node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
ctpA | rseP | BSU19590 | BSU16560 | Carboxy-terminal processing protease; Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; enzyme. | Regulator of sigma-W protease RasP; Is responsible for site-2 cleavage of the RsiW anti-sigma factor. This results, after a third proteolytic step catalyzed by the ClpXP protease, in the release of SigW and the transcription activation of the genes under the control of the sigma-W factor. Can also cleave liberated signal peptides of PenP and Mpr, probably within in the cell membrane. | 0.596 |
ctpA | ylbL | BSU19590 | BSU15050 | Carboxy-terminal processing protease; Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; enzyme. | Putative degradative enzyme; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme. | 0.845 |
ctpB | rseP | BSU35240 | BSU16560 | Swarming motility protein; Involved in the signal transduction pathway leading to the proteolytic activation of the mother cell transcription factor pro- sigma-K during sporulation. The signaling serine protease CtpB triggers pro-sigma-K processing by cleaving the pre-processed regulatory protein SpoIVFA and is necessary for the proper timing of sigma-K activation. Belongs to the peptidase S41A family. | Regulator of sigma-W protease RasP; Is responsible for site-2 cleavage of the RsiW anti-sigma factor. This results, after a third proteolytic step catalyzed by the ClpXP protease, in the release of SigW and the transcription activation of the genes under the control of the sigma-W factor. Can also cleave liberated signal peptides of PenP and Mpr, probably within in the cell membrane. | 0.822 |
ctpB | spoIVB | BSU35240 | BSU24230 | Swarming motility protein; Involved in the signal transduction pathway leading to the proteolytic activation of the mother cell transcription factor pro- sigma-K during sporulation. The signaling serine protease CtpB triggers pro-sigma-K processing by cleaving the pre-processed regulatory protein SpoIVFA and is necessary for the proper timing of sigma-K activation. Belongs to the peptidase S41A family. | Regulatory membrane-associated serine protease; Plays a central role in the sigma-K checkpoint which coordinates gene expression during the later stages of spore formation. The protease is activated by trans cleavage of the zymogen precursor producing SpoIVB-45 kDa. This undergoes further trimming by cis cleavage to form SpoIVB-43 kDa and SpoIVB-42 kDa. The protease then cleaves the C-terminus of the SpoIVFA metalloprotease activating the latter. | 0.945 |
htrA | htrB | BSU12900 | BSU33000 | Membrane bound serine protease Do, quality control protease (heat-shock protein); Degrades abnormal exported proteins and responsible for the propeptide processing of a natural pro-protein and for the maturation of a native protein. It also plays a prominent role in stress (heat shock, ethanol, puromycin and NaCl) resistance during active exponential growth (Probable); Belongs to the peptidase S1C family. | HtrA-like serine protease; Degrades abnormal exported proteins and responsible for the propeptide processing of a natural pro-protein and for the maturation of a native protein. It also plays a prominent role in stress (heat shock, ethanol, puromycin and NaCl) resistance during active exponential growth (Probable); Belongs to the peptidase S1C family. | 0.974 |
htrA | rseP | BSU12900 | BSU16560 | Membrane bound serine protease Do, quality control protease (heat-shock protein); Degrades abnormal exported proteins and responsible for the propeptide processing of a natural pro-protein and for the maturation of a native protein. It also plays a prominent role in stress (heat shock, ethanol, puromycin and NaCl) resistance during active exponential growth (Probable); Belongs to the peptidase S1C family. | Regulator of sigma-W protease RasP; Is responsible for site-2 cleavage of the RsiW anti-sigma factor. This results, after a third proteolytic step catalyzed by the ClpXP protease, in the release of SigW and the transcription activation of the genes under the control of the sigma-W factor. Can also cleave liberated signal peptides of PenP and Mpr, probably within in the cell membrane. | 0.825 |
