node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
atpA | atpB | b3734 | b3738 | F1 sector of membrane-bound ATP synthase, alpha subunit; Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit. | F0 sector of membrane-bound ATP synthase, subunit a; Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane. | 0.999 |
atpA | atpE | b3734 | b3737 | F1 sector of membrane-bound ATP synthase, alpha subunit; Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit. | F0 sector of membrane-bound 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 | b3734 | b3736 | F1 sector of membrane-bound ATP synthase, alpha subunit; Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit. | F0 sector of membrane-bound ATP synthase, subunit b; 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 | fimA | b3734 | b4314 | F1 sector of membrane-bound ATP synthase, alpha subunit; Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit. | Major type 1 subunit fimbrin (pilin); Fimbriae (also called pili), polar filaments radiating from the surface of the bacterium to a length of 0.5-1.5 micrometers and numbering 100-300 per cell, enable bacteria to colonize the epithelium of specific host organs. | 0.732 |
atpA | fimC | b3734 | b4316 | F1 sector of membrane-bound ATP synthase, alpha subunit; Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit. | Periplasmic chaperone; Required for the biogenesis of type 1 fimbriae. Binds and interact with FimH. | 0.459 |
atpA | fimH | b3734 | b4320 | F1 sector of membrane-bound ATP synthase, alpha subunit; Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit. | Minor component of type 1 fimbriae; Involved in regulation of length and mediation of adhesion of type 1 fimbriae (but not necessary for the production of fimbriae). Adhesin responsible for the binding to D-mannose. It is laterally positioned at intervals in the structure of the type 1 fimbriae. In order to integrate FimH in the fimbriae FimF and FimG are needed. | 0.891 |
atpA | sfmA | b3734 | b0530 | F1 sector of membrane-bound ATP synthase, alpha subunit; Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit. | FimA homolog, function unknown; Part of the sfmACDHF fimbrial operon. Could contribute to adhesion to various surfaces in specific environmental niches. Increases adhesion to eukaryotic T24 bladder epithelial cells in the absence of fim genes. | 0.640 |
atpA | sfmH | b3734 | b0533 | F1 sector of membrane-bound ATP synthase, alpha subunit; Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit. | FimA homolog, function unknown; Part of the sfmACDHF fimbrial operon. Could contribute to adhesion to various surfaces in specific environmental niches. Increases adhesion to eukaryotic T24 bladder epithelial cells in the absence of fim genes. | 0.891 |
atpA | yfaL | b3734 | b2233 | F1 sector of membrane-bound ATP synthase, alpha subunit; Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit. | Adhesin; Probably an autotransporter. | 0.809 |
atpB | atpA | b3738 | b3734 | F0 sector of membrane-bound ATP synthase, subunit a; Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane. | F1 sector of membrane-bound ATP synthase, alpha subunit; Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit. | 0.999 |
atpB | atpE | b3738 | b3737 | F0 sector of membrane-bound ATP synthase, subunit a; Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane. | F0 sector of membrane-bound 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 |
atpB | atpF | b3738 | b3736 | F0 sector of membrane-bound ATP synthase, subunit a; Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane. | F0 sector of membrane-bound ATP synthase, subunit b; 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 |
atpB | fimA | b3738 | b4314 | F0 sector of membrane-bound ATP synthase, subunit a; Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane. | Major type 1 subunit fimbrin (pilin); Fimbriae (also called pili), polar filaments radiating from the surface of the bacterium to a length of 0.5-1.5 micrometers and numbering 100-300 per cell, enable bacteria to colonize the epithelium of specific host organs. | 0.530 |
atpB | fimC | b3738 | b4316 | F0 sector of membrane-bound ATP synthase, subunit a; Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane. | Periplasmic chaperone; Required for the biogenesis of type 1 fimbriae. Binds and interact with FimH. | 0.892 |
atpB | fimH | b3738 | b4320 | F0 sector of membrane-bound ATP synthase, subunit a; Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane. | Minor component of type 1 fimbriae; Involved in regulation of length and mediation of adhesion of type 1 fimbriae (but not necessary for the production of fimbriae). Adhesin responsible for the binding to D-mannose. It is laterally positioned at intervals in the structure of the type 1 fimbriae. In order to integrate FimH in the fimbriae FimF and FimG are needed. | 0.730 |
atpB | sfmC | b3738 | b0531 | F0 sector of membrane-bound ATP synthase, subunit a; Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane. | Putative periplasmic pilus chaperone; Part of the sfmACDHF fimbrial operon. Could contribute to adhesion to various surfaces in specific environmental niches. Increases adhesion to eukaryotic T24 bladder epithelial cells in the absence of fim genes. | 0.790 |
atpB | sfmH | b3738 | b0533 | F0 sector of membrane-bound ATP synthase, subunit a; Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane. | FimA homolog, function unknown; Part of the sfmACDHF fimbrial operon. Could contribute to adhesion to various surfaces in specific environmental niches. Increases adhesion to eukaryotic T24 bladder epithelial cells in the absence of fim genes. | 0.700 |
atpB | yfaL | b3738 | b2233 | F0 sector of membrane-bound ATP synthase, subunit a; Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane. | Adhesin; Probably an autotransporter. | 0.881 |
atpE | atpA | b3737 | b3734 | F0 sector of membrane-bound 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. | F1 sector of membrane-bound ATP synthase, alpha subunit; Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit. | 0.999 |
atpE | atpB | b3737 | b3738 | F0 sector of membrane-bound 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. | F0 sector of membrane-bound ATP synthase, subunit a; Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane. | 0.999 |