node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
SHE51443.1 | htpX | SAMN05444339_101588 | SAMN05444339_101585 | Amino acid ABC transporter substrate-binding protein, PAAT family. | Heat shock protein HtpX; Belongs to the peptidase M48B family. | 0.520 |
SHF04218.1 | SHF07451.1 | SAMN05444339_10394 | SAMN05444339_103196 | Thioredoxin. | UPF0716 protein FxsA. | 0.848 |
SHF04218.1 | SHF55554.1 | SAMN05444339_10394 | SAMN05444339_1084 | Thioredoxin. | ATP-dependent Zn proteases; Belongs to the AAA ATPase family. | 0.420 |
SHF04218.1 | clpB | SAMN05444339_10394 | SAMN05444339_1033 | Thioredoxin. | ATP-dependent Clp protease ATP-binding subunit 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. | 0.523 |
SHF04218.1 | dnaJ | SAMN05444339_10394 | SAMN05444339_103127 | Thioredoxin. | Molecular 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, [...] | 0.823 |
SHF04218.1 | ftsH | SAMN05444339_10394 | SAMN05444339_102195 | Thioredoxin. | Membrane protease FtsH catalytic subunit; 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. | 0.420 |
SHF04218.1 | groS | SAMN05444339_10394 | SAMN05444339_102361 | Thioredoxin. | Chaperonin GroES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.645 |
SHF04218.1 | grpE | SAMN05444339_10394 | SAMN05444339_103213 | Thioredoxin. | Molecular 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 [...] | 0.905 |
SHF04218.1 | htpX | SAMN05444339_10394 | SAMN05444339_101585 | Thioredoxin. | Heat shock protein HtpX; Belongs to the peptidase M48B family. | 0.657 |
SHF07451.1 | SHF04218.1 | SAMN05444339_103196 | SAMN05444339_10394 | UPF0716 protein FxsA. | Thioredoxin. | 0.848 |
SHF07451.1 | grpE | SAMN05444339_103196 | SAMN05444339_103213 | UPF0716 protein FxsA. | Molecular 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 [...] | 0.443 |
SHF07451.1 | htpX | SAMN05444339_103196 | SAMN05444339_101585 | UPF0716 protein FxsA. | Heat shock protein HtpX; Belongs to the peptidase M48B family. | 0.539 |
SHF43530.1 | htpX | SAMN05444339_10674 | SAMN05444339_101585 | Hypothetical protein; Belongs to the BI1 family. | Heat shock protein HtpX; Belongs to the peptidase M48B family. | 0.539 |
SHF55554.1 | SHF04218.1 | SAMN05444339_1084 | SAMN05444339_10394 | ATP-dependent Zn proteases; Belongs to the AAA ATPase family. | Thioredoxin. | 0.420 |
SHF55554.1 | dnaJ | SAMN05444339_1084 | SAMN05444339_103127 | ATP-dependent Zn proteases; Belongs to the AAA ATPase family. | Molecular 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, [...] | 0.638 |
SHF55554.1 | grpE | SAMN05444339_1084 | SAMN05444339_103213 | ATP-dependent Zn proteases; Belongs to the AAA ATPase family. | Molecular 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 [...] | 0.476 |
SHF55554.1 | htpX | SAMN05444339_1084 | SAMN05444339_101585 | ATP-dependent Zn proteases; Belongs to the AAA ATPase family. | Heat shock protein HtpX; Belongs to the peptidase M48B family. | 0.630 |
clpB | SHF04218.1 | SAMN05444339_1033 | SAMN05444339_10394 | ATP-dependent Clp protease ATP-binding subunit 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. | Thioredoxin. | 0.523 |
clpB | dnaJ | SAMN05444339_1033 | SAMN05444339_103127 | ATP-dependent Clp protease ATP-binding subunit 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. | Molecular 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, [...] | 0.889 |
clpB | groS | SAMN05444339_1033 | SAMN05444339_102361 | ATP-dependent Clp protease ATP-binding subunit 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 GroES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.852 |