EC Number   |
General Information |
Reference |
|---|
   3.4.21.89 | evolution |
bacterial type I signal peptidase is evolutionarily related to the penicillin-binding proteins (PBPs) |
-, 752371 |
| 3.4.21.89 | evolution |
Escherichia coli and Bacillus subtilis primarily express a signal peptidase I contains a serine-lysine catalytic dyad, whilst those of archaeal and eukaryotic origin generally have a serine-histidine catalytic dyad |
-, 752663 |
| 3.4.21.89 | evolution |
Escherichia coli and Bacillus subtilis primarily express a signal peptidase I contains a serine-lysine catalytic dyad, whilst those of archaeal and eukaryotic origin generally have a serine-histidine catalytic dyad. Bacillus subtilis contains five chromosomally encoded signal peptidases |
-, 752663 |
| 3.4.21.89 | evolution |
Escherichia coli and Bacillus subtilis primarily express a signal peptidase I that contains a serine-lysine catalytic dyad, whilst those of archaeal and eukaryotic origin generally have a serine-histidine catalytic dyad |
752663 |
| 3.4.21.89 | evolution |
evolutionary adaptation from the ribosome-dependent co-translational insertion to the chaperone-dependent post-translational transport of SPase I |
754121 |
| 3.4.21.89 | malfunction |
potential consequences of SPase inhibition on bacterial virulence, overview. The antivirulence effects of inhibiting SPase are expected due to the many proteinaceous virulence factors that rely on SPase for processing into functional forms. SPase inhibition results in the accumulation of unprocessed proteins in the cytoplasmic membrane, which eventually causes it to lose its integrity and leads to cell death |
-, 752959 |
| 3.4.21.89 | malfunction |
potential consequences of SPase inhibition on bacterial virulence, overview. The antivirulence effects of inhibiting SPase are expected due to the many proteinaceous virulence factors that rely on SPase for processing into functional forms. SPase inhibition results in the accumulation of unprocessed proteins in the cytoplasmic membrane, which eventually causes it to lose its integrity and leads to cell death. Deletion of sipZ results in an almost complete loss of infectivity in a mouse model |
752959 |
| 3.4.21.89 | malfunction |
Staphylococcus aureus bacteria lacking the SPase I SpsB are viable and able to grow in vitro when overexpressing a native gene cassette encoding for a putative ABC transporter. This transporter apparently compensates for SpsB's essential function by mediating alternative cleavage of a subset of proteins at a site distinct from the SpsB-cleavage site, leading to SpsB-independent secretion |
754636 |
| 3.4.21.89 | malfunction |
the biofilm mutant, DELTASSA_0351, is deficient in type I signal peptidase (SPase), phenotype, overview. Proteomic analysis of mutant strain DELTASSA_0351, list of transcripts that are differentially regulated in DELTASSA_0351 |
-, 754659 |
| 3.4.21.89 | metabolism |
SPase may influence flagellar assembly and type IV secretion systems (T4SSs), as components of the translocation machinery itself are predicted to require SPase processing.79,80 For example, the T4SS mediates the direct transfer of proteins into target cells, but is perhaps best known for its role in the direct transfer of DNA, as this has been implicated as a primary means by which bacteria acquire foreign DNA leading to antibiotic resistance |
752959 |
