node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
KRT34692.1 | KRT35597.1 | HMPREF1705_03932 | HMPREF1705_02833 | KEGG: cbi:CLJ_B3821 2.2e-259 clpC; negative regulator of genetic competence MecB/ClpC K03696; Psort location: Cytoplasmic, score: 9.97; Belongs to the ClpA/ClpB family. | ATP-dependent protease HslVU, peptidase subunit; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.629 |
KRT34692.1 | KRT35688.1 | HMPREF1705_03932 | HMPREF1705_02931 | KEGG: cbi:CLJ_B3821 2.2e-259 clpC; negative regulator of genetic competence MecB/ClpC K03696; Psort location: Cytoplasmic, score: 9.97; Belongs to the ClpA/ClpB family. | DnaK family protein; KEGG: lre:Lreu_0706 6.2e-38 dnaK; molecular chaperone DnaK K04043; Psort location: Cytoplasmic, score: 9.97; Belongs to the heat shock protein 70 family. | 0.988 |
KRT34692.1 | dnaJ | HMPREF1705_03932 | HMPREF1705_02925 | KEGG: cbi:CLJ_B3821 2.2e-259 clpC; negative regulator of genetic competence MecB/ClpC K03696; Psort location: Cytoplasmic, score: 9.97; 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 [...] | 0.890 |
KRT34692.1 | dnaK | HMPREF1705_03932 | HMPREF1705_02924 | KEGG: cbi:CLJ_B3821 2.2e-259 clpC; negative regulator of genetic competence MecB/ClpC K03696; Psort location: Cytoplasmic, score: 9.97; Belongs to the ClpA/ClpB family. | Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.988 |
KRT34692.1 | groL | HMPREF1705_03932 | HMPREF1705_03010 | KEGG: cbi:CLJ_B3821 2.2e-259 clpC; negative regulator of genetic competence MecB/ClpC K03696; Psort location: Cytoplasmic, score: 9.97; Belongs to the ClpA/ClpB family. | Chaperonin GroL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.846 |
KRT34692.1 | groS | HMPREF1705_03932 | HMPREF1705_03009 | KEGG: cbi:CLJ_B3821 2.2e-259 clpC; negative regulator of genetic competence MecB/ClpC K03696; Psort location: Cytoplasmic, score: 9.97; Belongs to the ClpA/ClpB family. | Chaperonin GroS; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.852 |
KRT34692.1 | grpE | HMPREF1705_03932 | HMPREF1705_02923 | KEGG: cbi:CLJ_B3821 2.2e-259 clpC; negative regulator of genetic competence MecB/ClpC K03696; Psort location: Cytoplasmic, score: 9.97; 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 [...] | 0.900 |
KRT34692.1 | hslU | HMPREF1705_03932 | HMPREF1705_02834 | KEGG: cbi:CLJ_B3821 2.2e-259 clpC; negative regulator of genetic competence MecB/ClpC K03696; Psort location: Cytoplasmic, score: 9.97; Belongs to the ClpA/ClpB family. | ATP-dependent protease HslVU, ATPase subunit; 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. | 0.811 |
KRT35597.1 | KRT34692.1 | HMPREF1705_02833 | HMPREF1705_03932 | ATP-dependent protease HslVU, peptidase subunit; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | KEGG: cbi:CLJ_B3821 2.2e-259 clpC; negative regulator of genetic competence MecB/ClpC K03696; Psort location: Cytoplasmic, score: 9.97; Belongs to the ClpA/ClpB family. | 0.629 |
KRT35597.1 | KRT35688.1 | HMPREF1705_02833 | HMPREF1705_02931 | ATP-dependent protease HslVU, peptidase subunit; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | DnaK family protein; KEGG: lre:Lreu_0706 6.2e-38 dnaK; molecular chaperone DnaK K04043; Psort location: Cytoplasmic, score: 9.97; Belongs to the heat shock protein 70 family. | 0.551 |
KRT35597.1 | dnaJ | HMPREF1705_02833 | HMPREF1705_02925 | ATP-dependent protease HslVU, peptidase subunit; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 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 [...] | 0.666 |
KRT35597.1 | dnaK | HMPREF1705_02833 | HMPREF1705_02924 | ATP-dependent protease HslVU, peptidase subunit; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.551 |
KRT35597.1 | groL | HMPREF1705_02833 | HMPREF1705_03010 | ATP-dependent protease HslVU, peptidase subunit; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | Chaperonin GroL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.864 |
KRT35597.1 | groS | HMPREF1705_02833 | HMPREF1705_03009 | ATP-dependent protease HslVU, peptidase subunit; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | Chaperonin GroS; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.848 |
KRT35597.1 | grpE | HMPREF1705_02833 | HMPREF1705_02923 | ATP-dependent protease HslVU, peptidase subunit; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 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 [...] | 0.862 |
KRT35597.1 | hslU | HMPREF1705_02833 | HMPREF1705_02834 | ATP-dependent protease HslVU, peptidase subunit; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | ATP-dependent protease HslVU, ATPase subunit; 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. | 0.999 |
KRT35688.1 | KRT34692.1 | HMPREF1705_02931 | HMPREF1705_03932 | DnaK family protein; KEGG: lre:Lreu_0706 6.2e-38 dnaK; molecular chaperone DnaK K04043; Psort location: Cytoplasmic, score: 9.97; Belongs to the heat shock protein 70 family. | KEGG: cbi:CLJ_B3821 2.2e-259 clpC; negative regulator of genetic competence MecB/ClpC K03696; Psort location: Cytoplasmic, score: 9.97; Belongs to the ClpA/ClpB family. | 0.988 |
KRT35688.1 | KRT35597.1 | HMPREF1705_02931 | HMPREF1705_02833 | DnaK family protein; KEGG: lre:Lreu_0706 6.2e-38 dnaK; molecular chaperone DnaK K04043; Psort location: Cytoplasmic, score: 9.97; Belongs to the heat shock protein 70 family. | ATP-dependent protease HslVU, peptidase subunit; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.551 |
KRT35688.1 | dnaJ | HMPREF1705_02931 | HMPREF1705_02925 | DnaK family protein; KEGG: lre:Lreu_0706 6.2e-38 dnaK; molecular chaperone DnaK K04043; Psort location: Cytoplasmic, score: 9.97; 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 |
KRT35688.1 | dnaK | HMPREF1705_02931 | HMPREF1705_02924 | DnaK family protein; KEGG: lre:Lreu_0706 6.2e-38 dnaK; molecular chaperone DnaK K04043; Psort location: Cytoplasmic, score: 9.97; Belongs to the heat shock protein 70 family. | Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.905 |