node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
clpB | htpG | b2592 | b0473 | Protein disaggregation chaperone; Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE. Acts before DnaK, in the processing of protein aggregates. Protein binding stimulates the ATPase activity; ATP hydrolysis unfolds the denatured protein aggregates, which probably helps expose new hydrophobic binding sites on the surface of ClpB-bound aggregates, contributing to the solubilization and refolding of denatured protein aggregates by DnaK. | Protein refolding molecular co-chaperone Hsp90, Hsp70-dependent; Molecular chaperone. Has ATPase activity. | 0.994 |
clpB | ibpB | b2592 | b3686 | Protein disaggregation chaperone; Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE. Acts before DnaK, in the processing of protein aggregates. Protein binding stimulates the ATPase activity; ATP hydrolysis unfolds the denatured protein aggregates, which probably helps expose new hydrophobic binding sites on the surface of ClpB-bound aggregates, contributing to the solubilization and refolding of denatured protein aggregates by DnaK. | Heat shock chaperone; Associates with aggregated proteins, together with IbpA, to stabilize and protect them from irreversible denaturation and extensive proteolysis during heat shock and oxidative stress. Aggregated proteins bound to the IbpAB complex are more efficiently refolded and reactivated by the ATP-dependent chaperone systems ClpB and DnaK/DnaJ/GrpE. Its activity is ATP-independent. | 0.987 |
clpB | ybbN | b2592 | b0492 | Protein disaggregation chaperone; Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE. Acts before DnaK, in the processing of protein aggregates. Protein binding stimulates the ATPase activity; ATP hydrolysis unfolds the denatured protein aggregates, which probably helps expose new hydrophobic binding sites on the surface of ClpB-bound aggregates, contributing to the solubilization and refolding of denatured protein aggregates by DnaK. | DnaK co-chaperone, thioredoxin-like protein; Chaperedoxin that combines a chaperone activity with a redox- protective function. Involved in the protection against hypochlorous acid (HOCl), the active ingredient of bleach, which kills bacteria by causing protein aggregation. Functions as an efficient holdase chaperone that protects the substrates of the major folding systems GroEL/GroES and DnaK/DnaJ/GrpE from aggregation. In addition, it prevents the irreversible oxidation of its substrates through the formation of mixed disulfide complexes. After bleach stress, it transfers its substr [...] | 0.845 |
clpB | ybeD | b2592 | b0631 | Protein disaggregation chaperone; Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE. Acts before DnaK, in the processing of protein aggregates. Protein binding stimulates the ATPase activity; ATP hydrolysis unfolds the denatured protein aggregates, which probably helps expose new hydrophobic binding sites on the surface of ClpB-bound aggregates, contributing to the solubilization and refolding of denatured protein aggregates by DnaK. | UPF0250 family protein. | 0.477 |
clpB | ycjF | b2592 | b1322 | Protein disaggregation chaperone; Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE. Acts before DnaK, in the processing of protein aggregates. Protein binding stimulates the ATPase activity; ATP hydrolysis unfolds the denatured protein aggregates, which probably helps expose new hydrophobic binding sites on the surface of ClpB-bound aggregates, contributing to the solubilization and refolding of denatured protein aggregates by DnaK. | UPF0283 family inner membrane protein. | 0.727 |
clpB | ycjX | b2592 | b1321 | Protein disaggregation chaperone; Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE. Acts before DnaK, in the processing of protein aggregates. Protein binding stimulates the ATPase activity; ATP hydrolysis unfolds the denatured protein aggregates, which probably helps expose new hydrophobic binding sites on the surface of ClpB-bound aggregates, contributing to the solubilization and refolding of denatured protein aggregates by DnaK. | DUF463 family protein, puatative P-loop NTPase; Putative EC 2.1 enzymes; To H.influenzae HI_1637. | 0.607 |
fxsA | ibpB | b4140 | b3686 | Suppressor of F exclusion of phage T7; Overexpression alleviates the exclusion of phage T7 in cells harboring the F plasmid; Belongs to the UPF0716 (FxsA) family. | Heat shock chaperone; Associates with aggregated proteins, together with IbpA, to stabilize and protect them from irreversible denaturation and extensive proteolysis during heat shock and oxidative stress. Aggregated proteins bound to the IbpAB complex are more efficiently refolded and reactivated by the ATP-dependent chaperone systems ClpB and DnaK/DnaJ/GrpE. Its activity is ATP-independent. | 0.645 |
fxsA | ybbN | b4140 | b0492 | Suppressor of F exclusion of phage T7; Overexpression alleviates the exclusion of phage T7 in cells harboring the F plasmid; Belongs to the UPF0716 (FxsA) family. | DnaK co-chaperone, thioredoxin-like protein; Chaperedoxin that combines a chaperone activity with a redox- protective function. Involved in the protection against hypochlorous acid (HOCl), the active ingredient of bleach, which kills bacteria by causing protein aggregation. Functions as an efficient holdase chaperone that protects the substrates of the major folding systems GroEL/GroES and DnaK/DnaJ/GrpE from aggregation. In addition, it prevents the irreversible oxidation of its substrates through the formation of mixed disulfide complexes. After bleach stress, it transfers its substr [...] | 0.759 |
