| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| azo2479 | fliF | azo2479 | azo2716 | Conserved hypothetical membrane protein. Homology to VV12384 of Vibrio vulnificus of 60% (trembl|Q8DA26). No domains predicted. TMHMM2 reporting 1 TMH present. No signal peptide present; Conserved hypothetical protein. | Flagellar M-ring protein; The M ring may be actively involved in energy transduction. Belongs to the FliF family. | 0.715 |
| azo2479 | fliG | azo2479 | azo2717 | Conserved hypothetical membrane protein. Homology to VV12384 of Vibrio vulnificus of 60% (trembl|Q8DA26). No domains predicted. TMHMM2 reporting 1 TMH present. No signal peptide present; Conserved hypothetical protein. | Flagellar motor switch protein fliG. FLIG IS ONE OF THREE PROTEINS (FLIG FLIN FLIM) THAT FORM A SWITCH COMPLEX THAT IS PROPOSED TO BE 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). fliG: flagellar motor switch protein Pfam: fliG C-terminal domain no signal peptide no TMHs; High confidence in function and specificity. | 0.979 |
| azo2479 | fliH | azo2479 | azo2718 | Conserved hypothetical membrane protein. Homology to VV12384 of Vibrio vulnificus of 60% (trembl|Q8DA26). No domains predicted. TMHMM2 reporting 1 TMH present. No signal peptide present; Conserved hypothetical protein. | Probable Flagellar assembly protein FliH, 38% identity to TrEMBL;Q7VYE7, Q7WJB3, Q8XSS5. Has PF02108,Flagellar assembly protein FliH;IPR000563, Flag_FliH; Many flagellar proteins are exported by a flagellum-specific export pathway. Attempts have been made to characterise the apparatus responsible for this process, by designing assays to screen for mutants with export defects. Experiments involving filament removal from temperature-sensitive flagellar mutants of Salmonella typhimurium have shown that, while most mutants were able to regrow filaments, flhA, fliH, fliI and fliN mutants sh [...] | 0.596 |
| azo2479 | fliK | azo2479 | azo2721 | Conserved hypothetical membrane protein. Homology to VV12384 of Vibrio vulnificus of 60% (trembl|Q8DA26). No domains predicted. TMHMM2 reporting 1 TMH present. No signal peptide present; Conserved hypothetical protein. | Flagellar hook-length control protein. Controls the length of the flagellar hook. no TMHs no signal peptide; Family membership. | 0.607 |
| azo2479 | fliL | azo2479 | azo2722 | Conserved hypothetical membrane protein. Homology to VV12384 of Vibrio vulnificus of 60% (trembl|Q8DA26). No domains predicted. TMHMM2 reporting 1 TMH present. No signal peptide present; Conserved hypothetical protein. | Putative flagellar basal body-associated protein FliL; Controls the rotational direction of flagella during chemotaxis; Belongs to the FliL family. | 0.537 |
| azo2479 | fliM | azo2479 | azo2723 | Conserved hypothetical membrane protein. Homology to VV12384 of Vibrio vulnificus of 60% (trembl|Q8DA26). No domains predicted. TMHMM2 reporting 1 TMH present. No signal peptide present; Conserved hypothetical protein. | Flagellar motor switch protein fliM. FLIM IS ONE OF THREE PROTEINS (FLIG FLIN FLIM) THAT FORM A SWITCH COMPLEX THAT IS PROPOSED TO BE 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. InterPro: Flagellar motor switch protein FliM Pfam:Flagellar motor switch protein FliM no TMHs signale peptide: no analysis; High confidence in function and specificity. | 0.991 |
| azo2479 | fliN | azo2479 | azo2724 | Conserved hypothetical membrane protein. Homology to VV12384 of Vibrio vulnificus of 60% (trembl|Q8DA26). No domains predicted. TMHMM2 reporting 1 TMH present. No signal peptide present; Conserved hypothetical protein. | Flagellar motor switch protein fliN (Flagellar motor switch protein mopA) (Fragment). FliN is one of three proteins (FliG FliN FliM) that form a switch complex that is proposed to be 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 dirction of flagellar rotation (by similarity). InterPro: Surface presentation of antigens (SPOA) protein, Flagellar motor switch FliN protein Pfam: Surface presentation of antigens (SPOA) protein no signal peptide no TMHs; High confid [...] | 0.984 |
