node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
rsbP | rsbQ | BSU34110 | BSU34100 | Serine phosphatase; Positive regulator of sigma-B activity. Dephosphorylates RsbV in response to energy stress. | Regulator of RsbP phosphatase; Positive regulator required for energy stress activation of the sigma-B transcription factor. Could be required for RsbP phosphatase activity; Belongs to the AB hydrolase superfamily. | 0.998 |
rsbP | rsbRA | BSU34110 | BSU04670 | Serine phosphatase; Positive regulator of sigma-B activity. Dephosphorylates RsbV in response to energy stress. | Component of the piezosome (stressosome); Acts as a positive regulator of sigma-B activity in response to salt and heat stress by stimulating the activity of the RsbT kinase toward RsbS in vitro. Negative regulator of sigma-B activity. Non-phosphorylated RsbS binds to RsbT, preventing its association with RsbU. Requires any one of RsbRA, RsbRB, RsbRC or RsbRD to sequester RsbT. When RsbS and the RsbR paralog(s) are phosphorylated, they release RsbT, which can then bind and activate RsbU. | 0.967 |
rsbP | rsbRB | BSU34110 | BSU13200 | Serine phosphatase; Positive regulator of sigma-B activity. Dephosphorylates RsbV in response to energy stress. | Component of the piezosome (stressosome); One of 4 functionally non-identical RsbR paralogs, it functions in the environmental signaling branch of the general stress response. | 0.941 |
rsbP | rsbRC | BSU34110 | BSU19450 | Serine phosphatase; Positive regulator of sigma-B activity. Dephosphorylates RsbV in response to energy stress. | Component of the piezosome (stressosome); One of 4 functionally non-identical RsbR paralogs, it functions in the environmental signaling branch of the general stress response. | 0.908 |
rsbP | rsbRD | BSU34110 | BSU24760 | Serine phosphatase; Positive regulator of sigma-B activity. Dephosphorylates RsbV in response to energy stress. | Component of the piezosome (stressosome); One of 4 functionally non-identical RsbR paralogs, it functions in the environmental signaling branch of the general stress response. | 0.887 |
rsbP | rsbS | BSU34110 | BSU04680 | Serine phosphatase; Positive regulator of sigma-B activity. Dephosphorylates RsbV in response to energy stress. | Antagonist of RsbT; Negative regulator of sigma-B activity. Non-phosphorylated RsbS binds to RsbT, preventing its association with RsbU. Requires any one of RsbRA, RsbRB, RsbRC or RsbRD to sequester RsbT. When RsbS and the RsbR paralog(s) are phosphorylated, they release RsbT, which can then bind and activate RsbU. | 0.968 |
rsbP | rsbT | BSU34110 | BSU04690 | Serine phosphatase; Positive regulator of sigma-B activity. Dephosphorylates RsbV in response to energy stress. | Switch protein/serine-threonine kinase; Provides the crucial link between the upstream module (communication of environmental stress) and the downstream module (integration of the environmental signals with signals of energy stress) that compose the signal transduction pathway controlling the sigma-B factor. Phosphorylates and inactivates its specific antagonist protein RsbS thanks to its serine kinase activity. Upon phosphorylation of RsbS, RsbT is released to stimulate RsbU, a PP2C phosphatase, thereby initiating the signaling cascade that ultimately activates sigma-B. The activity o [...] | 0.976 |
rsbP | rsbV | BSU34110 | BSU04710 | Serine phosphatase; Positive regulator of sigma-B activity. Dephosphorylates RsbV in response to energy stress. | Anti-anti-sigma factor (antagonist of RsbW); Positive regulator of sigma-B activity. Non-phosphorylated RsbV binds to RsbW, preventing its association with sigma-B. When phosphorylated, releases RsbW, which is then free to complex with and inactivate sigma-B. | 0.977 |
rsbP | rsbW | BSU34110 | BSU04720 | Serine phosphatase; Positive regulator of sigma-B activity. Dephosphorylates RsbV in response to energy stress. | Switch protein/serine kinase and anti-sigma factor (inhibitory sigma-B binding protein); Negative regulator of sigma-B activity. Phosphorylates and inactivates its specific antagonist protein, RsbV. Upon phosphorylation of RsbV, RsbW is released and binds to sigma-B, thereby blocking its ability to form an RNA polymerase holoenzyme (E-sigma-B). | 0.981 |
rsbP | ytvA | BSU34110 | BSU30340 | Serine phosphatase; Positive regulator of sigma-B activity. Dephosphorylates RsbV in response to energy stress. | Blue light GTP-binding receptor; Exhibits the same spectroscopical features and blue-light induced photochemistry as plants phototropins, with the reversible formation of a blue-shifted photoproduct, assigned to an FMN-cysteine thiol adduct. Although it is a positive regulator in the activation of the environmental signaling branch of the general stress transcription factor sigma-B, its precise role is undetermined. | 0.973 |
rsbQ | rsbP | BSU34100 | BSU34110 | Regulator of RsbP phosphatase; Positive regulator required for energy stress activation of the sigma-B transcription factor. Could be required for RsbP phosphatase activity; Belongs to the AB hydrolase superfamily. | Serine phosphatase; Positive regulator of sigma-B activity. Dephosphorylates RsbV in response to energy stress. | 0.998 |