htrB | htrA | BSU33000 | BSU12900 | HtrA-like serine protease; Degrades abnormal exported proteins and responsible for the propeptide processing of a natural pro-protein and for the maturation of a native protein. It also plays a prominent role in stress (heat shock, ethanol, puromycin and NaCl) resistance during active exponential growth (Probable); Belongs to the peptidase S1C family. | Membrane bound serine protease Do, quality control protease (heat-shock protein); Degrades abnormal exported proteins and responsible for the propeptide processing of a natural pro-protein and for the maturation of a native protein. It also plays a prominent role in stress (heat shock, ethanol, puromycin and NaCl) resistance during active exponential growth (Probable); Belongs to the peptidase S1C family. | 0.974 |
htrB | rseP | BSU33000 | BSU16560 | HtrA-like serine protease; Degrades abnormal exported proteins and responsible for the propeptide processing of a natural pro-protein and for the maturation of a native protein. It also plays a prominent role in stress (heat shock, ethanol, puromycin and NaCl) resistance during active exponential growth (Probable); Belongs to the peptidase S1C family. | Regulator of sigma-W protease RasP; Is responsible for site-2 cleavage of the RsiW anti-sigma factor. This results, after a third proteolytic step catalyzed by the ClpXP protease, in the release of SigW and the transcription activation of the genes under the control of the sigma-W factor. Can also cleave liberated signal peptides of PenP and Mpr, probably within in the cell membrane. | 0.824 |
htrC | rseP | BSU40360 | BSU16560 | Putative sensor protein; Evidence 7: Gene remnant; Product type pr: putative regulator. | Regulator of sigma-W protease RasP; Is responsible for site-2 cleavage of the RsiW anti-sigma factor. This results, after a third proteolytic step catalyzed by the ClpXP protease, in the release of SigW and the transcription activation of the genes under the control of the sigma-W factor. Can also cleave liberated signal peptides of PenP and Mpr, probably within in the cell membrane. | 0.616 |
rseP | ctpA | BSU16560 | BSU19590 | Regulator of sigma-W protease RasP; Is responsible for site-2 cleavage of the RsiW anti-sigma factor. This results, after a third proteolytic step catalyzed by the ClpXP protease, in the release of SigW and the transcription activation of the genes under the control of the sigma-W factor. Can also cleave liberated signal peptides of PenP and Mpr, probably within in the cell membrane. | Carboxy-terminal processing protease; Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; enzyme. | 0.596 |
rseP | ctpB | BSU16560 | BSU35240 | Regulator of sigma-W protease RasP; Is responsible for site-2 cleavage of the RsiW anti-sigma factor. This results, after a third proteolytic step catalyzed by the ClpXP protease, in the release of SigW and the transcription activation of the genes under the control of the sigma-W factor. Can also cleave liberated signal peptides of PenP and Mpr, probably within in the cell membrane. | Swarming motility protein; Involved in the signal transduction pathway leading to the proteolytic activation of the mother cell transcription factor pro- sigma-K during sporulation. The signaling serine protease CtpB triggers pro-sigma-K processing by cleaving the pre-processed regulatory protein SpoIVFA and is necessary for the proper timing of sigma-K activation. Belongs to the peptidase S41A family. | 0.822 |
rseP | htrA | BSU16560 | BSU12900 | Regulator of sigma-W protease RasP; Is responsible for site-2 cleavage of the RsiW anti-sigma factor. This results, after a third proteolytic step catalyzed by the ClpXP protease, in the release of SigW and the transcription activation of the genes under the control of the sigma-W factor. Can also cleave liberated signal peptides of PenP and Mpr, probably within in the cell membrane. | Membrane bound serine protease Do, quality control protease (heat-shock protein); Degrades abnormal exported proteins and responsible for the propeptide processing of a natural pro-protein and for the maturation of a native protein. It also plays a prominent role in stress (heat shock, ethanol, puromycin and NaCl) resistance during active exponential growth (Probable); Belongs to the peptidase S1C family. | 0.825 |
rseP | htrB | BSU16560 | BSU33000 | Regulator of sigma-W protease RasP; Is responsible for site-2 cleavage of the RsiW anti-sigma factor. This results, after a third proteolytic step catalyzed by the ClpXP protease, in the release of SigW and the transcription activation of the genes under the control of the sigma-W factor. Can also cleave liberated signal peptides of PenP and Mpr, probably within in the cell membrane. | HtrA-like serine protease; Degrades abnormal exported proteins and responsible for the propeptide processing of a natural pro-protein and for the maturation of a native protein. It also plays a prominent role in stress (heat shock, ethanol, puromycin and NaCl) resistance during active exponential growth (Probable); Belongs to the peptidase S1C family. | 0.824 |
