node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
ANS85246.1 | ANS85926.1 | VSVS12_01479 | VSVS12_02165 | DnaJ like protein subfamily C member 24; Stimulates the ATPase activity of several Hsp70-type chaperones. This ability is enhanced by iron-binding. The iron- bound form is redox-active and can function as electron carrier. Plays a role in the diphthamide biosynthesis, a post-translational modification of histidine which occurs in translation elongation factor 2 (EEF2) (By similarity); Belongs to the DPH4 family; Contains 1 DPH-type zinc finger; Contains 1 J domain. | ATP-dependent specificity component of the ClpAP protease. It directs the protease to specific substrates. It has unfoldase activity. The primary function of the ClpA-ClpP complex appears to be the degradation of unfolded or abnormal proteins (By similarity); Belongs to the ClpA/ClpB family. | 0.646 |
ANS85246.1 | clpB | VSVS12_01479 | VSVS12_00790 | DnaJ like protein subfamily C member 24; Stimulates the ATPase activity of several Hsp70-type chaperones. This ability is enhanced by iron-binding. The iron- bound form is redox-active and can function as electron carrier. Plays a role in the diphthamide biosynthesis, a post-translational modification of histidine which occurs in translation elongation factor 2 (EEF2) (By similarity); Belongs to the DPH4 family; Contains 1 DPH-type zinc finger; Contains 1 J domain. | Chaperone protein 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. | 0.646 |
ANS85246.1 | dnaK | VSVS12_01479 | VSVS12_01480 | DnaJ like protein subfamily C member 24; Stimulates the ATPase activity of several Hsp70-type chaperones. This ability is enhanced by iron-binding. The iron- bound form is redox-active and can function as electron carrier. Plays a role in the diphthamide biosynthesis, a post-translational modification of histidine which occurs in translation elongation factor 2 (EEF2) (By similarity); Belongs to the DPH4 family; Contains 1 DPH-type zinc finger; Contains 1 J domain. | Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.974 |
ANS85246.1 | dnaK-2 | VSVS12_01479 | VSVS12_02412 | DnaJ like protein subfamily C member 24; Stimulates the ATPase activity of several Hsp70-type chaperones. This ability is enhanced by iron-binding. The iron- bound form is redox-active and can function as electron carrier. Plays a role in the diphthamide biosynthesis, a post-translational modification of histidine which occurs in translation elongation factor 2 (EEF2) (By similarity); Belongs to the DPH4 family; Contains 1 DPH-type zinc finger; Contains 1 J domain. | Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.955 |
ANS85246.1 | groL | VSVS12_01479 | VSVS12_00362 | DnaJ like protein subfamily C member 24; Stimulates the ATPase activity of several Hsp70-type chaperones. This ability is enhanced by iron-binding. The iron- bound form is redox-active and can function as electron carrier. Plays a role in the diphthamide biosynthesis, a post-translational modification of histidine which occurs in translation elongation factor 2 (EEF2) (By similarity); Belongs to the DPH4 family; Contains 1 DPH-type zinc finger; Contains 1 J domain. | 60 kDa chaperonin; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.819 |
ANS85246.1 | groS | VSVS12_01479 | VSVS12_00361 | DnaJ like protein subfamily C member 24; Stimulates the ATPase activity of several Hsp70-type chaperones. This ability is enhanced by iron-binding. The iron- bound form is redox-active and can function as electron carrier. Plays a role in the diphthamide biosynthesis, a post-translational modification of histidine which occurs in translation elongation factor 2 (EEF2) (By similarity); Belongs to the DPH4 family; Contains 1 DPH-type zinc finger; Contains 1 J domain. | 10 kDa chaperonin; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.664 |
ANS85246.1 | grpE | VSVS12_01479 | VSVS12_02418 | DnaJ like protein subfamily C member 24; Stimulates the ATPase activity of several Hsp70-type chaperones. This ability is enhanced by iron-binding. The iron- bound form is redox-active and can function as electron carrier. Plays a role in the diphthamide biosynthesis, a post-translational modification of histidine which occurs in translation elongation factor 2 (EEF2) (By similarity); Belongs to the DPH4 family; Contains 1 DPH-type zinc finger; Contains 1 J domain. | Protein 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-dependent i [...] | 0.936 |
ANS85246.1 | htpG | VSVS12_01479 | VSVS12_00953 | DnaJ like protein subfamily C member 24; Stimulates the ATPase activity of several Hsp70-type chaperones. This ability is enhanced by iron-binding. The iron- bound form is redox-active and can function as electron carrier. Plays a role in the diphthamide biosynthesis, a post-translational modification of histidine which occurs in translation elongation factor 2 (EEF2) (By similarity); Belongs to the DPH4 family; Contains 1 DPH-type zinc finger; Contains 1 J domain. | Chaperone protein HtpG; Molecular chaperone. Has ATPase activity. | 0.883 |
