| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| AMF_867 | dnaK | AMF_867 | AMF_630 | Called by Glimmer 2; Conserved hypothetical protein called by Glimmer 2; psort: bacterial inner membrane --- Certainty= 0.582(Affirmative). | DNAK protein; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.971 |
| AMF_867 | groEL | AMF_867 | AMF_725 | Called by Glimmer 2; Conserved hypothetical protein called by Glimmer 2; psort: bacterial inner membrane --- Certainty= 0.582(Affirmative). | 60 kD chaperonin (groEL); Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.776 |
| AMF_867 | groES | AMF_867 | AMF_724 | Called by Glimmer 2; Conserved hypothetical protein called by Glimmer 2; psort: bacterial inner membrane --- Certainty= 0.582(Affirmative). | 10 KD chaperonin (groES); Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.713 |
| AMF_867 | grpE | AMF_867 | AMF_012 | Called by Glimmer 2; Conserved hypothetical protein called by Glimmer 2; psort: bacterial inner membrane --- Certainty= 0.582(Affirmative). | GrpE protein (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-depe [...] | 0.893 |
| AMF_867 | hscA | AMF_867 | AMF_485 | Called by Glimmer 2; Conserved hypothetical protein called by Glimmer 2; psort: bacterial inner membrane --- Certainty= 0.582(Affirmative). | Heat shock protein (hscA); Chaperone involved in the maturation of iron-sulfur cluster- containing proteins. Has a low intrinsic ATPase activity which is markedly stimulated by HscB. | 0.971 |
| AMF_867 | hslU | AMF_867 | AMF_760 | Called by Glimmer 2; Conserved hypothetical protein called by Glimmer 2; psort: bacterial inner membrane --- Certainty= 0.582(Affirmative). | Heat shock protein (hslU); ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. | 0.664 |
| AMF_867 | hslV | AMF_867 | AMF_759 | Called by Glimmer 2; Conserved hypothetical protein called by Glimmer 2; psort: bacterial inner membrane --- Certainty= 0.582(Affirmative). | Heat shock protein (hslV); Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.592 |
| AMF_867 | htpG | AMF_867 | AMF_276 | Called by Glimmer 2; Conserved hypothetical protein called by Glimmer 2; psort: bacterial inner membrane --- Certainty= 0.582(Affirmative). | Heat shock protein (htpG); Molecular chaperone. Has ATPase activity. | 0.975 |
| AMF_867 | lon | AMF_867 | AMF_232 | Called by Glimmer 2; Conserved hypothetical protein called by Glimmer 2; psort: bacterial inner membrane --- Certainty= 0.582(Affirmative). | ATP-dependent protease LA (lon); 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. | 0.614 |
| dnaJ | dnaK | AMF_978 | AMF_630 | DNAJ 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, DnaK [...] | DNAK protein; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.999 |
| dnaJ | groEL | AMF_978 | AMF_725 | DNAJ 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, DnaK [...] | 60 kD chaperonin (groEL); Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.923 |
| dnaJ | groES | AMF_978 | AMF_724 | DNAJ 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, DnaK [...] | 10 KD chaperonin (groES); Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.905 |
| dnaJ | grpE | AMF_978 | AMF_012 | DNAJ 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, DnaK [...] | GrpE protein (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-depe [...] | 0.984 |
| dnaJ | hscA | AMF_978 | AMF_485 | DNAJ 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, DnaK [...] | Heat shock protein (hscA); Chaperone involved in the maturation of iron-sulfur cluster- containing proteins. Has a low intrinsic ATPase activity which is markedly stimulated by HscB. | 0.996 |
| dnaJ | hslU | AMF_978 | AMF_760 | DNAJ 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, DnaK [...] | Heat shock protein (hslU); ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. | 0.941 |
| dnaJ | hslV | AMF_978 | AMF_759 | DNAJ 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, DnaK [...] | Heat shock protein (hslV); Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.853 |
| dnaJ | htpG | AMF_978 | AMF_276 | DNAJ 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, DnaK [...] | Heat shock protein (htpG); Molecular chaperone. Has ATPase activity. | 0.995 |
| dnaJ | lon | AMF_978 | AMF_232 | DNAJ 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, DnaK [...] | ATP-dependent protease LA (lon); 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. | 0.814 |
| dnaK | AMF_867 | AMF_630 | AMF_867 | DNAK protein; Acts as a chaperone; Belongs to the heat shock protein 70 family. | Called by Glimmer 2; Conserved hypothetical protein called by Glimmer 2; psort: bacterial inner membrane --- Certainty= 0.582(Affirmative). | 0.971 |
| dnaK | dnaJ | AMF_630 | AMF_978 | DNAK protein; Acts as a chaperone; Belongs to the heat shock protein 70 family. | DNAJ 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, DnaK [...] | 0.999 |