rsbQ | rsbRA | BSU34100 | BSU04670 | Regulator of RsbP phosphatase; Positive regulator required for energy stress activation of the sigma-B transcription factor. Could be required for RsbP phosphatase activity; Belongs to the AB hydrolase superfamily. | Component of the piezosome (stressosome); Acts as a positive regulator of sigma-B activity in response to salt and heat stress by stimulating the activity of the RsbT kinase toward RsbS in vitro. Negative regulator of sigma-B activity. Non-phosphorylated RsbS binds to RsbT, preventing its association with RsbU. Requires any one of RsbRA, RsbRB, RsbRC or RsbRD to sequester RsbT. When RsbS and the RsbR paralog(s) are phosphorylated, they release RsbT, which can then bind and activate RsbU. | 0.866 |
rsbQ | rsbRB | BSU34100 | BSU13200 | Regulator of RsbP phosphatase; Positive regulator required for energy stress activation of the sigma-B transcription factor. Could be required for RsbP phosphatase activity; Belongs to the AB hydrolase superfamily. | Component of the piezosome (stressosome); One of 4 functionally non-identical RsbR paralogs, it functions in the environmental signaling branch of the general stress response. | 0.724 |
rsbQ | rsbRC | BSU34100 | BSU19450 | Regulator of RsbP phosphatase; Positive regulator required for energy stress activation of the sigma-B transcription factor. Could be required for RsbP phosphatase activity; Belongs to the AB hydrolase superfamily. | Component of the piezosome (stressosome); One of 4 functionally non-identical RsbR paralogs, it functions in the environmental signaling branch of the general stress response. | 0.756 |
rsbQ | rsbRD | BSU34100 | BSU24760 | Regulator of RsbP phosphatase; Positive regulator required for energy stress activation of the sigma-B transcription factor. Could be required for RsbP phosphatase activity; Belongs to the AB hydrolase superfamily. | Component of the piezosome (stressosome); One of 4 functionally non-identical RsbR paralogs, it functions in the environmental signaling branch of the general stress response. | 0.642 |
rsbQ | rsbS | BSU34100 | BSU04680 | Regulator of RsbP phosphatase; Positive regulator required for energy stress activation of the sigma-B transcription factor. Could be required for RsbP phosphatase activity; Belongs to the AB hydrolase superfamily. | Antagonist of RsbT; Negative regulator of sigma-B activity. Non-phosphorylated RsbS binds to RsbT, preventing its association with RsbU. Requires any one of RsbRA, RsbRB, RsbRC or RsbRD to sequester RsbT. When RsbS and the RsbR paralog(s) are phosphorylated, they release RsbT, which can then bind and activate RsbU. | 0.868 |
rsbQ | rsbT | BSU34100 | BSU04690 | Regulator of RsbP phosphatase; Positive regulator required for energy stress activation of the sigma-B transcription factor. Could be required for RsbP phosphatase activity; Belongs to the AB hydrolase superfamily. | Switch protein/serine-threonine kinase; Provides the crucial link between the upstream module (communication of environmental stress) and the downstream module (integration of the environmental signals with signals of energy stress) that compose the signal transduction pathway controlling the sigma-B factor. Phosphorylates and inactivates its specific antagonist protein RsbS thanks to its serine kinase activity. Upon phosphorylation of RsbS, RsbT is released to stimulate RsbU, a PP2C phosphatase, thereby initiating the signaling cascade that ultimately activates sigma-B. The activity o [...] | 0.929 |
rsbQ | rsbV | BSU34100 | BSU04710 | Regulator of RsbP phosphatase; Positive regulator required for energy stress activation of the sigma-B transcription factor. Could be required for RsbP phosphatase activity; Belongs to the AB hydrolase superfamily. | Anti-anti-sigma factor (antagonist of RsbW); Positive regulator of sigma-B activity. Non-phosphorylated RsbV binds to RsbW, preventing its association with sigma-B. When phosphorylated, releases RsbW, which is then free to complex with and inactivate sigma-B. | 0.901 |
rsbQ | rsbW | BSU34100 | BSU04720 | Regulator of RsbP phosphatase; Positive regulator required for energy stress activation of the sigma-B transcription factor. Could be required for RsbP phosphatase activity; Belongs to the AB hydrolase superfamily. | Switch protein/serine kinase and anti-sigma factor (inhibitory sigma-B binding protein); Negative regulator of sigma-B activity. Phosphorylates and inactivates its specific antagonist protein, RsbV. Upon phosphorylation of RsbV, RsbW is released and binds to sigma-B, thereby blocking its ability to form an RNA polymerase holoenzyme (E-sigma-B). | 0.895 |
rsbQ | ytvA | BSU34100 | BSU30340 | Regulator of RsbP phosphatase; Positive regulator required for energy stress activation of the sigma-B transcription factor. Could be required for RsbP phosphatase activity; Belongs to the AB hydrolase superfamily. | Blue light GTP-binding receptor; Exhibits the same spectroscopical features and blue-light induced photochemistry as plants phototropins, with the reversible formation of a blue-shifted photoproduct, assigned to an FMN-cysteine thiol adduct. Although it is a positive regulator in the activation of the environmental signaling branch of the general stress transcription factor sigma-B, its precise role is undetermined. | 0.752 |