| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| ndh | slyD | HI_0747 | HI_0699 | NADH dehydrogenase (ndh); Transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone. Does not couple the redox reaction to proton translocation (By similarity). | Peptidyl-prolyl cis-trans isomerase, FkbP-type (slyD); Folding helper with both chaperone and peptidyl-prolyl cis- trans isomerase (PPIase) activities. Chaperone activity prevents aggregation of unfolded or partially folded proteins and promotes their correct folding. PPIases catalyze the cis-trans isomerization of Xaa- Pro bonds of peptides, which accelerates slow steps of protein folding and thus shortens the lifetime of intermediates. Both strategies lower the concentration of intermediates and increase the productivity and yield of the folding reaction (By similarity); Belongs to t [...] | 0.430 |
| ppx | slyD | HI_0695 | HI_0699 | Exopolyphosphatase, putative; Degradation of inorganic polyphosphates (polyP). Releases orthophosphate processively from the ends of the polyP chain. | Peptidyl-prolyl cis-trans isomerase, FkbP-type (slyD); Folding helper with both chaperone and peptidyl-prolyl cis- trans isomerase (PPIase) activities. Chaperone activity prevents aggregation of unfolded or partially folded proteins and promotes their correct folding. PPIases catalyze the cis-trans isomerization of Xaa- Pro bonds of peptides, which accelerates slow steps of protein folding and thus shortens the lifetime of intermediates. Both strategies lower the concentration of intermediates and increase the productivity and yield of the folding reaction (By similarity); Belongs to t [...] | 0.553 |
| ppx | tamB | HI_0695 | HI_0696 | Exopolyphosphatase, putative; Degradation of inorganic polyphosphates (polyP). Releases orthophosphate processively from the ends of the polyP chain. | Conserved hypothetical protein; Part of the translocation and assembly module (TAM) autotransporter assembly complex, which functions in translocation of autotransporters across the outer membrane. Substrate binding to TamA moves its POTRA domains about 30 Angstroms into the periplasm, which would deform either the outer membrane or TamB and may provide force to reset TAM (By similarity). | 0.780 |
| ppx | tama | HI_0695 | HI_0698 | Exopolyphosphatase, putative; Degradation of inorganic polyphosphates (polyP). Releases orthophosphate processively from the ends of the polyP chain. | Conserved hypothetical protein; Part of the translocation and assembly module (TAM) autotransporter assembly complex, which functions in translocation of autotransporters across the outer membrane. Has anion selective channel-forming ability, but the physiological relevance of this activity is unclear; Belongs to the TamA family. | 0.823 |
| rpsJ | slyD | HI_0776 | HI_0699 | Ribosomal protein S10 (rpS10); Involved in the binding of tRNA to the ribosomes. Belongs to the universal ribosomal protein uS10 family. | Peptidyl-prolyl cis-trans isomerase, FkbP-type (slyD); Folding helper with both chaperone and peptidyl-prolyl cis- trans isomerase (PPIase) activities. Chaperone activity prevents aggregation of unfolded or partially folded proteins and promotes their correct folding. PPIases catalyze the cis-trans isomerization of Xaa- Pro bonds of peptides, which accelerates slow steps of protein folding and thus shortens the lifetime of intermediates. Both strategies lower the concentration of intermediates and increase the productivity and yield of the folding reaction (By similarity); Belongs to t [...] | 0.464 |
| rpsJ | tig | HI_0776 | HI_0713 | Ribosomal protein S10 (rpS10); Involved in the binding of tRNA to the ribosomes. Belongs to the universal ribosomal protein uS10 family. | Trigger factor (tig); Involved in protein export. Acts as a chaperone by maintaining the newly synthesized protein in an open conformation. Functions as a peptidyl-prolyl cis-trans isomerase (By similarity). Belongs to the FKBP-type PPIase family. Tig subfamily. | 0.959 |
| rraB | slyD | HI_0700 | HI_0699 | Conserved hypothetical protein; Globally modulates RNA abundance by binding to RNase E (Rne) and regulating its endonucleolytic activity. Can modulate Rne action in a substrate-dependent manner by altering the composition of the degradosome. | Peptidyl-prolyl cis-trans isomerase, FkbP-type (slyD); Folding helper with both chaperone and peptidyl-prolyl cis- trans isomerase (PPIase) activities. Chaperone activity prevents aggregation of unfolded or partially folded proteins and promotes their correct folding. PPIases catalyze the cis-trans isomerization of Xaa- Pro bonds of peptides, which accelerates slow steps of protein folding and thus shortens the lifetime of intermediates. Both strategies lower the concentration of intermediates and increase the productivity and yield of the folding reaction (By similarity); Belongs to t [...] | 0.558 |
