node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
cheV | flgB | BSU14010 | BSU16180 | Coupling protein and response regulator for CheA activity in response to attractants (chemotaxis); Involved in the transmission of sensory signals from the chemoreceptors to the flagellar motors. Chemotaxis involves both a phosphorylation-dependent excitation and a methylation-dependent adaptation. CheV and CheW are involved in the coupling of the methyl- accepting chemoreceptors to the central two-component kinase CheA; they are both necessary for efficient chemotaxis. Moreover, CheA-dependent phosphorylation of CheV is required for adaptation to attractants during B.subtilis chemotaxis. | Flagellar component of cell-proximal portion of basal-body rod; Structural component of flagellum, the bacterial motility apparatus. Part of the rod structure of flagellar basal body. | 0.953 |
cheV | flgC | BSU14010 | BSU16190 | Coupling protein and response regulator for CheA activity in response to attractants (chemotaxis); Involved in the transmission of sensory signals from the chemoreceptors to the flagellar motors. Chemotaxis involves both a phosphorylation-dependent excitation and a methylation-dependent adaptation. CheV and CheW are involved in the coupling of the methyl- accepting chemoreceptors to the central two-component kinase CheA; they are both necessary for efficient chemotaxis. Moreover, CheA-dependent phosphorylation of CheV is required for adaptation to attractants during B.subtilis chemotaxis. | Flagellar component of cell-proximal portion of basal-body rod; Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; Product type s: structure; Belongs to the flagella basal body rod proteins family. | 0.931 |
cheV | flgK | BSU14010 | BSU35410 | Coupling protein and response regulator for CheA activity in response to attractants (chemotaxis); Involved in the transmission of sensory signals from the chemoreceptors to the flagellar motors. Chemotaxis involves both a phosphorylation-dependent excitation and a methylation-dependent adaptation. CheV and CheW are involved in the coupling of the methyl- accepting chemoreceptors to the central two-component kinase CheA; they are both necessary for efficient chemotaxis. Moreover, CheA-dependent phosphorylation of CheV is required for adaptation to attractants during B.subtilis chemotaxis. | Flagellar hook-filament junction; Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; structure. | 0.976 |
cheV | fliG | BSU14010 | BSU16220 | Coupling protein and response regulator for CheA activity in response to attractants (chemotaxis); Involved in the transmission of sensory signals from the chemoreceptors to the flagellar motors. Chemotaxis involves both a phosphorylation-dependent excitation and a methylation-dependent adaptation. CheV and CheW are involved in the coupling of the methyl- accepting chemoreceptors to the central two-component kinase CheA; they are both necessary for efficient chemotaxis. Moreover, CheA-dependent phosphorylation of CheV is required for adaptation to attractants during B.subtilis chemotaxis. | Flagellar motor switching and energizing component; One of the proteins that forms a switch complex that is proposed to be located at the base of the basal body. This complex interacts with chemotaxis proteins (such as CheY) in addition to contacting components of the motor that determine the direction of flagellar rotation; Belongs to the FliG family. | 0.912 |
cheV | fliS | BSU14010 | BSU35330 | Coupling protein and response regulator for CheA activity in response to attractants (chemotaxis); Involved in the transmission of sensory signals from the chemoreceptors to the flagellar motors. Chemotaxis involves both a phosphorylation-dependent excitation and a methylation-dependent adaptation. CheV and CheW are involved in the coupling of the methyl- accepting chemoreceptors to the central two-component kinase CheA; they are both necessary for efficient chemotaxis. Moreover, CheA-dependent phosphorylation of CheV is required for adaptation to attractants during B.subtilis chemotaxis. | Flagellar assembly protein FliS; Essential for filament assembly. May act as a facilitator of flagellin (hag) secretion. Antagonizes translational repressor CsrA indirectly. Belongs to the FliS family. | 0.993 |
cheV | fliY | BSU14010 | BSU16320 | Coupling protein and response regulator for CheA activity in response to attractants (chemotaxis); Involved in the transmission of sensory signals from the chemoreceptors to the flagellar motors. Chemotaxis involves both a phosphorylation-dependent excitation and a methylation-dependent adaptation. CheV and CheW are involved in the coupling of the methyl- accepting chemoreceptors to the central two-component kinase CheA; they are both necessary for efficient chemotaxis. Moreover, CheA-dependent phosphorylation of CheV is required for adaptation to attractants during B.subtilis chemotaxis. | 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. | 0.999 |
cheV | motA | BSU14010 | BSU13690 | Coupling protein and response regulator for CheA activity in response to attractants (chemotaxis); Involved in the transmission of sensory signals from the chemoreceptors to the flagellar motors. Chemotaxis involves both a phosphorylation-dependent excitation and a methylation-dependent adaptation. CheV and CheW are involved in the coupling of the methyl- accepting chemoreceptors to the central two-component kinase CheA; they are both necessary for efficient chemotaxis. Moreover, CheA-dependent phosphorylation of CheV is required for adaptation to attractants during B.subtilis chemotaxis. | Motility protein A; MotA and MotB comprise the stator element of the flagellar motor complex. Required for rotation of the flagellar motor. Probable transmembrane proton channel (By similarity). | 0.972 |
cheV | motB | BSU14010 | BSU13680 | Coupling protein and response regulator for CheA activity in response to attractants (chemotaxis); Involved in the transmission of sensory signals from the chemoreceptors to the flagellar motors. Chemotaxis involves both a phosphorylation-dependent excitation and a methylation-dependent adaptation. CheV and CheW are involved in the coupling of the methyl- accepting chemoreceptors to the central two-component kinase CheA; they are both necessary for efficient chemotaxis. Moreover, CheA-dependent phosphorylation of CheV is required for adaptation to attractants during B.subtilis chemotaxis. | Motility protein B; MotA and MotB comprise the stator element of the flagellar motor complex. Required for the rotation of the flagellar motor. Might be a linker that fastens the torque-generating machinery to the cell wall (By similarity). | 0.983 |
