| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| RPA3930 | RPA3932 | RPA3930 | RPA3932 | Unknown protein; Observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished. | Probable flagellar hook protein flgE; Observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished. | 0.969 |
| RPA3930 | flgC | RPA3930 | RPA3887 | Unknown protein; Observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished. | Flagellar basal-body rod protein flgC; Belongs to the flagella basal body rod proteins family. | 0.621 |
| RPA3930 | flgG | RPA3930 | RPA3900 | Unknown protein; Observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished. | Putative flagellar basal-body rod protein flgg (distal rod protein); Observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished; Belongs to the flagella basal body rod proteins family. | 0.604 |
| RPA3930 | flgH | RPA3930 | RPA3902 | Unknown protein; Observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished. | Putative flagellar L-ring protein FlgH; Assembles around the rod to form the L-ring and probably protects the motor/basal body from shearing forces during rotation. | 0.758 |
| RPA3930 | flgK2 | RPA3930 | RPA3931 | Unknown protein; Observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished. | Possible flagellar hook-associated protein 1 FlgK; Observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished. | 0.991 |
| RPA3930 | fliD | RPA3930 | RPA0641 | Unknown protein; Observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished. | Possible flagellar hook-associated protein 2 (FliD, filament cap protein); Required for morphogenesis and for the elongation of the flagellar filament by facilitating polymerization of the flagellin monomers at the tip of growing filament. Forms a capping structure, which prevents flagellin subunits (transported through the central channel of the flagellum) from leaking out without polymerization at the distal end. | 0.879 |
| RPA3930 | fliF | RPA3930 | RPA1264 | Unknown protein; Observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished. | Putative flagellar M-ring protein; The M ring may be actively involved in energy transduction. Belongs to the FliF family. | 0.749 |
| RPA3930 | fliG | RPA3930 | RPA1265 | Unknown protein; Observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished. | Putative flagellar motor switch 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. | 0.700 |
| RPA3930 | fliM | RPA3930 | RPA3897 | Unknown protein; Observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished. | Possible flagellar motor switch protein FliM; 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. | 0.882 |
| RPA3930 | fliY | RPA3930 | RPA1267 | Unknown protein; Observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished. | Putative flagellar motor switch protein; FliN is one of three proteins (FliG, FliN, FliM) that form 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. Belongs to the FliN/MopA/SpaO family. | 0.553 |
| RPA3932 | RPA3930 | RPA3932 | RPA3930 | Probable flagellar hook protein flgE; Observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished. | Unknown protein; Observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished. | 0.969 |
| RPA3932 | flgC | RPA3932 | RPA3887 | Probable flagellar hook protein flgE; Observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished. | Flagellar basal-body rod protein flgC; Belongs to the flagella basal body rod proteins family. | 0.990 |
| RPA3932 | flgG | RPA3932 | RPA3900 | Probable flagellar hook protein flgE; Observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished. | Putative flagellar basal-body rod protein flgg (distal rod protein); Observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished; Belongs to the flagella basal body rod proteins family. | 0.968 |
| RPA3932 | flgH | RPA3932 | RPA3902 | Probable flagellar hook protein flgE; Observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished. | Putative flagellar L-ring protein FlgH; Assembles around the rod to form the L-ring and probably protects the motor/basal body from shearing forces during rotation. | 0.989 |
| RPA3932 | flgK2 | RPA3932 | RPA3931 | Probable flagellar hook protein flgE; Observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished. | Possible flagellar hook-associated protein 1 FlgK; Observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished. | 0.985 |
| RPA3932 | fliD | RPA3932 | RPA0641 | Probable flagellar hook protein flgE; Observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished. | Possible flagellar hook-associated protein 2 (FliD, filament cap protein); Required for morphogenesis and for the elongation of the flagellar filament by facilitating polymerization of the flagellin monomers at the tip of growing filament. Forms a capping structure, which prevents flagellin subunits (transported through the central channel of the flagellum) from leaking out without polymerization at the distal end. | 0.892 |
| RPA3932 | fliF | RPA3932 | RPA1264 | Probable flagellar hook protein flgE; Observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished. | Putative flagellar M-ring protein; The M ring may be actively involved in energy transduction. Belongs to the FliF family. | 0.990 |
| RPA3932 | fliG | RPA3932 | RPA1265 | Probable flagellar hook protein flgE; Observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished. | Putative flagellar motor switch 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. | 0.978 |
| RPA3932 | fliM | RPA3932 | RPA3897 | Probable flagellar hook protein flgE; Observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished. | Possible flagellar motor switch protein FliM; 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. | 0.969 |
| RPA3932 | fliY | RPA3932 | RPA1267 | Probable flagellar hook protein flgE; Observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished. | Putative flagellar motor switch protein; FliN is one of three proteins (FliG, FliN, FliM) that form 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. Belongs to the FliN/MopA/SpaO family. | 0.975 |