node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
fliY | rsbP | BSU16320 | BSU34110 | Flagellar motor switching and energizing phosphatase; Component of the flagellar switch. Binds CheY-P and increases its hydrolysis rate in vitro. May function constitutively to remove CheY-P around the flagellar switch to maintain an optimal level of CheY-P whereas CheC may function after addition of an attractant to cope with increased levels of CheY-P; Belongs to the FliN/MopA/SpaO family. | Serine phosphatase; Positive regulator of sigma-B activity. Dephosphorylates RsbV in response to energy stress. | 0.506 |
fliY | rsbRA | BSU16320 | BSU04670 | Flagellar motor switching and energizing phosphatase; Component of the flagellar switch. Binds CheY-P and increases its hydrolysis rate in vitro. May function constitutively to remove CheY-P around the flagellar switch to maintain an optimal level of CheY-P whereas CheC may function after addition of an attractant to cope with increased levels of CheY-P; Belongs to the FliN/MopA/SpaO family. | 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. | 0.842 |
fliY | rsbS | BSU16320 | BSU04680 | Flagellar motor switching and energizing phosphatase; Component of the flagellar switch. Binds CheY-P and increases its hydrolysis rate in vitro. May function constitutively to remove CheY-P around the flagellar switch to maintain an optimal level of CheY-P whereas CheC may function after addition of an attractant to cope with increased levels of CheY-P; Belongs to the FliN/MopA/SpaO family. | 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. | 0.842 |
fliY | rsbT | BSU16320 | BSU04690 | Flagellar motor switching and energizing phosphatase; Component of the flagellar switch. Binds CheY-P and increases its hydrolysis rate in vitro. May function constitutively to remove CheY-P around the flagellar switch to maintain an optimal level of CheY-P whereas CheC may function after addition of an attractant to cope with increased levels of CheY-P; Belongs to the FliN/MopA/SpaO family. | 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 [...] | 0.497 |
fliY | rsbU | BSU16320 | BSU04700 | Flagellar motor switching and energizing phosphatase; Component of the flagellar switch. Binds CheY-P and increases its hydrolysis rate in vitro. May function constitutively to remove CheY-P around the flagellar switch to maintain an optimal level of CheY-P whereas CheC may function after addition of an attractant to cope with increased levels of CheY-P; Belongs to the FliN/MopA/SpaO family. | Serine phosphatase; Positive regulator of sigma-B activity. Dephosphorylates RsbV in response to environmental stress conveyed from the RsbXST module. | 0.505 |
fliY | rsbV | BSU16320 | BSU04710 | Flagellar motor switching and energizing phosphatase; Component of the flagellar switch. Binds CheY-P and increases its hydrolysis rate in vitro. May function constitutively to remove CheY-P around the flagellar switch to maintain an optimal level of CheY-P whereas CheC may function after addition of an attractant to cope with increased levels of CheY-P; Belongs to the FliN/MopA/SpaO family. | 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. | 0.842 |
fliY | rsbW | BSU16320 | BSU04720 | Flagellar motor switching and energizing phosphatase; Component of the flagellar switch. Binds CheY-P and increases its hydrolysis rate in vitro. May function constitutively to remove CheY-P around the flagellar switch to maintain an optimal level of CheY-P whereas CheC may function after addition of an attractant to cope with increased levels of CheY-P; Belongs to the FliN/MopA/SpaO family. | 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). | 0.497 |
fliY | rsbX | BSU16320 | BSU04740 | Flagellar motor switching and energizing phosphatase; Component of the flagellar switch. Binds CheY-P and increases its hydrolysis rate in vitro. May function constitutively to remove CheY-P around the flagellar switch to maintain an optimal level of CheY-P whereas CheC may function after addition of an attractant to cope with increased levels of CheY-P; Belongs to the FliN/MopA/SpaO family. | Serine phosphatase; Negative regulator of sigma-B activity. Dephosphorylates RsbS. Plays a role both in maintaining low sigma-B activity during growth and in reestablishing prestress sigma-B activity after induction. Could have a negative feedback role by indirectly communicating sigma-B protein levels. | 0.502 |
rsbP | fliY | BSU34110 | BSU16320 | Serine phosphatase; Positive regulator of sigma-B activity. Dephosphorylates RsbV in response to energy stress. | Flagellar motor switching and energizing phosphatase; Component of the flagellar switch. Binds CheY-P and increases its hydrolysis rate in vitro. May function constitutively to remove CheY-P around the flagellar switch to maintain an optimal level of CheY-P whereas CheC may function after addition of an attractant to cope with increased levels of CheY-P; Belongs to the FliN/MopA/SpaO family. | 0.506 |
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 | 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 | rsbU | BSU34110 | BSU04700 | Serine phosphatase; Positive regulator of sigma-B activity. Dephosphorylates RsbV in response to energy stress. | Serine phosphatase; Positive regulator of sigma-B activity. Dephosphorylates RsbV in response to environmental stress conveyed from the RsbXST module. | 0.552 |
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 | rsbX | BSU34110 | BSU04740 | Serine phosphatase; Positive regulator of sigma-B activity. Dephosphorylates RsbV in response to energy stress. | Serine phosphatase; Negative regulator of sigma-B activity. Dephosphorylates RsbS. Plays a role both in maintaining low sigma-B activity during growth and in reestablishing prestress sigma-B activity after induction. Could have a negative feedback role by indirectly communicating sigma-B protein levels. | 0.860 |
rsbP | sigB | BSU34110 | BSU04730 | Serine phosphatase; Positive regulator of sigma-B activity. Dephosphorylates RsbV in response to energy stress. | RNA polymerase sigma-37 factor (sigma(B)); Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released. Sigma B is not essential for sporulation; rather it is required for maximal expression of ctc and csbA which are transcribed in the early stationary phase under conditions inimical to sporulation. May play a role in the ability of the bacterium to adapt to various stresses but is not essential for its survival under these conditions. Positively regulates expression of its own operon; Belongs to the sigma-70 fac [...] | 0.800 |
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 |