| rraB | tamB | HI_0700 | HI_0696 | Conserved hypothetical protein; Globally modulates RNA abundance by binding to RNase E (Rne) and regulating its endonucleolytic activity. Can modulate Rne action in a substrate-dependent manner by altering the composition of the degradosome. | Conserved hypothetical protein; Part of the translocation and assembly module (TAM) autotransporter assembly complex, which functions in translocation of autotransporters across the outer membrane. Substrate binding to TamA moves its POTRA domains about 30 Angstroms into the periplasm, which would deform either the outer membrane or TamB and may provide force to reset TAM (By similarity). | 0.551 |
| rraB | tama | HI_0700 | HI_0698 | Conserved hypothetical protein; Globally modulates RNA abundance by binding to RNase E (Rne) and regulating its endonucleolytic activity. Can modulate Rne action in a substrate-dependent manner by altering the composition of the degradosome. | Conserved hypothetical protein; Part of the translocation and assembly module (TAM) autotransporter assembly complex, which functions in translocation of autotransporters across the outer membrane. Has anion selective channel-forming ability, but the physiological relevance of this activity is unclear; Belongs to the TamA family. | 0.446 |
| rraB | truD | HI_0700 | HI_0701 | Conserved hypothetical protein; Globally modulates RNA abundance by binding to RNase E (Rne) and regulating its endonucleolytic activity. Can modulate Rne action in a substrate-dependent manner by altering the composition of the degradosome. | Conserved hypothetical protein; Responsible for synthesis of pseudouridine from uracil-13 in transfer RNAs; Belongs to the pseudouridine synthase TruD family. | 0.542 |
| slyD | ndh | HI_0699 | HI_0747 | Peptidyl-prolyl cis-trans isomerase, FkbP-type (slyD); Folding helper with both chaperone and peptidyl-prolyl cis- trans isomerase (PPIase) activities. Chaperone activity prevents aggregation of unfolded or partially folded proteins and promotes their correct folding. PPIases catalyze the cis-trans isomerization of Xaa- Pro bonds of peptides, which accelerates slow steps of protein folding and thus shortens the lifetime of intermediates. Both strategies lower the concentration of intermediates and increase the productivity and yield of the folding reaction (By similarity); Belongs to t [...] | NADH dehydrogenase (ndh); Transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone. Does not couple the redox reaction to proton translocation (By similarity). | 0.430 |
| slyD | ppx | HI_0699 | HI_0695 | Peptidyl-prolyl cis-trans isomerase, FkbP-type (slyD); Folding helper with both chaperone and peptidyl-prolyl cis- trans isomerase (PPIase) activities. Chaperone activity prevents aggregation of unfolded or partially folded proteins and promotes their correct folding. PPIases catalyze the cis-trans isomerization of Xaa- Pro bonds of peptides, which accelerates slow steps of protein folding and thus shortens the lifetime of intermediates. Both strategies lower the concentration of intermediates and increase the productivity and yield of the folding reaction (By similarity); Belongs to t [...] | Exopolyphosphatase, putative; Degradation of inorganic polyphosphates (polyP). Releases orthophosphate processively from the ends of the polyP chain. | 0.553 |
| slyD | rpsJ | HI_0699 | HI_0776 | Peptidyl-prolyl cis-trans isomerase, FkbP-type (slyD); Folding helper with both chaperone and peptidyl-prolyl cis- trans isomerase (PPIase) activities. Chaperone activity prevents aggregation of unfolded or partially folded proteins and promotes their correct folding. PPIases catalyze the cis-trans isomerization of Xaa- Pro bonds of peptides, which accelerates slow steps of protein folding and thus shortens the lifetime of intermediates. Both strategies lower the concentration of intermediates and increase the productivity and yield of the folding reaction (By similarity); Belongs to t [...] | Ribosomal protein S10 (rpS10); Involved in the binding of tRNA to the ribosomes. Belongs to the universal ribosomal protein uS10 family. | 0.464 |
| slyD | rraB | HI_0699 | HI_0700 | Peptidyl-prolyl cis-trans isomerase, FkbP-type (slyD); Folding helper with both chaperone and peptidyl-prolyl cis- trans isomerase (PPIase) activities. Chaperone activity prevents aggregation of unfolded or partially folded proteins and promotes their correct folding. PPIases catalyze the cis-trans isomerization of Xaa- Pro bonds of peptides, which accelerates slow steps of protein folding and thus shortens the lifetime of intermediates. Both strategies lower the concentration of intermediates and increase the productivity and yield of the folding reaction (By similarity); Belongs to t [...] | Conserved hypothetical protein; Globally modulates RNA abundance by binding to RNase E (Rne) and regulating its endonucleolytic activity. Can modulate Rne action in a substrate-dependent manner by altering the composition of the degradosome. | 0.558 |
