node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
LVIS_0499 | LVIS_0500 | LVIS_0499 | LVIS_0500 | Protein-tyrosine-phosphatase; Belongs to the low molecular weight phosphotyrosine protein phosphatase family. | Hypothetical protein. | 0.535 |
LVIS_0499 | LVIS_0502 | LVIS_0499 | LVIS_0502 | Protein-tyrosine-phosphatase; Belongs to the low molecular weight phosphotyrosine protein phosphatase family. | Hypothetical protein. | 0.416 |
LVIS_0499 | htpX | LVIS_0499 | LVIS_0501 | Protein-tyrosine-phosphatase; Belongs to the low molecular weight phosphotyrosine protein phosphatase family. | HtpX-2 peptidase. Metallo peptidase. MEROPS family M48B; Belongs to the peptidase M48B family. | 0.534 |
LVIS_0500 | LVIS_0499 | LVIS_0500 | LVIS_0499 | Hypothetical protein. | Protein-tyrosine-phosphatase; Belongs to the low molecular weight phosphotyrosine protein phosphatase family. | 0.535 |
LVIS_0500 | LVIS_0502 | LVIS_0500 | LVIS_0502 | Hypothetical protein. | Hypothetical protein. | 0.611 |
LVIS_0500 | htpX | LVIS_0500 | LVIS_0501 | Hypothetical protein. | HtpX-2 peptidase. Metallo peptidase. MEROPS family M48B; Belongs to the peptidase M48B family. | 0.888 |
LVIS_0502 | LVIS_0499 | LVIS_0502 | LVIS_0499 | Hypothetical protein. | Protein-tyrosine-phosphatase; Belongs to the low molecular weight phosphotyrosine protein phosphatase family. | 0.416 |
LVIS_0502 | LVIS_0500 | LVIS_0502 | LVIS_0500 | Hypothetical protein. | Hypothetical protein. | 0.611 |
LVIS_0502 | htpX | LVIS_0502 | LVIS_0501 | Hypothetical protein. | HtpX-2 peptidase. Metallo peptidase. MEROPS family M48B; Belongs to the peptidase M48B family. | 0.602 |
clpB | dnaJ | LVIS_0762 | LVIS_1328 | ATP-binding subunit of Clp protease and DnaK/DnaJ chaperones; 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. | DnaJ-class molecular chaperone with C-terminal Zn finger domain; 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 A [...] | 0.738 |
clpB | grpE | LVIS_0762 | LVIS_1330 | ATP-binding subunit of Clp protease and DnaK/DnaJ chaperones; 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. | 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. [...] | 0.743 |
clpB | htpX | LVIS_0762 | LVIS_0501 | ATP-binding subunit of Clp protease and DnaK/DnaJ chaperones; 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. | HtpX-2 peptidase. Metallo peptidase. MEROPS family M48B; Belongs to the peptidase M48B family. | 0.487 |
dnaJ | clpB | LVIS_1328 | LVIS_0762 | DnaJ-class molecular chaperone with C-terminal Zn finger domain; 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 A [...] | ATP-binding subunit of Clp protease and DnaK/DnaJ chaperones; 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. | 0.738 |
dnaJ | ftsH | LVIS_1328 | LVIS_0523 | DnaJ-class molecular chaperone with C-terminal Zn finger domain; 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 A [...] | FtsH-2 peptidase. Metallo peptidase. MEROPS family M41; 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. | 0.653 |
dnaJ | grpE | LVIS_1328 | LVIS_1330 | DnaJ-class molecular chaperone with C-terminal Zn finger domain; 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 A [...] | 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. [...] | 0.994 |
dnaJ | htpX | LVIS_1328 | LVIS_0501 | DnaJ-class molecular chaperone with C-terminal Zn finger domain; 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 A [...] | HtpX-2 peptidase. Metallo peptidase. MEROPS family M48B; Belongs to the peptidase M48B family. | 0.558 |
ftsH | dnaJ | LVIS_0523 | LVIS_1328 | FtsH-2 peptidase. Metallo peptidase. MEROPS family M41; 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. | DnaJ-class molecular chaperone with C-terminal Zn finger domain; 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 A [...] | 0.653 |
ftsH | grpE | LVIS_0523 | LVIS_1330 | FtsH-2 peptidase. Metallo peptidase. MEROPS family M41; 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. | 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. [...] | 0.454 |
ftsH | htpX | LVIS_0523 | LVIS_0501 | FtsH-2 peptidase. Metallo peptidase. MEROPS family M41; 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. | HtpX-2 peptidase. Metallo peptidase. MEROPS family M48B; Belongs to the peptidase M48B family. | 0.499 |
grpE | clpB | LVIS_1330 | LVIS_0762 | 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. [...] | ATP-binding subunit of Clp protease and DnaK/DnaJ chaperones; 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. | 0.743 |