cheV | ytxD | BSU14010 | BSU29730 | Coupling protein and response regulator for CheA activity in response to attractants (chemotaxis); Involved in the transmission of sensory signals from the chemoreceptors to the flagellar motors. Chemotaxis involves both a phosphorylation-dependent excitation and a methylation-dependent adaptation. CheV and CheW are involved in the coupling of the methyl- accepting chemoreceptors to the central two-component kinase CheA; they are both necessary for efficient chemotaxis. Moreover, CheA-dependent phosphorylation of CheV is required for adaptation to attractants during B.subtilis chemotaxis. | Putative flagellar motor component; May be involved in some transport function; Belongs to the MotA family. | 0.920 |
cheV | ytxE | BSU14010 | BSU29720 | Coupling protein and response regulator for CheA activity in response to attractants (chemotaxis); Involved in the transmission of sensory signals from the chemoreceptors to the flagellar motors. Chemotaxis involves both a phosphorylation-dependent excitation and a methylation-dependent adaptation. CheV and CheW are involved in the coupling of the methyl- accepting chemoreceptors to the central two-component kinase CheA; they are both necessary for efficient chemotaxis. Moreover, CheA-dependent phosphorylation of CheV is required for adaptation to attractants during B.subtilis chemotaxis. | Putative flagellar motor apparatus component; May be involved in some transport function; Belongs to the MotB family. | 0.897 |
flgB | cheV | BSU16180 | BSU14010 | Flagellar component of cell-proximal portion of basal-body rod; Structural component of flagellum, the bacterial motility apparatus. Part of the rod structure of flagellar basal body. | Coupling protein and response regulator for CheA activity in response to attractants (chemotaxis); Involved in the transmission of sensory signals from the chemoreceptors to the flagellar motors. Chemotaxis involves both a phosphorylation-dependent excitation and a methylation-dependent adaptation. CheV and CheW are involved in the coupling of the methyl- accepting chemoreceptors to the central two-component kinase CheA; they are both necessary for efficient chemotaxis. Moreover, CheA-dependent phosphorylation of CheV is required for adaptation to attractants during B.subtilis chemotaxis. | 0.953 |
flgB | flgC | BSU16180 | BSU16190 | Flagellar component of cell-proximal portion of basal-body rod; Structural component of flagellum, the bacterial motility apparatus. Part of the rod structure of flagellar basal body. | Flagellar component of cell-proximal portion of basal-body rod; Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; Product type s: structure; Belongs to the flagella basal body rod proteins family. | 0.999 |
flgB | flgK | BSU16180 | BSU35410 | Flagellar component of cell-proximal portion of basal-body rod; Structural component of flagellum, the bacterial motility apparatus. Part of the rod structure of flagellar basal body. | Flagellar hook-filament junction; Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; structure. | 0.998 |
flgB | fliG | BSU16180 | BSU16220 | Flagellar component of cell-proximal portion of basal-body rod; Structural component of flagellum, the bacterial motility apparatus. Part of the rod structure of flagellar basal body. | Flagellar motor switching and energizing component; One of the proteins that forms a switch complex that is proposed to be located at the base of the basal body. This complex interacts with chemotaxis proteins (such as CheY) in addition to contacting components of the motor that determine the direction of flagellar rotation; Belongs to the FliG family. | 0.999 |
flgB | fliS | BSU16180 | BSU35330 | Flagellar component of cell-proximal portion of basal-body rod; Structural component of flagellum, the bacterial motility apparatus. Part of the rod structure of flagellar basal body. | Flagellar assembly protein FliS; Essential for filament assembly. May act as a facilitator of flagellin (hag) secretion. Antagonizes translational repressor CsrA indirectly. Belongs to the FliS family. | 0.994 |
flgB | fliY | BSU16180 | BSU16320 | Flagellar component of cell-proximal portion of basal-body rod; Structural component of flagellum, the bacterial motility apparatus. Part of the rod structure of flagellar basal body. | 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. | 0.998 |
flgB | motA | BSU16180 | BSU13690 | Flagellar component of cell-proximal portion of basal-body rod; Structural component of flagellum, the bacterial motility apparatus. Part of the rod structure of flagellar basal body. | Motility protein A; MotA and MotB comprise the stator element of the flagellar motor complex. Required for rotation of the flagellar motor. Probable transmembrane proton channel (By similarity). | 0.972 |
flgB | motB | BSU16180 | BSU13680 | Flagellar component of cell-proximal portion of basal-body rod; Structural component of flagellum, the bacterial motility apparatus. Part of the rod structure of flagellar basal body. | Motility protein B; MotA and MotB comprise the stator element of the flagellar motor complex. Required for the rotation of the flagellar motor. Might be a linker that fastens the torque-generating machinery to the cell wall (By similarity). | 0.986 |
flgB | ytxD | BSU16180 | BSU29730 | Flagellar component of cell-proximal portion of basal-body rod; Structural component of flagellum, the bacterial motility apparatus. Part of the rod structure of flagellar basal body. | Putative flagellar motor component; May be involved in some transport function; Belongs to the MotA family. | 0.951 |
flgB | ytxE | BSU16180 | BSU29720 | Flagellar component of cell-proximal portion of basal-body rod; Structural component of flagellum, the bacterial motility apparatus. Part of the rod structure of flagellar basal body. | Putative flagellar motor apparatus component; May be involved in some transport function; Belongs to the MotB family. | 0.909 |