node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
ETY75182.1 | ETY75183.1 | LFAB_02625 | LFAB_02630 | ATPase; Derived by automated computational analysis using gene prediction method: Protein Homology. | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.619 |
ETY75182.1 | atpA | LFAB_02625 | LFAB_10685 | ATPase; Derived by automated computational analysis using gene prediction method: Protein Homology. | F0F1 ATP synthase subunit alpha; Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit. | 0.748 |
ETY75182.1 | atpB | LFAB_02625 | LFAB_10705 | ATPase; Derived by automated computational analysis using gene prediction method: Protein Homology. | F0F1 ATP synthase subunit A; Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane. Belongs to the ATPase A chain family. | 0.731 |
ETY75182.1 | atpC | LFAB_02625 | LFAB_10670 | ATPase; Derived by automated computational analysis using gene prediction method: Protein Homology. | F0F1 ATP synthase subunit epsilon; Produces ATP from ADP in the presence of a proton gradient across the membrane. | 0.729 |
ETY75182.1 | atpD | LFAB_02625 | LFAB_10675 | ATPase; Derived by automated computational analysis using gene prediction method: Protein Homology. | F0F1 ATP synthase subunit beta; Produces ATP from ADP in the presence of a proton gradient across the membrane. The catalytic sites are hosted primarily by the beta subunits. | 0.788 |
ETY75182.1 | atpE | LFAB_02625 | LFAB_10700 | ATPase; Derived by automated computational analysis using gene prediction method: Protein Homology. | F0F1 ATP synthase subunit C; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. | 0.744 |
ETY75182.1 | atpF | LFAB_02625 | LFAB_10695 | ATPase; Derived by automated computational analysis using gene prediction method: Protein Homology. | F0F1 ATP synthase subunit B; Component of the F(0) channel, it forms part of the peripheral stalk, linking F(1) to F(0); Belongs to the ATPase B chain family. | 0.727 |
ETY75182.1 | atpG | LFAB_02625 | LFAB_10680 | ATPase; Derived by automated computational analysis using gene prediction method: Protein Homology. | F0F1 ATP synthase subunit gamma; Produces ATP from ADP in the presence of a proton gradient across the membrane. The gamma chain is believed to be important in regulating ATPase activity and the flow of protons through the CF(0) complex. | 0.752 |
ETY75182.1 | atpH | LFAB_02625 | LFAB_10690 | ATPase; Derived by automated computational analysis using gene prediction method: Protein Homology. | F0F1 ATP synthase subunit delta; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. | 0.773 |
ETY75182.1 | ppaC | LFAB_02625 | LFAB_07980 | ATPase; Derived by automated computational analysis using gene prediction method: Protein Homology. | Pyrophosphatase; Catalyzes the hydrolysis of pyrophosphate to phosphate; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.740 |
ETY75183.1 | ETY75182.1 | LFAB_02630 | LFAB_02625 | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | ATPase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.619 |
atpA | ETY75182.1 | LFAB_10685 | LFAB_02625 | F0F1 ATP synthase subunit alpha; Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit. | ATPase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.748 |
atpA | atpB | LFAB_10685 | LFAB_10705 | F0F1 ATP synthase subunit alpha; Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit. | F0F1 ATP synthase subunit A; Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane. Belongs to the ATPase A chain family. | 0.999 |
atpA | atpC | LFAB_10685 | LFAB_10670 | F0F1 ATP synthase subunit alpha; Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit. | F0F1 ATP synthase subunit epsilon; Produces ATP from ADP in the presence of a proton gradient across the membrane. | 0.999 |
atpA | atpD | LFAB_10685 | LFAB_10675 | F0F1 ATP synthase subunit alpha; Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit. | F0F1 ATP synthase subunit beta; Produces ATP from ADP in the presence of a proton gradient across the membrane. The catalytic sites are hosted primarily by the beta subunits. | 0.999 |
atpA | atpE | LFAB_10685 | LFAB_10700 | F0F1 ATP synthase subunit alpha; Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit. | F0F1 ATP synthase subunit C; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. | 0.999 |
atpA | atpF | LFAB_10685 | LFAB_10695 | F0F1 ATP synthase subunit alpha; Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit. | F0F1 ATP synthase subunit B; Component of the F(0) channel, it forms part of the peripheral stalk, linking F(1) to F(0); Belongs to the ATPase B chain family. | 0.999 |
atpA | atpG | LFAB_10685 | LFAB_10680 | F0F1 ATP synthase subunit alpha; Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit. | F0F1 ATP synthase subunit gamma; Produces ATP from ADP in the presence of a proton gradient across the membrane. The gamma chain is believed to be important in regulating ATPase activity and the flow of protons through the CF(0) complex. | 0.999 |
atpA | atpH | LFAB_10685 | LFAB_10690 | F0F1 ATP synthase subunit alpha; Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit. | F0F1 ATP synthase subunit delta; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. | 0.999 |
atpA | ppaC | LFAB_10685 | LFAB_07980 | F0F1 ATP synthase subunit alpha; Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit. | Pyrophosphatase; Catalyzes the hydrolysis of pyrophosphate to phosphate; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.922 |