| azo2479 | fliP | azo2479 | azo2726 | Conserved hypothetical membrane protein. Homology to VV12384 of Vibrio vulnificus of 60% (trembl|Q8DA26). No domains predicted. TMHMM2 reporting 1 TMH present. No signal peptide present; Conserved hypothetical protein. | Flagellar biosynthetic protein FliP; Plays a role in the flagellum-specific transport system. Belongs to the FliP/MopC/SpaP family. | 0.623 |
| azo2479 | fliQ | azo2479 | azo2727 | Conserved hypothetical membrane protein. Homology to VV12384 of Vibrio vulnificus of 60% (trembl|Q8DA26). No domains predicted. TMHMM2 reporting 1 TMH present. No signal peptide present; Conserved hypothetical protein. | Flagellar biosynthesis protein FliQ; Role in flagellar biosynthesis. Belongs to the FliQ/MopD/SpaQ family. | 0.625 |
| flgJ | fliF | azo2732 | azo2716 | Peptidoglycan hydrolase flgJ (EC 3.2.1.-) (Muramidase flgJ). Flagellum-specific muramidase which hydrolyses the peptidoglycan layer to assemble the rod structure in the periplasmic space (by similarity). InterPro: Mannosyl-glycoprotein endo-beta-N-acetylglucosamidases Pfam: Mannosyl-glycoprotein endo-beta-N-acetylglucosamidases no signal peptide no TMHs; High confidence in function and specificity. | Flagellar M-ring protein; The M ring may be actively involved in energy transduction. Belongs to the FliF family. | 0.981 |
| flgJ | fliG | azo2732 | azo2717 | Peptidoglycan hydrolase flgJ (EC 3.2.1.-) (Muramidase flgJ). Flagellum-specific muramidase which hydrolyses the peptidoglycan layer to assemble the rod structure in the periplasmic space (by similarity). InterPro: Mannosyl-glycoprotein endo-beta-N-acetylglucosamidases Pfam: Mannosyl-glycoprotein endo-beta-N-acetylglucosamidases no signal peptide no TMHs; High confidence in function and specificity. | Flagellar motor switch protein fliG. FLIG IS ONE OF THREE PROTEINS (FLIG FLIN FLIM) THAT FORM A SWITCH COMPLEX THAT IS PROPOSED TO BE 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). fliG: flagellar motor switch protein Pfam: fliG C-terminal domain no signal peptide no TMHs; High confidence in function and specificity. | 0.977 |
| flgJ | fliH | azo2732 | azo2718 | Peptidoglycan hydrolase flgJ (EC 3.2.1.-) (Muramidase flgJ). Flagellum-specific muramidase which hydrolyses the peptidoglycan layer to assemble the rod structure in the periplasmic space (by similarity). InterPro: Mannosyl-glycoprotein endo-beta-N-acetylglucosamidases Pfam: Mannosyl-glycoprotein endo-beta-N-acetylglucosamidases no signal peptide no TMHs; High confidence in function and specificity. | Probable Flagellar assembly protein FliH, 38% identity to TrEMBL;Q7VYE7, Q7WJB3, Q8XSS5. Has PF02108,Flagellar assembly protein FliH;IPR000563, Flag_FliH; Many flagellar proteins are exported by a flagellum-specific export pathway. Attempts have been made to characterise the apparatus responsible for this process, by designing assays to screen for mutants with export defects. Experiments involving filament removal from temperature-sensitive flagellar mutants of Salmonella typhimurium have shown that, while most mutants were able to regrow filaments, flhA, fliH, fliI and fliN mutants sh [...] | 0.987 |
| flgJ | fliK | azo2732 | azo2721 | Peptidoglycan hydrolase flgJ (EC 3.2.1.-) (Muramidase flgJ). Flagellum-specific muramidase which hydrolyses the peptidoglycan layer to assemble the rod structure in the periplasmic space (by similarity). InterPro: Mannosyl-glycoprotein endo-beta-N-acetylglucosamidases Pfam: Mannosyl-glycoprotein endo-beta-N-acetylglucosamidases no signal peptide no TMHs; High confidence in function and specificity. | Flagellar hook-length control protein. Controls the length of the flagellar hook. no TMHs no signal peptide; Family membership. | 0.990 |
| flgJ | fliL | azo2732 | azo2722 | Peptidoglycan hydrolase flgJ (EC 3.2.1.-) (Muramidase flgJ). Flagellum-specific muramidase which hydrolyses the peptidoglycan layer to assemble the rod structure in the periplasmic space (by similarity). InterPro: Mannosyl-glycoprotein endo-beta-N-acetylglucosamidases Pfam: Mannosyl-glycoprotein endo-beta-N-acetylglucosamidases no signal peptide no TMHs; High confidence in function and specificity. | Putative flagellar basal body-associated protein FliL; Controls the rotational direction of flagella during chemotaxis; Belongs to the FliL family. | 0.978 |
