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Literature summary for 3.4.24.85 extracted from

  • Saito, A.; Hizukuri, Y.; Matsuo, E.; Chiba, S.; Mori, H.; Nishimura, O.; Ito, K.; Akiyama, Y.
    Post-liberation cleavage of signal peptides is catalyzed by the site-2 protease (S2P) in bacteria (2011), Proc. Natl. Acad. Sci. USA, 108, 13740-13745.
    View publication on PubMedView publication on EuropePMC

Protein Variants

Protein Variants Comment Organism
H22F active site mutant Bacillus subtilis
H22F active site mutant Escherichia coli

Localization

Localization Comment Organism GeneOntology No. Textmining
cytoplasmic membrane
-
Bacillus subtilis
-
-
cytoplasmic membrane
-
Escherichia coli
-
-

Metals/Ions

Metals/Ions Comment Organism Structure
Zn2+ a zinc metalloprotease Bacillus subtilis
Zn2+ a zinc metalloprotease Escherichia coli

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
45000
-
x * 45000, SDS-PAGE Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
beta-lactamase signal peptide + H2O Escherichia coli cleaves within the hydrophobic core at Pro12-Phe13. Cleavage of signal peptide requires a preceding processing of preproteins by Lep ?
-
?
LivK signal peptide + H2O Bacillus subtilis
-
?
-
?
MSIQHFRVALIPFFAAFCLPVFA + H2O Escherichia coli
-
MSIQHFRVALIP + FFAAFCLPVFA
-
?
RseA protein + H2O Escherichia coli
-
?
-
?

Organism

Organism UniProt Comment Textmining
Bacillus subtilis
-
-
-
Escherichia coli
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
beta-lactamase signal peptide + H2O cleaves within the hydrophobic core at Pro12-Phe13. Cleavage of signal peptide requires a preceding processing of preproteins by Lep Escherichia coli ?
-
?
LivK signal peptide + H2O
-
Bacillus subtilis ?
-
?
MSIQHFRVALIPFFAAFCLPVFA + H2O
-
Escherichia coli MSIQHFRVALIP + FFAAFCLPVFA
-
?
RseA protein + H2O
-
Escherichia coli ?
-
?

Subunits

Subunits Comment Organism
? x * 45000, SDS-PAGE Escherichia coli

Synonyms

Synonyms Comment Organism
I-CLiP
-
Bacillus subtilis
intramembrane-cleaving protease
-
Bacillus subtilis
intramembrane-cleaving protease
-
Escherichia coli
RasP
-
Bacillus subtilis
RseP
-
Escherichia coli
S2P
-
Bacillus subtilis
S2P
-
Escherichia coli
site-2 protease
-
Bacillus subtilis
site-2 protease
-
Escherichia coli

General Information

General Information Comment Organism
physiological function RasP is involved in transmembrane stress signal transduction Bacillus subtilis
physiological function RseP introduces a cleavage into signal peptides after their signal peptidase-mediated liberation from preproteins. The enzyme is involved in degradation of remnant signal peptides left in the bacterial cytoplasmic membrane Escherichia coli