| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| barA | cheA | STM2958 | STM1921 | Sensory histidine kinase; Similar to E. coli sensor-regulator, activates OmpR by phophorylation (AAC75828.1); Blastp hit to AAC75828.1 (918 aa), 90% identity in aa 1 - 918. | Sensory histitine protein kinase; Involved in the transmission of sensory signals from the chemoreceptors to the flagellar motors. CheA is autophosphorylated; it can transfer its phosphate group to either CheB or CheY. | 0.797 |
| barA | flhA | STM2958 | STM1913 | Sensory histidine kinase; Similar to E. coli sensor-regulator, activates OmpR by phophorylation (AAC75828.1); Blastp hit to AAC75828.1 (918 aa), 90% identity in aa 1 - 918. | Flagellar biosynthesis protein; Required for formation of the rod structure of the flagellar apparatus. Together with FliI and FliH, may constitute the export apparatus of flagellin. | 0.607 |
| barA | fliG | STM2958 | STM1970 | Sensory histidine kinase; Similar to E. coli sensor-regulator, activates OmpR by phophorylation (AAC75828.1); Blastp hit to AAC75828.1 (918 aa), 90% identity in aa 1 - 918. | Flagellar biosynthesis protein; FliG is one of three proteins (FliG, FliN, FliM) that forms the rotor-mounted switch complex (C ring), located at the base of the basal body. This complex interacts with the CheY and CheZ chemotaxis proteins, in addition to contacting components of the motor that determine the direction of flagellar rotation (By similarity). | 0.869 |
| barA | fliM | STM2958 | STM1976 | Sensory histidine kinase; Similar to E. coli sensor-regulator, activates OmpR by phophorylation (AAC75828.1); Blastp hit to AAC75828.1 (918 aa), 90% identity in aa 1 - 918. | Flagellar biosynthesis protein; FliM is one of three proteins (FliG, FliN, FliM) that forms the rotor-mounted switch complex (C ring), located at the base of the basal body. This complex interacts with the CheY and CheZ chemotaxis proteins, in addition to contacting components of the motor that determine the direction of flagellar rotation (By similarity). | 0.839 |
| barA | glnL | STM2958 | STM4006 | Sensory histidine kinase; Similar to E. coli sensor-regulator, activates OmpR by phophorylation (AAC75828.1); Blastp hit to AAC75828.1 (918 aa), 90% identity in aa 1 - 918. | Sensory histidine kinase/phosphatase NtrB; Member of the two-component regulatory system NtrB/NtrC, which controls expression of the nitrogen-regulated (ntr) genes in response to nitrogen limitation. Under conditions of nitrogen limitation, NtrB autophosphorylates and transfers the phosphoryl group to NtrC. In the presence of nitrogen, acts as a phosphatase that dephosphorylates and inactivates NtrC. | 0.586 |
| barA | hydG | STM2958 | STM4174 | Sensory histidine kinase; Similar to E. coli sensor-regulator, activates OmpR by phophorylation (AAC75828.1); Blastp hit to AAC75828.1 (918 aa), 90% identity in aa 1 - 918. | Response regulator in two-component reguatory system with HydH; Member of the two-component regulatory system ZraS/ZraR. When activated by ZraS it acts in conjunction with sigma-54 to regulate the expression of zraP. Positively autoregulates the expression of the zraSR operon (By similarity). | 0.643 |
| barA | hydH | STM2958 | STM4173 | Sensory histidine kinase; Similar to E. coli sensor-regulator, activates OmpR by phophorylation (AAC75828.1); Blastp hit to AAC75828.1 (918 aa), 90% identity in aa 1 - 918. | Sensory kinase in two component regulatory system with HydG; Member of the two-component regulatory system ZraS/ZraR. May function as a membrane-associated protein kinase that phosphorylates ZraR in response to high concentrations of zinc or lead in the medium (By similarity). | 0.749 |
| barA | ttrS | STM2958 | STM1386 | Sensory histidine kinase; Similar to E. coli sensor-regulator, activates OmpR by phophorylation (AAC75828.1); Blastp hit to AAC75828.1 (918 aa), 90% identity in aa 1 - 918. | Tetrathionate reductase complex: sensory transduction histidine kinase; Member of the two-component regulatory system TtrR/TtrS, which is required for synthesis of tetrathionate reductase. Probably functions as a sensor protein kinase which is autophosphorylated at a histidine residue in response to tetrathionate, and transfers its phosphate group to TtrR. During mice infection, the ability to use tetrathionate as an electron acceptor is a growth advantage for S.typhimurium over the competing microbiota in the lumen of the inflamed gut. | 0.756 |
| cheA | barA | STM1921 | STM2958 | Sensory histitine protein kinase; Involved in the transmission of sensory signals from the chemoreceptors to the flagellar motors. CheA is autophosphorylated; it can transfer its phosphate group to either CheB or CheY. | Sensory histidine kinase; Similar to E. coli sensor-regulator, activates OmpR by phophorylation (AAC75828.1); Blastp hit to AAC75828.1 (918 aa), 90% identity in aa 1 - 918. | 0.797 |
| cheA | flhA | STM1921 | STM1913 | Sensory histitine protein kinase; Involved in the transmission of sensory signals from the chemoreceptors to the flagellar motors. CheA is autophosphorylated; it can transfer its phosphate group to either CheB or CheY. | Flagellar biosynthesis protein; Required for formation of the rod structure of the flagellar apparatus. Together with FliI and FliH, may constitute the export apparatus of flagellin. | 0.944 |