ANS85926.1 | ANS85246.1 | VSVS12_02165 | VSVS12_01479 | ATP-dependent specificity component of the ClpAP protease. It directs the protease to specific substrates. It has unfoldase activity. The primary function of the ClpA-ClpP complex appears to be the degradation of unfolded or abnormal proteins (By similarity); Belongs to the ClpA/ClpB family. | DnaJ like protein subfamily C member 24; Stimulates the ATPase activity of several Hsp70-type chaperones. This ability is enhanced by iron-binding. The iron- bound form is redox-active and can function as electron carrier. Plays a role in the diphthamide biosynthesis, a post-translational modification of histidine which occurs in translation elongation factor 2 (EEF2) (By similarity); Belongs to the DPH4 family; Contains 1 DPH-type zinc finger; Contains 1 J domain. | 0.646 |
ANS85926.1 | dnaJ | VSVS12_02165 | VSVS12_02411 | ATP-dependent specificity component of the ClpAP protease. It directs the protease to specific substrates. It has unfoldase activity. The primary function of the ClpA-ClpP complex appears to be the degradation of unfolded or abnormal proteins (By similarity); 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 [...] | 0.646 |
ANS85926.1 | dnaK | VSVS12_02165 | VSVS12_01480 | ATP-dependent specificity component of the ClpAP protease. It directs the protease to specific substrates. It has unfoldase activity. The primary function of the ClpA-ClpP complex appears to be the degradation of unfolded or abnormal proteins (By similarity); Belongs to the ClpA/ClpB family. | Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.814 |
ANS85926.1 | dnaK-2 | VSVS12_02165 | VSVS12_02412 | ATP-dependent specificity component of the ClpAP protease. It directs the protease to specific substrates. It has unfoldase activity. The primary function of the ClpA-ClpP complex appears to be the degradation of unfolded or abnormal proteins (By similarity); Belongs to the ClpA/ClpB family. | Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.814 |
ANS85926.1 | groL | VSVS12_02165 | VSVS12_00362 | ATP-dependent specificity component of the ClpAP protease. It directs the protease to specific substrates. It has unfoldase activity. The primary function of the ClpA-ClpP complex appears to be the degradation of unfolded or abnormal proteins (By similarity); Belongs to the ClpA/ClpB family. | 60 kDa chaperonin; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.697 |
ANS85926.1 | groS | VSVS12_02165 | VSVS12_00361 | ATP-dependent specificity component of the ClpAP protease. It directs the protease to specific substrates. It has unfoldase activity. The primary function of the ClpA-ClpP complex appears to be the degradation of unfolded or abnormal proteins (By similarity); Belongs to the ClpA/ClpB family. | 10 kDa chaperonin; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.664 |
ANS85926.1 | grpE | VSVS12_02165 | VSVS12_02418 | ATP-dependent specificity component of the ClpAP protease. It directs the protease to specific substrates. It has unfoldase activity. The primary function of the ClpA-ClpP complex appears to be the degradation of unfolded or abnormal proteins (By similarity); Belongs to the ClpA/ClpB family. | Protein 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-dependent i [...] | 0.794 |
ANS85926.1 | htpG | VSVS12_02165 | VSVS12_00953 | ATP-dependent specificity component of the ClpAP protease. It directs the protease to specific substrates. It has unfoldase activity. The primary function of the ClpA-ClpP complex appears to be the degradation of unfolded or abnormal proteins (By similarity); Belongs to the ClpA/ClpB family. | Chaperone protein HtpG; Molecular chaperone. Has ATPase activity. | 0.683 |
clpB | ANS85246.1 | VSVS12_00790 | VSVS12_01479 | Chaperone protein 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. | DnaJ like protein subfamily C member 24; Stimulates the ATPase activity of several Hsp70-type chaperones. This ability is enhanced by iron-binding. The iron- bound form is redox-active and can function as electron carrier. Plays a role in the diphthamide biosynthesis, a post-translational modification of histidine which occurs in translation elongation factor 2 (EEF2) (By similarity); Belongs to the DPH4 family; Contains 1 DPH-type zinc finger; Contains 1 J domain. | 0.646 |
clpB | dnaJ | VSVS12_00790 | VSVS12_02411 | Chaperone protein 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 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 [...] | 0.646 |
clpB | dnaK | VSVS12_00790 | VSVS12_01480 | Chaperone protein 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 protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.827 |
clpB | dnaK-2 | VSVS12_00790 | VSVS12_02412 | Chaperone protein 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 protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.836 |