SppA

• 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: Protein secretion
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 This image was kindly provided by SubtiList
Expression at a glance   PubMed

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]

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:

• Domains:

• Modification:

• Cofactors:

• Effectors of protein activity:

• Interactions:
  • the protein forms a dome shaped octameric complex PubMed

• Localization:
  • cell membrane PubMed

Database entries

• Structure: 3RST PubMed

• UniProt: O34525

• KEGG entry: [3]

• E.C. number:

Expression and regulation

• Operon: sppA-yteJ PubMed

• Expression browser: sppA PubMed

• Sigma factor: SigW PubMed

• 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:

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)