| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| ECA1820 | dnaJ | ECA1820 | ECA3881 | Conserved hypothetical protein; Similar to Salmonella typhimurium putative heat shock protein yegd or stm2125 SWALL:Q8ZNQ4 (EMBL:AE008794) (450 aa) fasta scores: E(): 1.2e-121, 68.22% id in 450 aa, and to Escherichia coli hypothetical chaperone protein yegd yegd or b2069 SWALL:YEGD_ECOLI (SWALL:P36928) (450 aa) fasta scores: E(): 1.6e-121, 69.33% id in 450 aa. | 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 [...] | 0.889 |
| ECA1820 | groL | ECA1820 | ECA0625 | Conserved hypothetical protein; Similar to Salmonella typhimurium putative heat shock protein yegd or stm2125 SWALL:Q8ZNQ4 (EMBL:AE008794) (450 aa) fasta scores: E(): 1.2e-121, 68.22% id in 450 aa, and to Escherichia coli hypothetical chaperone protein yegd yegd or b2069 SWALL:YEGD_ECOLI (SWALL:P36928) (450 aa) fasta scores: E(): 1.6e-121, 69.33% id in 450 aa. | 60 kDa chaperonin; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.845 |
| ECA1820 | groS | ECA1820 | ECA0624 | Conserved hypothetical protein; Similar to Salmonella typhimurium putative heat shock protein yegd or stm2125 SWALL:Q8ZNQ4 (EMBL:AE008794) (450 aa) fasta scores: E(): 1.2e-121, 68.22% id in 450 aa, and to Escherichia coli hypothetical chaperone protein yegd yegd or b2069 SWALL:YEGD_ECOLI (SWALL:P36928) (450 aa) fasta scores: E(): 1.6e-121, 69.33% id in 450 aa. | 10 kDa chaperonin; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.786 |
| ECA1820 | grpE | ECA1820 | ECA0842 | Conserved hypothetical protein; Similar to Salmonella typhimurium putative heat shock protein yegd or stm2125 SWALL:Q8ZNQ4 (EMBL:AE008794) (450 aa) fasta scores: E(): 1.2e-121, 68.22% id in 450 aa, and to Escherichia coli hypothetical chaperone protein yegd yegd or b2069 SWALL:YEGD_ECOLI (SWALL:P36928) (450 aa) fasta scores: E(): 1.6e-121, 69.33% id in 450 aa. | 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. Several rounds of ATP-depen [...] | 0.907 |
| ECA1820 | hslU | ECA1820 | ECA4262 | Conserved hypothetical protein; Similar to Salmonella typhimurium putative heat shock protein yegd or stm2125 SWALL:Q8ZNQ4 (EMBL:AE008794) (450 aa) fasta scores: E(): 1.2e-121, 68.22% id in 450 aa, and to Escherichia coli hypothetical chaperone protein yegd yegd or b2069 SWALL:YEGD_ECOLI (SWALL:P36928) (450 aa) fasta scores: E(): 1.6e-121, 69.33% id in 450 aa. | ATP-dependent Hsl protease ATP-binding subunit (heat shock protein); 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. | 0.544 |
| ECA1820 | hslV | ECA1820 | ECA4261 | Conserved hypothetical protein; Similar to Salmonella typhimurium putative heat shock protein yegd or stm2125 SWALL:Q8ZNQ4 (EMBL:AE008794) (450 aa) fasta scores: E(): 1.2e-121, 68.22% id in 450 aa, and to Escherichia coli hypothetical chaperone protein yegd yegd or b2069 SWALL:YEGD_ECOLI (SWALL:P36928) (450 aa) fasta scores: E(): 1.6e-121, 69.33% id in 450 aa. | ATP-dependent protease (heat shock protein); Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.475 |
| ECA1820 | htpG | ECA1820 | ECA1179 | Conserved hypothetical protein; Similar to Salmonella typhimurium putative heat shock protein yegd or stm2125 SWALL:Q8ZNQ4 (EMBL:AE008794) (450 aa) fasta scores: E(): 1.2e-121, 68.22% id in 450 aa, and to Escherichia coli hypothetical chaperone protein yegd yegd or b2069 SWALL:YEGD_ECOLI (SWALL:P36928) (450 aa) fasta scores: E(): 1.6e-121, 69.33% id in 450 aa. | Chaperone protein; Molecular chaperone. Has ATPase activity. | 0.864 |
| ECA1820 | lon | ECA1820 | ECA1150 | Conserved hypothetical protein; Similar to Salmonella typhimurium putative heat shock protein yegd or stm2125 SWALL:Q8ZNQ4 (EMBL:AE008794) (450 aa) fasta scores: E(): 1.2e-121, 68.22% id in 450 aa, and to Escherichia coli hypothetical chaperone protein yegd yegd or b2069 SWALL:YEGD_ECOLI (SWALL:P36928) (450 aa) fasta scores: E(): 1.6e-121, 69.33% id in 450 aa. | 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. | 0.663 |
| dnaJ | ECA1820 | ECA3881 | ECA1820 | 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 [...] | Conserved hypothetical protein; Similar to Salmonella typhimurium putative heat shock protein yegd or stm2125 SWALL:Q8ZNQ4 (EMBL:AE008794) (450 aa) fasta scores: E(): 1.2e-121, 68.22% id in 450 aa, and to Escherichia coli hypothetical chaperone protein yegd yegd or b2069 SWALL:YEGD_ECOLI (SWALL:P36928) (450 aa) fasta scores: E(): 1.6e-121, 69.33% id in 450 aa. | 0.889 |
| dnaJ | dnaK | ECA3881 | ECA3882 | 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. | 0.999 |
| dnaJ | groL | ECA3881 | ECA0625 | 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 [...] | 60 kDa chaperonin; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.988 |
| dnaJ | groS | ECA3881 | ECA0624 | 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 [...] | 10 kDa chaperonin; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.852 |
| dnaJ | grpE | ECA3881 | ECA0842 | 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; 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-depen [...] | 0.996 |
| dnaJ | hscA | ECA3881 | ECA3233 | 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; Chaperone involved in the maturation of iron-sulfur cluster- containing proteins. Has a low intrinsic ATPase activity which is markedly stimulated by HscB. Involved in the maturation of IscU. | 0.986 |
| dnaJ | hslU | ECA3881 | ECA4262 | 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 [...] | ATP-dependent Hsl protease ATP-binding subunit (heat shock protein); 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. | 0.969 |
| dnaJ | hslV | ECA3881 | ECA4261 | 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 [...] | ATP-dependent protease (heat shock protein); Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.954 |
| dnaJ | htpG | ECA3881 | ECA1179 | 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; Molecular chaperone. Has ATPase activity. | 0.994 |
| dnaJ | lon | ECA3881 | ECA1150 | 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 [...] | 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. | 0.939 |
| dnaK | dnaJ | ECA3882 | ECA3881 | Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 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 [...] | 0.999 |
| dnaK | groL | ECA3882 | ECA0625 | Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 60 kDa chaperonin; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.968 |
