| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| AFE_0871 | dnaK | AFE_0871 | AFE_2665 | Heat shock protein, Hsp20 family; Identified by similarity to GB:CAE31747.1; match to protein family HMM PF00011; Belongs to the small heat shock protein (HSP20) family. | Chaperone protein Dnak; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.424 |
| AFE_0871 | grpE | AFE_0871 | AFE_2666 | Heat shock protein, Hsp20 family; Identified by similarity to GB:CAE31747.1; match to protein family HMM PF00011; Belongs to the small heat shock protein (HSP20) family. | 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 [...] | 0.417 |
| AFE_0871 | hscA | AFE_0871 | AFE_0677 | Heat shock protein, Hsp20 family; Identified by similarity to GB:CAE31747.1; match to protein family HMM PF00011; Belongs to the small heat shock protein (HSP20) family. | 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. | 0.424 |
| AFE_0871 | hslV | AFE_0871 | AFE_2747 | Heat shock protein, Hsp20 family; Identified by similarity to GB:CAE31747.1; match to protein family HMM PF00011; Belongs to the small heat shock protein (HSP20) family. | Heat shock protein HslV; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.400 |
| AFE_0871 | htpG | AFE_0871 | AFE_3158 | Heat shock protein, Hsp20 family; Identified by similarity to GB:CAE31747.1; match to protein family HMM PF00011; Belongs to the small heat shock protein (HSP20) family. | Heat shock protein HtpG; Molecular chaperone. Has ATPase activity. | 0.437 |
| AFE_0871 | lon-2 | AFE_0871 | AFE_0872 | Heat shock protein, Hsp20 family; Identified by similarity to GB:CAE31747.1; match to protein family HMM PF00011; Belongs to the small heat shock protein (HSP20) family. | ATP-dependent protease La; ATP-dependent serine protease that mediates the selective degradation of mutant and abnormal proteins as well as certain short- lived regulatory proteins. Required for cellular homeostasis and for survival from DNA damage and developmental changes induced by stress. Degrades polypeptides processively to yield small peptide fragments that are 5 to 10 amino acids long. Binds to DNA in a double-stranded, site-specific manner. | 0.822 |
| AFE_3000 | dnaJ | AFE_3000 | AFE_2664 | Identified by similarity to SP:Q60176; match to protein family HMM PF00056. | 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 [...] | 0.425 |
| AFE_3000 | dnaK | AFE_3000 | AFE_2665 | Identified by similarity to SP:Q60176; match to protein family HMM PF00056. | Chaperone protein Dnak; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.541 |
| AFE_3000 | groEL | AFE_3000 | AFE_0542 | Identified by similarity to SP:Q60176; match to protein family HMM PF00056. | Chaperonin, 60 kDa; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.923 |
| AFE_3000 | grpE | AFE_3000 | AFE_2666 | Identified by similarity to SP:Q60176; match to protein family HMM PF00056. | 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 [...] | 0.487 |
| AFE_3000 | hscA | AFE_3000 | AFE_0677 | Identified by similarity to SP:Q60176; match to protein family HMM PF00056. | 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. | 0.541 |
| AFE_3000 | lon-2 | AFE_3000 | AFE_0872 | Identified by similarity to SP:Q60176; match to protein family HMM PF00056. | ATP-dependent protease La; ATP-dependent serine protease that mediates the selective degradation of mutant and abnormal proteins as well as certain short- lived regulatory proteins. Required for cellular homeostasis and for survival from DNA damage and developmental changes induced by stress. Degrades polypeptides processively to yield small peptide fragments that are 5 to 10 amino acids long. Binds to DNA in a double-stranded, site-specific manner. | 0.641 |
| dnaJ | AFE_3000 | AFE_2664 | AFE_3000 | 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 [...] | Identified by similarity to SP:Q60176; match to protein family HMM PF00056. | 0.425 |
| dnaJ | dnaK | AFE_2664 | AFE_2665 | 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 [...] | Chaperone protein Dnak; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.998 |
| dnaJ | groEL | AFE_2664 | AFE_0542 | 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 [...] | Chaperonin, 60 kDa; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.968 |
| dnaJ | grpE | AFE_2664 | AFE_2666 | 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 [...] | 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 [...] | 0.992 |
| dnaJ | hscA | AFE_2664 | AFE_0677 | 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 [...] | 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. | 0.991 |
| dnaJ | hslU | AFE_2664 | AFE_2748 | 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 [...] | 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. | 0.929 |
| dnaJ | hslV | AFE_2664 | AFE_2747 | 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 [...] | Heat shock protein HslV; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.886 |
| dnaJ | htpG | AFE_2664 | AFE_3158 | 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 [...] | Heat shock protein HtpG; Molecular chaperone. Has ATPase activity. | 0.992 |
