| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| EAQ07035.1 | htpX | SKA53_01526 | SKA53_08161 | COG0670 Integral membrane protein, interacts with FtsH; Belongs to the BI1 family. | Heat shock protein HtpX; COG0501 Zn-dependent protease with chaperone function; Belongs to the peptidase M48B family. | 0.518 |
| EAQ07539.1 | EAQ07753.1 | SKA53_11918 | SKA53_12988 | FxsA; COG3030 Protein affecting phage T7 exclusion by the F plasmid. | COG3118 Thioredoxin domain-containing protein. | 0.791 |
| EAQ07539.1 | htpX | SKA53_11918 | SKA53_08161 | FxsA; COG3030 Protein affecting phage T7 exclusion by the F plasmid. | Heat shock protein HtpX; COG0501 Zn-dependent protease with chaperone function; Belongs to the peptidase M48B family. | 0.498 |
| EAQ07753.1 | EAQ07539.1 | SKA53_12988 | SKA53_11918 | COG3118 Thioredoxin domain-containing protein. | FxsA; COG3030 Protein affecting phage T7 exclusion by the F plasmid. | 0.791 |
| EAQ07753.1 | clpB | SKA53_12988 | SKA53_10369 | COG3118 Thioredoxin domain-containing protein. | Chaperone ClpB; Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE; Belongs to the ClpA/ClpB family. | 0.504 |
| EAQ07753.1 | dnaJ | SKA53_12988 | SKA53_11638 | COG3118 Thioredoxin domain-containing protein. | Chaperone, 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 and [...] | 0.724 |
| EAQ07753.1 | ftsH | SKA53_12988 | SKA53_08551 | COG3118 Thioredoxin domain-containing protein. | ATP-dependent metalloprotease FtsH; Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins; Belongs to the AAA ATPase family. In the central section; belongs to the AAA ATPase family. | 0.439 |
| EAQ07753.1 | groS | SKA53_12988 | SKA53_08661 | COG3118 Thioredoxin domain-containing protein. | Chaperonin Cpn10 (GroES); Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.587 |
| EAQ07753.1 | grpE | SKA53_12988 | SKA53_11833 | COG3118 Thioredoxin domain-containing protein. | 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 [...] | 0.897 |
| EAQ07753.1 | htpX | SKA53_12988 | SKA53_08161 | COG3118 Thioredoxin domain-containing protein. | Heat shock protein HtpX; COG0501 Zn-dependent protease with chaperone function; Belongs to the peptidase M48B family. | 0.550 |
| EAQ07753.1 | lon | SKA53_12988 | SKA53_02726 | COG3118 Thioredoxin domain-containing protein. | Probable ATP-dependent protease La protein; 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. | 0.561 |
| clpB | EAQ07753.1 | SKA53_10369 | SKA53_12988 | Chaperone ClpB; Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE; Belongs to the ClpA/ClpB family. | COG3118 Thioredoxin domain-containing protein. | 0.504 |
| clpB | dnaJ | SKA53_10369 | SKA53_11638 | Chaperone ClpB; Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE; Belongs to the ClpA/ClpB family. | Chaperone, 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 and [...] | 0.830 |
| clpB | groS | SKA53_10369 | SKA53_08661 | Chaperone ClpB; Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE; Belongs to the ClpA/ClpB family. | Chaperonin Cpn10 (GroES); Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.786 |
| clpB | grpE | SKA53_10369 | SKA53_11833 | Chaperone ClpB; Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE; Belongs to the ClpA/ClpB 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 [...] | 0.903 |
| clpB | htpX | SKA53_10369 | SKA53_08161 | Chaperone ClpB; Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE; Belongs to the ClpA/ClpB family. | Heat shock protein HtpX; COG0501 Zn-dependent protease with chaperone function; Belongs to the peptidase M48B family. | 0.574 |
| clpB | lon | SKA53_10369 | SKA53_02726 | Chaperone ClpB; Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE; Belongs to the ClpA/ClpB family. | Probable ATP-dependent protease La protein; 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. | 0.708 |
| clpB | rpoC | SKA53_10369 | SKA53_13278 | Chaperone ClpB; Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE; Belongs to the ClpA/ClpB family. | DNA-directed RNA polymerase beta' subunit; DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. | 0.461 |
| dnaJ | EAQ07753.1 | SKA53_11638 | SKA53_12988 | Chaperone, 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 and [...] | COG3118 Thioredoxin domain-containing protein. | 0.724 |
| dnaJ | clpB | SKA53_11638 | SKA53_10369 | Chaperone, 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 and [...] | Chaperone ClpB; Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE; Belongs to the ClpA/ClpB family. | 0.830 |
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