| flgJ | fliM | azo2732 | azo2723 | Peptidoglycan hydrolase flgJ (EC 3.2.1.-) (Muramidase flgJ). Flagellum-specific muramidase which hydrolyses the peptidoglycan layer to assemble the rod structure in the periplasmic space (by similarity). InterPro: Mannosyl-glycoprotein endo-beta-N-acetylglucosamidases Pfam: Mannosyl-glycoprotein endo-beta-N-acetylglucosamidases no signal peptide no TMHs; High confidence in function and specificity. | Flagellar motor switch protein fliM. FLIM IS ONE OF THREE PROTEINS (FLIG FLIN FLIM) THAT FORM A SWITCH COMPLEX THAT IS PROPOSED TO BE 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. InterPro: Flagellar motor switch protein FliM Pfam:Flagellar motor switch protein FliM no TMHs signale peptide: no analysis; High confidence in function and specificity. | 0.986 |
| flgJ | fliN | azo2732 | azo2724 | Peptidoglycan hydrolase flgJ (EC 3.2.1.-) (Muramidase flgJ). Flagellum-specific muramidase which hydrolyses the peptidoglycan layer to assemble the rod structure in the periplasmic space (by similarity). InterPro: Mannosyl-glycoprotein endo-beta-N-acetylglucosamidases Pfam: Mannosyl-glycoprotein endo-beta-N-acetylglucosamidases no signal peptide no TMHs; High confidence in function and specificity. | Flagellar motor switch protein fliN (Flagellar motor switch protein mopA) (Fragment). FliN is one of three proteins (FliG FliN FliM) that form a switch complex that is proposed to be 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 dirction of flagellar rotation (by similarity). InterPro: Surface presentation of antigens (SPOA) protein, Flagellar motor switch FliN protein Pfam: Surface presentation of antigens (SPOA) protein no signal peptide no TMHs; High confid [...] | 0.963 |
| flgJ | fliP | azo2732 | azo2726 | Peptidoglycan hydrolase flgJ (EC 3.2.1.-) (Muramidase flgJ). Flagellum-specific muramidase which hydrolyses the peptidoglycan layer to assemble the rod structure in the periplasmic space (by similarity). InterPro: Mannosyl-glycoprotein endo-beta-N-acetylglucosamidases Pfam: Mannosyl-glycoprotein endo-beta-N-acetylglucosamidases no signal peptide no TMHs; High confidence in function and specificity. | Flagellar biosynthetic protein FliP; Plays a role in the flagellum-specific transport system. Belongs to the FliP/MopC/SpaP family. | 0.956 |
| flgJ | fliQ | azo2732 | azo2727 | Peptidoglycan hydrolase flgJ (EC 3.2.1.-) (Muramidase flgJ). Flagellum-specific muramidase which hydrolyses the peptidoglycan layer to assemble the rod structure in the periplasmic space (by similarity). InterPro: Mannosyl-glycoprotein endo-beta-N-acetylglucosamidases Pfam: Mannosyl-glycoprotein endo-beta-N-acetylglucosamidases no signal peptide no TMHs; High confidence in function and specificity. | Flagellar biosynthesis protein FliQ; Role in flagellar biosynthesis. Belongs to the FliQ/MopD/SpaQ family. | 0.952 |
| fliF | azo2479 | azo2716 | azo2479 | Flagellar M-ring protein; The M ring may be actively involved in energy transduction. Belongs to the FliF family. | Conserved hypothetical membrane protein. Homology to VV12384 of Vibrio vulnificus of 60% (trembl|Q8DA26). No domains predicted. TMHMM2 reporting 1 TMH present. No signal peptide present; Conserved hypothetical protein. | 0.715 |
| fliF | flgJ | azo2716 | azo2732 | Flagellar M-ring protein; The M ring may be actively involved in energy transduction. Belongs to the FliF family. | Peptidoglycan hydrolase flgJ (EC 3.2.1.-) (Muramidase flgJ). Flagellum-specific muramidase which hydrolyses the peptidoglycan layer to assemble the rod structure in the periplasmic space (by similarity). InterPro: Mannosyl-glycoprotein endo-beta-N-acetylglucosamidases Pfam: Mannosyl-glycoprotein endo-beta-N-acetylglucosamidases no signal peptide no TMHs; High confidence in function and specificity. | 0.981 |