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 | 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 | 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 | 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 | 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 |
glrK | ycjF | b2556 | b1322 | Sensor protein kinase regulating glmY sRNA in two-component system with response regulator GlrR; Member of the two-component regulatory system GlrR/GlrK that up-regulates transcription of the glmY sRNA when cells enter the stationary growth phase. Activates GlrR by phosphorylation. | UPF0283 family inner membrane protein. | 0.735 |
glrK | ycjX | b2556 | b1321 | Sensor protein kinase regulating glmY sRNA in two-component system with response regulator GlrR; Member of the two-component regulatory system GlrR/GlrK that up-regulates transcription of the glmY sRNA when cells enter the stationary growth phase. Activates GlrR by phosphorylation. | DUF463 family protein, puatative P-loop NTPase; Putative EC 2.1 enzymes; To H.influenzae HI_1637. | 0.435 |
glrK | yhcB | b2556 | b3233 | Sensor protein kinase regulating glmY sRNA in two-component system with response regulator GlrR; Member of the two-component regulatory system GlrR/GlrK that up-regulates transcription of the glmY sRNA when cells enter the stationary growth phase. Activates GlrR by phosphorylation. | DUF1043 family inner membrane-anchored protein. | 0.652 |
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 | 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 | 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 |
mepA | ycjF | b2328 | b1322 | Murein DD-endopeptidase; Murein endopeptidase that cleaves the D-alanyl-meso-2,6- diamino-pimelyl amide bond that connects peptidoglycan strands. Likely plays a role in the removal of murein from the sacculus and could also play a role in the integration of nascent murein strands into the sacculus. | UPF0283 family inner membrane protein. | 0.674 |
mepA | ycjX | b2328 | b1321 | Murein DD-endopeptidase; Murein endopeptidase that cleaves the D-alanyl-meso-2,6- diamino-pimelyl amide bond that connects peptidoglycan strands. Likely plays a role in the removal of murein from the sacculus and could also play a role in the integration of nascent murein strands into the sacculus. | DUF463 family protein, puatative P-loop NTPase; Putative EC 2.1 enzymes; To H.influenzae HI_1637. | 0.684 |
tyrR | ycjF | b1323 | b1322 | Aromatic amino acid biosynthesis and transport regulon transcriptional regulator; Involved in transcriptional regulation of aromatic amino acid biosynthesis and transport. Modulates the expression of at least 8 unlinked operons. Seven of these operons are regulated in response to changes in the concentration of the three aromatic amino acids (phenylalanine, tyrosine and tryptophan). These amino acids are suggested to act as co-effectors which bind to the TyrR protein to form an active regulatory protein. In most cases TyrR causes negative regulation, but positive effects on the tyrP ge [...] | UPF0283 family inner membrane protein. | 0.677 |
tyrR | ycjX | b1323 | b1321 | Aromatic amino acid biosynthesis and transport regulon transcriptional regulator; Involved in transcriptional regulation of aromatic amino acid biosynthesis and transport. Modulates the expression of at least 8 unlinked operons. Seven of these operons are regulated in response to changes in the concentration of the three aromatic amino acids (phenylalanine, tyrosine and tryptophan). These amino acids are suggested to act as co-effectors which bind to the TyrR protein to form an active regulatory protein. In most cases TyrR causes negative regulation, but positive effects on the tyrP ge [...] | DUF463 family protein, puatative P-loop NTPase; Putative EC 2.1 enzymes; To H.influenzae HI_1637. | 0.649 |
ybbN | clpB | b0492 | b2592 | 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 [...] | 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. | 0.845 |
ybbN | fxsA | b0492 | b4140 | 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 [...] | 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. | 0.759 |