • KEGG entry: [3]
  • E.C. number:

Additional information

Expression and regulation

  • Regulation:
    • induced in response to cell wall stress (SigW) PubMed
  • Regulatory mechanism:
  • Additional information:
    • self-processes its own C-termini PubMed

Biological materials

  • Mutant:
  • Expression vector:
  • lacZ fusion:
  • GFP fusion:
  • two-hybrid system:
  • Antibody:

Labs working on this gene/protein

Your additional remarks

References

Sung-Eun Nam, Mark Paetzel
Structure of signal peptide peptidase A with C-termini bound in the active sites: insights into specificity, self-processing, and regulation.
Biochemistry: 2013, 52(49);8811-22
[PubMed:24228759] [WorldCat.org] [DOI] (I p)

Anthony W Kingston, Xiaojie Liao, John D Helmann
Contributions of the σ(W) , σ(M) and σ(X) regulons to the lantibiotic resistome of Bacillus subtilis.
Mol Microbiol: 2013, 90(3);502-18
[PubMed:23980836] [WorldCat.org] [DOI] (I p)

Sung-Eun Nam, Apollos C Kim, Mark Paetzel
Crystal structure of Bacillus subtilis signal peptide peptidase A.
J Mol Biol: 2012, 419(5);347-58
[PubMed:22472423] [WorldCat.org] [DOI] (I p)

Min Cao, Tao Wang, Rick Ye, John D Helmann
Antibiotics that inhibit cell wall biosynthesis induce expression of the Bacillus subtilis sigma(W) and sigma(M) regulons.
Mol Microbiol: 2002, 45(5);1267-76
[PubMed:12207695] [WorldCat.org] [DOI] (P p)

X Huang, A Gaballa, M Cao, J D Helmann
Identification of target promoters for the Bacillus subtilis extracytoplasmic function sigma factor, sigma W.
Mol Microbiol: 1999, 31(1);361-71
[PubMed:9987136] [WorldCat.org] [DOI] (P p)