fxsA | ybeD | b4140 | b0631 | Suppressor of F exclusion of phage T7; Overexpression alleviates the exclusion of phage T7 in cells harboring the F plasmid; Belongs to the UPF0716 (FxsA) family. | UPF0250 family protein. | 0.745 |
fxsA | ycjF | b4140 | b1322 | Suppressor of F exclusion of phage T7; Overexpression alleviates the exclusion of phage T7 in cells harboring the F plasmid; Belongs to the UPF0716 (FxsA) family. | UPF0283 family inner membrane protein. | 0.704 |
fxsA | ycjX | b4140 | b1321 | Suppressor of F exclusion of phage T7; Overexpression alleviates the exclusion of phage T7 in cells harboring the F plasmid; Belongs to the UPF0716 (FxsA) family. | DUF463 family protein, puatative P-loop NTPase; Putative EC 2.1 enzymes; To H.influenzae HI_1637. | 0.583 |
htpG | clpB | b0473 | b2592 | Protein refolding molecular co-chaperone Hsp90, Hsp70-dependent; Molecular chaperone. Has ATPase activity. | Protein disaggregation chaperone; Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE. Acts before DnaK, in the processing of protein aggregates. Protein binding stimulates the ATPase activity; ATP hydrolysis unfolds the denatured protein aggregates, which probably helps expose new hydrophobic binding sites on the surface of ClpB-bound aggregates, contributing to the solubilization and refolding of denatured protein aggregates by DnaK. | 0.994 |
htpG | ibpB | b0473 | b3686 | Protein refolding molecular co-chaperone Hsp90, Hsp70-dependent; Molecular chaperone. Has ATPase activity. | Heat shock chaperone; Associates with aggregated proteins, together with IbpA, to stabilize and protect them from irreversible denaturation and extensive proteolysis during heat shock and oxidative stress. Aggregated proteins bound to the IbpAB complex are more efficiently refolded and reactivated by the ATP-dependent chaperone systems ClpB and DnaK/DnaJ/GrpE. Its activity is ATP-independent. | 0.943 |
htpG | ybbN | b0473 | b0492 | Protein refolding molecular co-chaperone Hsp90, Hsp70-dependent; Molecular chaperone. Has ATPase activity. | DnaK co-chaperone, thioredoxin-like protein; Chaperedoxin that combines a chaperone activity with a redox- protective function. Involved in the protection against hypochlorous acid (HOCl), the active ingredient of bleach, which kills bacteria by causing protein aggregation. Functions as an efficient holdase chaperone that protects the substrates of the major folding systems GroEL/GroES and DnaK/DnaJ/GrpE from aggregation. In addition, it prevents the irreversible oxidation of its substrates through the formation of mixed disulfide complexes. After bleach stress, it transfers its substr [...] | 0.873 |
htpG | ybeD | b0473 | b0631 | Protein refolding molecular co-chaperone Hsp90, Hsp70-dependent; Molecular chaperone. Has ATPase activity. | UPF0250 family protein. | 0.506 |
htpG | ycjF | b0473 | b1322 | Protein refolding molecular co-chaperone Hsp90, Hsp70-dependent; Molecular chaperone. Has ATPase activity. | UPF0283 family inner membrane protein. | 0.654 |
htpG | ycjX | b0473 | b1321 | Protein refolding molecular co-chaperone Hsp90, Hsp70-dependent; Molecular chaperone. Has ATPase activity. | DUF463 family protein, puatative P-loop NTPase; Putative EC 2.1 enzymes; To H.influenzae HI_1637. | 0.538 |
ibpB | clpB | b3686 | b2592 | Heat shock chaperone; Associates with aggregated proteins, together with IbpA, to stabilize and protect them from irreversible denaturation and extensive proteolysis during heat shock and oxidative stress. Aggregated proteins bound to the IbpAB complex are more efficiently refolded and reactivated by the ATP-dependent chaperone systems ClpB and DnaK/DnaJ/GrpE. Its activity is ATP-independent. | Protein disaggregation chaperone; Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE. Acts before DnaK, in the processing of protein aggregates. Protein binding stimulates the ATPase activity; ATP hydrolysis unfolds the denatured protein aggregates, which probably helps expose new hydrophobic binding sites on the surface of ClpB-bound aggregates, contributing to the solubilization and refolding of denatured protein aggregates by DnaK. | 0.987 |
ibpB | fxsA | b3686 | b4140 | Heat shock chaperone; Associates with aggregated proteins, together with IbpA, to stabilize and protect them from irreversible denaturation and extensive proteolysis during heat shock and oxidative stress. Aggregated proteins bound to the IbpAB complex are more efficiently refolded and reactivated by the ATP-dependent chaperone systems ClpB and DnaK/DnaJ/GrpE. Its activity is ATP-independent. | Suppressor of F exclusion of phage T7; Overexpression alleviates the exclusion of phage T7 in cells harboring the F plasmid; Belongs to the UPF0716 (FxsA) family. | 0.645 |
ibpB | htpG | b3686 | b0473 | Heat shock chaperone; Associates with aggregated proteins, together with IbpA, to stabilize and protect them from irreversible denaturation and extensive proteolysis during heat shock and oxidative stress. Aggregated proteins bound to the IbpAB complex are more efficiently refolded and reactivated by the ATP-dependent chaperone systems ClpB and DnaK/DnaJ/GrpE. Its activity is ATP-independent. | Protein refolding molecular co-chaperone Hsp90, Hsp70-dependent; Molecular chaperone. Has ATPase activity. | 0.943 |