| cheA | fliG | STM1921 | STM1970 | Sensory histitine protein kinase; Involved in the transmission of sensory signals from the chemoreceptors to the flagellar motors. CheA is autophosphorylated; it can transfer its phosphate group to either CheB or CheY. | Flagellar biosynthesis protein; FliG is one of three proteins (FliG, FliN, FliM) that forms the rotor-mounted switch complex (C ring), located at the base of the basal body. This complex interacts with the CheY and CheZ chemotaxis proteins, in addition to contacting components of the motor that determine the direction of flagellar rotation (By similarity). | 0.975 |
| cheA | fliM | STM1921 | STM1976 | Sensory histitine protein kinase; Involved in the transmission of sensory signals from the chemoreceptors to the flagellar motors. CheA is autophosphorylated; it can transfer its phosphate group to either CheB or CheY. | Flagellar biosynthesis protein; FliM is one of three proteins (FliG, FliN, FliM) that forms the rotor-mounted switch complex (C ring), located at the base of the basal body. This complex interacts with the CheY and CheZ chemotaxis proteins, in addition to contacting components of the motor that determine the direction of flagellar rotation (By similarity). | 0.995 |
| cheA | glnL | STM1921 | STM4006 | Sensory histitine protein kinase; Involved in the transmission of sensory signals from the chemoreceptors to the flagellar motors. CheA is autophosphorylated; it can transfer its phosphate group to either CheB or CheY. | Sensory histidine kinase/phosphatase NtrB; Member of the two-component regulatory system NtrB/NtrC, which controls expression of the nitrogen-regulated (ntr) genes in response to nitrogen limitation. Under conditions of nitrogen limitation, NtrB autophosphorylates and transfers the phosphoryl group to NtrC. In the presence of nitrogen, acts as a phosphatase that dephosphorylates and inactivates NtrC. | 0.754 |
| cheA | hydG | STM1921 | STM4174 | Sensory histitine protein kinase; Involved in the transmission of sensory signals from the chemoreceptors to the flagellar motors. CheA is autophosphorylated; it can transfer its phosphate group to either CheB or CheY. | Response regulator in two-component reguatory system with HydH; Member of the two-component regulatory system ZraS/ZraR. When activated by ZraS it acts in conjunction with sigma-54 to regulate the expression of zraP. Positively autoregulates the expression of the zraSR operon (By similarity). | 0.641 |
| cheA | ttrS | STM1921 | STM1386 | Sensory histitine protein kinase; Involved in the transmission of sensory signals from the chemoreceptors to the flagellar motors. CheA is autophosphorylated; it can transfer its phosphate group to either CheB or CheY. | Tetrathionate reductase complex: sensory transduction histidine kinase; Member of the two-component regulatory system TtrR/TtrS, which is required for synthesis of tetrathionate reductase. Probably functions as a sensor protein kinase which is autophosphorylated at a histidine residue in response to tetrathionate, and transfers its phosphate group to TtrR. During mice infection, the ability to use tetrathionate as an electron acceptor is a growth advantage for S.typhimurium over the competing microbiota in the lumen of the inflamed gut. | 0.453 |
| flhA | barA | STM1913 | STM2958 | Flagellar biosynthesis protein; Required for formation of the rod structure of the flagellar apparatus. Together with FliI and FliH, may constitute the export apparatus of flagellin. | Sensory histidine kinase; Similar to E. coli sensor-regulator, activates OmpR by phophorylation (AAC75828.1); Blastp hit to AAC75828.1 (918 aa), 90% identity in aa 1 - 918. | 0.607 |
| flhA | cheA | STM1913 | STM1921 | Flagellar biosynthesis protein; Required for formation of the rod structure of the flagellar apparatus. Together with FliI and FliH, may constitute the export apparatus of flagellin. | Sensory histitine protein kinase; Involved in the transmission of sensory signals from the chemoreceptors to the flagellar motors. CheA is autophosphorylated; it can transfer its phosphate group to either CheB or CheY. | 0.944 |
| flhA | fliG | STM1913 | STM1970 | Flagellar biosynthesis protein; Required for formation of the rod structure of the flagellar apparatus. Together with FliI and FliH, may constitute the export apparatus of flagellin. | Flagellar biosynthesis protein; FliG is one of three proteins (FliG, FliN, FliM) that forms the rotor-mounted switch complex (C ring), located at the base of the basal body. This complex interacts with the CheY and CheZ chemotaxis proteins, in addition to contacting components of the motor that determine the direction of flagellar rotation (By similarity). | 0.998 |
| flhA | fliM | STM1913 | STM1976 | Flagellar biosynthesis protein; Required for formation of the rod structure of the flagellar apparatus. Together with FliI and FliH, may constitute the export apparatus of flagellin. | Flagellar biosynthesis protein; FliM is one of three proteins (FliG, FliN, FliM) that forms the rotor-mounted switch complex (C ring), located at the base of the basal body. This complex interacts with the CheY and CheZ chemotaxis proteins, in addition to contacting components of the motor that determine the direction of flagellar rotation (By similarity). | 0.997 |
| flhA | hydG | STM1913 | STM4174 | Flagellar biosynthesis protein; Required for formation of the rod structure of the flagellar apparatus. Together with FliI and FliH, may constitute the export apparatus of flagellin. | Response regulator in two-component reguatory system with HydH; Member of the two-component regulatory system ZraS/ZraR. When activated by ZraS it acts in conjunction with sigma-54 to regulate the expression of zraP. Positively autoregulates the expression of the zraSR operon (By similarity). | 0.647 |