| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| AEX85087.1 | AEX85401.1 | Marpi_0649 | Marpi_0989 | DnaJ-class molecular chaperone with C-terminal Zn finger domain; PFAM: DnaJ domain. | ATPase with chaperone activity, ATP-binding subunit; PFAM: AAA domain (Cdc48 subfamily); Clp amino terminal domain; C-terminal, D2-small domain, of ClpB protein; ATPase family associated with various cellular activities (AAA); Belongs to the ClpA/ClpB family. | 0.786 |
| AEX85087.1 | dnaK | Marpi_0649 | Marpi_0460 | DnaJ-class molecular chaperone with C-terminal Zn finger domain; PFAM: DnaJ domain. | Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.990 |
| AEX85087.1 | groL | Marpi_0649 | Marpi_1900 | DnaJ-class molecular chaperone with C-terminal Zn finger domain; PFAM: DnaJ domain. | Chaperonin GroL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.768 |
| AEX85087.1 | groS | Marpi_0649 | Marpi_1899 | DnaJ-class molecular chaperone with C-terminal Zn finger domain; PFAM: DnaJ domain. | Co-chaperonin GroES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.704 |
| AEX85087.1 | grpE | Marpi_0649 | Marpi_1207 | DnaJ-class molecular chaperone with C-terminal Zn finger domain; PFAM: DnaJ domain. | Molecular chaperone GrpE (heat shock protein); 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. [...] | 0.912 |
| AEX85087.1 | hrcA | Marpi_0649 | Marpi_1208 | DnaJ-class molecular chaperone with C-terminal Zn finger domain; PFAM: DnaJ domain. | Transcriptional regulator of heat shock gene; Negative regulator of class I heat shock genes (grpE-dnaK- dnaJ and groELS operons). Prevents heat-shock induction of these operons. | 0.717 |
| AEX85087.1 | hslU | Marpi_0649 | Marpi_0659 | DnaJ-class molecular chaperone with C-terminal Zn finger domain; PFAM: DnaJ domain. | ATP-dependent protease HslVU, ATPase subunit; 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. | 0.768 |
| AEX85087.1 | hslV | Marpi_0649 | Marpi_1550 | DnaJ-class molecular chaperone with C-terminal Zn finger domain; PFAM: DnaJ domain. | ATP-dependent protease HslVU, peptidase subunit; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.608 |
| AEX85087.1 | lon | Marpi_0649 | Marpi_1531 | DnaJ-class molecular chaperone with C-terminal Zn finger domain; PFAM: DnaJ domain. | 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. | 0.680 |
| AEX85401.1 | AEX85087.1 | Marpi_0989 | Marpi_0649 | ATPase with chaperone activity, ATP-binding subunit; PFAM: AAA domain (Cdc48 subfamily); Clp amino terminal domain; C-terminal, D2-small domain, of ClpB protein; ATPase family associated with various cellular activities (AAA); Belongs to the ClpA/ClpB family. | DnaJ-class molecular chaperone with C-terminal Zn finger domain; PFAM: DnaJ domain. | 0.786 |
| AEX85401.1 | dnaJ | Marpi_0989 | Marpi_1206 | ATPase with chaperone activity, ATP-binding subunit; PFAM: AAA domain (Cdc48 subfamily); Clp amino terminal domain; C-terminal, D2-small domain, of ClpB protein; ATPase family associated with various cellular activities (AAA); Belongs to the ClpA/ClpB 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 [...] | 0.786 |
| AEX85401.1 | dnaK | Marpi_0989 | Marpi_0460 | ATPase with chaperone activity, ATP-binding subunit; PFAM: AAA domain (Cdc48 subfamily); Clp amino terminal domain; C-terminal, D2-small domain, of ClpB protein; ATPase family associated with various cellular activities (AAA); Belongs to the ClpA/ClpB family. | Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.957 |
| AEX85401.1 | groL | Marpi_0989 | Marpi_1900 | ATPase with chaperone activity, ATP-binding subunit; PFAM: AAA domain (Cdc48 subfamily); Clp amino terminal domain; C-terminal, D2-small domain, of ClpB protein; ATPase family associated with various cellular activities (AAA); Belongs to the ClpA/ClpB family. | Chaperonin GroL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.697 |
| AEX85401.1 | groS | Marpi_0989 | Marpi_1899 | ATPase with chaperone activity, ATP-binding subunit; PFAM: AAA domain (Cdc48 subfamily); Clp amino terminal domain; C-terminal, D2-small domain, of ClpB protein; ATPase family associated with various cellular activities (AAA); Belongs to the ClpA/ClpB family. | Co-chaperonin GroES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.706 |
| AEX85401.1 | grpE | Marpi_0989 | Marpi_1207 | ATPase with chaperone activity, ATP-binding subunit; PFAM: AAA domain (Cdc48 subfamily); Clp amino terminal domain; C-terminal, D2-small domain, of ClpB protein; ATPase family associated with various cellular activities (AAA); Belongs to the ClpA/ClpB family. | Molecular chaperone GrpE (heat shock protein); 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. [...] | 0.816 |
| AEX85401.1 | hrcA | Marpi_0989 | Marpi_1208 | ATPase with chaperone activity, ATP-binding subunit; PFAM: AAA domain (Cdc48 subfamily); Clp amino terminal domain; C-terminal, D2-small domain, of ClpB protein; ATPase family associated with various cellular activities (AAA); Belongs to the ClpA/ClpB family. | Transcriptional regulator of heat shock gene; Negative regulator of class I heat shock genes (grpE-dnaK- dnaJ and groELS operons). Prevents heat-shock induction of these operons. | 0.637 |
| AEX85401.1 | hslU | Marpi_0989 | Marpi_0659 | ATPase with chaperone activity, ATP-binding subunit; PFAM: AAA domain (Cdc48 subfamily); Clp amino terminal domain; C-terminal, D2-small domain, of ClpB protein; ATPase family associated with various cellular activities (AAA); Belongs to the ClpA/ClpB family. | ATP-dependent protease HslVU, ATPase subunit; 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. | 0.636 |
| AEX85401.1 | hslV | Marpi_0989 | Marpi_1550 | ATPase with chaperone activity, ATP-binding subunit; PFAM: AAA domain (Cdc48 subfamily); Clp amino terminal domain; C-terminal, D2-small domain, of ClpB protein; ATPase family associated with various cellular activities (AAA); Belongs to the ClpA/ClpB family. | ATP-dependent protease HslVU, peptidase subunit; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.518 |
| AEX85401.1 | lon | Marpi_0989 | Marpi_1531 | ATPase with chaperone activity, ATP-binding subunit; PFAM: AAA domain (Cdc48 subfamily); Clp amino terminal domain; C-terminal, D2-small domain, of ClpB protein; ATPase family associated with various cellular activities (AAA); Belongs to the ClpA/ClpB 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. | 0.702 |
| dnaJ | AEX85401.1 | Marpi_1206 | Marpi_0989 | 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 [...] | ATPase with chaperone activity, ATP-binding subunit; PFAM: AAA domain (Cdc48 subfamily); Clp amino terminal domain; C-terminal, D2-small domain, of ClpB protein; ATPase family associated with various cellular activities (AAA); Belongs to the ClpA/ClpB family. | 0.786 |