| slyD | tamB | HI_0699 | HI_0696 | Peptidyl-prolyl cis-trans isomerase, FkbP-type (slyD); Folding helper with both chaperone and peptidyl-prolyl cis- trans isomerase (PPIase) activities. Chaperone activity prevents aggregation of unfolded or partially folded proteins and promotes their correct folding. PPIases catalyze the cis-trans isomerization of Xaa- Pro bonds of peptides, which accelerates slow steps of protein folding and thus shortens the lifetime of intermediates. Both strategies lower the concentration of intermediates and increase the productivity and yield of the folding reaction (By similarity); Belongs to t [...] | Conserved hypothetical protein; Part of the translocation and assembly module (TAM) autotransporter assembly complex, which functions in translocation of autotransporters across the outer membrane. Substrate binding to TamA moves its POTRA domains about 30 Angstroms into the periplasm, which would deform either the outer membrane or TamB and may provide force to reset TAM (By similarity). | 0.540 |
| slyD | tama | HI_0699 | HI_0698 | Peptidyl-prolyl cis-trans isomerase, FkbP-type (slyD); Folding helper with both chaperone and peptidyl-prolyl cis- trans isomerase (PPIase) activities. Chaperone activity prevents aggregation of unfolded or partially folded proteins and promotes their correct folding. PPIases catalyze the cis-trans isomerization of Xaa- Pro bonds of peptides, which accelerates slow steps of protein folding and thus shortens the lifetime of intermediates. Both strategies lower the concentration of intermediates and increase the productivity and yield of the folding reaction (By similarity); Belongs to t [...] | Conserved hypothetical protein; Part of the translocation and assembly module (TAM) autotransporter assembly complex, which functions in translocation of autotransporters across the outer membrane. Has anion selective channel-forming ability, but the physiological relevance of this activity is unclear; Belongs to the TamA family. | 0.476 |
| slyD | tig | HI_0699 | HI_0713 | Peptidyl-prolyl cis-trans isomerase, FkbP-type (slyD); Folding helper with both chaperone and peptidyl-prolyl cis- trans isomerase (PPIase) activities. Chaperone activity prevents aggregation of unfolded or partially folded proteins and promotes their correct folding. PPIases catalyze the cis-trans isomerization of Xaa- Pro bonds of peptides, which accelerates slow steps of protein folding and thus shortens the lifetime of intermediates. Both strategies lower the concentration of intermediates and increase the productivity and yield of the folding reaction (By similarity); Belongs to t [...] | Trigger factor (tig); Involved in protein export. Acts as a chaperone by maintaining the newly synthesized protein in an open conformation. Functions as a peptidyl-prolyl cis-trans isomerase (By similarity). Belongs to the FKBP-type PPIase family. Tig subfamily. | 0.440 |
| slyD | truD | HI_0699 | HI_0701 | Peptidyl-prolyl cis-trans isomerase, FkbP-type (slyD); Folding helper with both chaperone and peptidyl-prolyl cis- trans isomerase (PPIase) activities. Chaperone activity prevents aggregation of unfolded or partially folded proteins and promotes their correct folding. PPIases catalyze the cis-trans isomerization of Xaa- Pro bonds of peptides, which accelerates slow steps of protein folding and thus shortens the lifetime of intermediates. Both strategies lower the concentration of intermediates and increase the productivity and yield of the folding reaction (By similarity); Belongs to t [...] | Conserved hypothetical protein; Responsible for synthesis of pseudouridine from uracil-13 in transfer RNAs; Belongs to the pseudouridine synthase TruD family. | 0.563 |
| slyD | ureE | HI_0699 | HI_0538 | Peptidyl-prolyl cis-trans isomerase, FkbP-type (slyD); Folding helper with both chaperone and peptidyl-prolyl cis- trans isomerase (PPIase) activities. Chaperone activity prevents aggregation of unfolded or partially folded proteins and promotes their correct folding. PPIases catalyze the cis-trans isomerization of Xaa- Pro bonds of peptides, which accelerates slow steps of protein folding and thus shortens the lifetime of intermediates. Both strategies lower the concentration of intermediates and increase the productivity and yield of the folding reaction (By similarity); Belongs to t [...] | Urease accessory protein (ureE); Involved in urease metallocenter assembly. Binds nickel. Probably functions as a nickel donor during metallocenter assembly. Belongs to the UreE family. | 0.511 |
| slyD | ureG | HI_0699 | HI_0536 | Peptidyl-prolyl cis-trans isomerase, FkbP-type (slyD); Folding helper with both chaperone and peptidyl-prolyl cis- trans isomerase (PPIase) activities. Chaperone activity prevents aggregation of unfolded or partially folded proteins and promotes their correct folding. PPIases catalyze the cis-trans isomerization of Xaa- Pro bonds of peptides, which accelerates slow steps of protein folding and thus shortens the lifetime of intermediates. Both strategies lower the concentration of intermediates and increase the productivity and yield of the folding reaction (By similarity); Belongs to t [...] | Urease accessory protein (ureG); Facilitates the functional incorporation of the urease nickel metallocenter. This process requires GTP hydrolysis, probably effectuated by UreG. | 0.905 |
