node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
AHA_0547 | AHA_4146 | AHA_0547 | AHA_4146 | Molecular chaperones; Identified by match to protein family HMM PF00226. | Hypothetical chaperone protein YegD. | 0.893 |
AHA_0547 | clpP | AHA_0547 | AHA_2011 | Molecular chaperones; Identified by match to protein family HMM PF00226. | ATP-dependent Clp protease, proteolytic subunit ClpP; Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins. Belongs to the peptidase S14 family. | 0.550 |
AHA_0547 | dnaK | AHA_0547 | AHA_2983 | Molecular chaperones; Identified by match to protein family HMM PF00226. | Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.948 |
AHA_0547 | groL | AHA_0547 | AHA_0860 | Molecular chaperones; Identified by match to protein family HMM PF00226. | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.843 |
AHA_0547 | groS | AHA_0547 | AHA_0859 | Molecular chaperones; Identified by match to protein family HMM PF00226. | Chaperonin GroS; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.821 |
AHA_0547 | grpE | AHA_0547 | AHA_2984 | Molecular chaperones; Identified by match to protein family HMM PF00226. | Co-chaperone GrpE; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-depend [...] | 0.889 |
AHA_0547 | hscA | AHA_0547 | AHA_1751 | Molecular chaperones; Identified by match to protein family HMM PF00226. | Fe-S protein assembly chaperone HscA; Chaperone involved in the maturation of iron-sulfur cluster- containing proteins. Has a low intrinsic ATPase activity which is markedly stimulated by HscB. | 0.893 |
AHA_0547 | hslU | AHA_0547 | AHA_4115 | Molecular chaperones; Identified by match to protein family HMM PF00226. | Heat shock protein HslVU, ATPase subunit HslU; ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. The binding of ATP and its subsequent hydrolysis by HslU are essential for unfolding of protein substrates subsequently hydrolyzed by HslV. HslU recognizes the N-terminal part of its protein substrates and unfolds these before they are guided to HslV for hydrolysis. | 0.649 |
AHA_0547 | htpG | AHA_0547 | AHA_2490 | Molecular chaperones; Identified by match to protein family HMM PF00226. | Chaperone protein HtpG; Molecular chaperone. Has ATPase activity. | 0.928 |
AHA_4146 | AHA_0547 | AHA_4146 | AHA_0547 | Hypothetical chaperone protein YegD. | Molecular chaperones; Identified by match to protein family HMM PF00226. | 0.893 |
AHA_4146 | clpP | AHA_4146 | AHA_2011 | Hypothetical chaperone protein YegD. | ATP-dependent Clp protease, proteolytic subunit ClpP; Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins. Belongs to the peptidase S14 family. | 0.633 |
AHA_4146 | dnaJ | AHA_4146 | AHA_2982 | Hypothetical chaperone protein YegD. | Chaperone protein DnaJ; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, D [...] | 0.923 |
AHA_4146 | groL | AHA_4146 | AHA_0860 | Hypothetical chaperone protein YegD. | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.882 |
AHA_4146 | groS | AHA_4146 | AHA_0859 | Hypothetical chaperone protein YegD. | Chaperonin GroS; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.812 |
AHA_4146 | grpE | AHA_4146 | AHA_2984 | Hypothetical chaperone protein YegD. | Co-chaperone GrpE; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-depend [...] | 0.937 |
AHA_4146 | hslU | AHA_4146 | AHA_4115 | Hypothetical chaperone protein YegD. | Heat shock protein HslVU, ATPase subunit HslU; ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. The binding of ATP and its subsequent hydrolysis by HslU are essential for unfolding of protein substrates subsequently hydrolyzed by HslV. HslU recognizes the N-terminal part of its protein substrates and unfolds these before they are guided to HslV for hydrolysis. | 0.549 |
AHA_4146 | htpG | AHA_4146 | AHA_2490 | Hypothetical chaperone protein YegD. | Chaperone protein HtpG; Molecular chaperone. Has ATPase activity. | 0.951 |
clpP | AHA_0547 | AHA_2011 | AHA_0547 | ATP-dependent Clp protease, proteolytic subunit ClpP; Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins. Belongs to the peptidase S14 family. | Molecular chaperones; Identified by match to protein family HMM PF00226. | 0.550 |
clpP | AHA_4146 | AHA_2011 | AHA_4146 | ATP-dependent Clp protease, proteolytic subunit ClpP; Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins. Belongs to the peptidase S14 family. | Hypothetical chaperone protein YegD. | 0.633 |
clpP | dnaJ | AHA_2011 | AHA_2982 | ATP-dependent Clp protease, proteolytic subunit ClpP; Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins. Belongs to the peptidase S14 family. | Chaperone protein DnaJ; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, D [...] | 0.574 |