rseP | htrC | BSU16560 | BSU40360 | Regulator of sigma-W protease RasP; Is responsible for site-2 cleavage of the RsiW anti-sigma factor. This results, after a third proteolytic step catalyzed by the ClpXP protease, in the release of SigW and the transcription activation of the genes under the control of the sigma-W factor. Can also cleave liberated signal peptides of PenP and Mpr, probably within in the cell membrane. | Putative sensor protein; Evidence 7: Gene remnant; Product type pr: putative regulator. | 0.616 |
rseP | spoIVB | BSU16560 | BSU24230 | Regulator of sigma-W protease RasP; Is responsible for site-2 cleavage of the RsiW anti-sigma factor. This results, after a third proteolytic step catalyzed by the ClpXP protease, in the release of SigW and the transcription activation of the genes under the control of the sigma-W factor. Can also cleave liberated signal peptides of PenP and Mpr, probably within in the cell membrane. | Regulatory membrane-associated serine protease; Plays a central role in the sigma-K checkpoint which coordinates gene expression during the later stages of spore formation. The protease is activated by trans cleavage of the zymogen precursor producing SpoIVB-45 kDa. This undergoes further trimming by cis cleavage to form SpoIVB-43 kDa and SpoIVB-42 kDa. The protease then cleaves the C-terminus of the SpoIVFA metalloprotease activating the latter. | 0.456 |
rseP | ylbL | BSU16560 | BSU15050 | Regulator of sigma-W protease RasP; Is responsible for site-2 cleavage of the RsiW anti-sigma factor. This results, after a third proteolytic step catalyzed by the ClpXP protease, in the release of SigW and the transcription activation of the genes under the control of the sigma-W factor. Can also cleave liberated signal peptides of PenP and Mpr, probably within in the cell membrane. | Putative degradative enzyme; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme. | 0.483 |
spoIVB | ctpB | BSU24230 | BSU35240 | Regulatory membrane-associated serine protease; Plays a central role in the sigma-K checkpoint which coordinates gene expression during the later stages of spore formation. The protease is activated by trans cleavage of the zymogen precursor producing SpoIVB-45 kDa. This undergoes further trimming by cis cleavage to form SpoIVB-43 kDa and SpoIVB-42 kDa. The protease then cleaves the C-terminus of the SpoIVFA metalloprotease activating the latter. | Swarming motility protein; Involved in the signal transduction pathway leading to the proteolytic activation of the mother cell transcription factor pro- sigma-K during sporulation. The signaling serine protease CtpB triggers pro-sigma-K processing by cleaving the pre-processed regulatory protein SpoIVFA and is necessary for the proper timing of sigma-K activation. Belongs to the peptidase S41A family. | 0.945 |
spoIVB | rseP | BSU24230 | BSU16560 | Regulatory membrane-associated serine protease; Plays a central role in the sigma-K checkpoint which coordinates gene expression during the later stages of spore formation. The protease is activated by trans cleavage of the zymogen precursor producing SpoIVB-45 kDa. This undergoes further trimming by cis cleavage to form SpoIVB-43 kDa and SpoIVB-42 kDa. The protease then cleaves the C-terminus of the SpoIVFA metalloprotease activating the latter. | Regulator of sigma-W protease RasP; Is responsible for site-2 cleavage of the RsiW anti-sigma factor. This results, after a third proteolytic step catalyzed by the ClpXP protease, in the release of SigW and the transcription activation of the genes under the control of the sigma-W factor. Can also cleave liberated signal peptides of PenP and Mpr, probably within in the cell membrane. | 0.456 |
ylbL | ctpA | BSU15050 | BSU19590 | Putative degradative enzyme; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme. | Carboxy-terminal processing protease; Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; enzyme. | 0.845 |
ylbL | rseP | BSU15050 | BSU16560 | Putative degradative enzyme; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme. | Regulator of sigma-W protease RasP; Is responsible for site-2 cleavage of the RsiW anti-sigma factor. This results, after a third proteolytic step catalyzed by the ClpXP protease, in the release of SigW and the transcription activation of the genes under the control of the sigma-W factor. Can also cleave liberated signal peptides of PenP and Mpr, probably within in the cell membrane. | 0.483 |