node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
ABK46393.1 | dnaJ | Shewana3_0149 | Shewana3_0960 | PFAM: RNA-binding S4 domain protein; KEGG: son:SO0164 heat shock protein 15; Belongs to the HSP15 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 [...] | 0.533 |
ABK46393.1 | grpE | Shewana3_0149 | Shewana3_2902 | PFAM: RNA-binding S4 domain protein; KEGG: son:SO0164 heat shock protein 15; Belongs to the HSP15 family. | GrpE 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. Several rounds of ATP-dependent i [...] | 0.566 |
ABK46393.1 | hslO | Shewana3_0149 | Shewana3_0148 | PFAM: RNA-binding S4 domain protein; KEGG: son:SO0164 heat shock protein 15; Belongs to the HSP15 family. | Hsp33 protein; Redox regulated molecular chaperone. Protects both thermally unfolding and oxidatively damaged proteins from irreversible aggregation. Plays an important role in the bacterial defense system toward oxidative stress. | 0.947 |
ABK46393.1 | hslU | Shewana3_0149 | Shewana3_3700 | PFAM: RNA-binding S4 domain protein; KEGG: son:SO0164 heat shock protein 15; Belongs to the HSP15 family. | Heat shock protein HslVU, ATPase subunit HslU; 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. | 0.575 |
ABK46393.1 | hslV | Shewana3_0149 | Shewana3_3699 | PFAM: RNA-binding S4 domain protein; KEGG: son:SO0164 heat shock protein 15; Belongs to the HSP15 family. | HslV component of HslUV peptidase. Threonine peptidase. MEROPS family T01B; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.670 |
ABK46393.1 | htpG | Shewana3_0149 | Shewana3_2443 | PFAM: RNA-binding S4 domain protein; KEGG: son:SO0164 heat shock protein 15; Belongs to the HSP15 family. | Heat shock protein Hsp90; Molecular chaperone. Has ATPase activity. | 0.483 |
ABK48500.1 | dnaJ | Shewana3_2271 | Shewana3_0960 | PFAM: heat shock protein Hsp20; KEGG: son:SO2277 16 kDa heat shock protein A; Belongs to the small heat shock protein (HSP20) 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 [...] | 0.566 |
ABK48500.1 | grpE | Shewana3_2271 | Shewana3_2902 | PFAM: heat shock protein Hsp20; KEGG: son:SO2277 16 kDa heat shock protein A; Belongs to the small heat shock protein (HSP20) family. | GrpE 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. Several rounds of ATP-dependent i [...] | 0.688 |
ABK48500.1 | hslO | Shewana3_2271 | Shewana3_0148 | PFAM: heat shock protein Hsp20; KEGG: son:SO2277 16 kDa heat shock protein A; Belongs to the small heat shock protein (HSP20) family. | Hsp33 protein; Redox regulated molecular chaperone. Protects both thermally unfolding and oxidatively damaged proteins from irreversible aggregation. Plays an important role in the bacterial defense system toward oxidative stress. | 0.544 |
ABK48500.1 | hslU | Shewana3_2271 | Shewana3_3700 | PFAM: heat shock protein Hsp20; KEGG: son:SO2277 16 kDa heat shock protein A; Belongs to the small heat shock protein (HSP20) family. | Heat shock protein HslVU, ATPase subunit HslU; 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. | 0.582 |
ABK48500.1 | hslV | Shewana3_2271 | Shewana3_3699 | PFAM: heat shock protein Hsp20; KEGG: son:SO2277 16 kDa heat shock protein A; Belongs to the small heat shock protein (HSP20) family. | HslV component of HslUV peptidase. Threonine peptidase. MEROPS family T01B; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.600 |
ABK48500.1 | htpG | Shewana3_2271 | Shewana3_2443 | PFAM: heat shock protein Hsp20; KEGG: son:SO2277 16 kDa heat shock protein A; Belongs to the small heat shock protein (HSP20) family. | Heat shock protein Hsp90; Molecular chaperone. Has ATPase activity. | 0.737 |
ABK48500.1 | lon | Shewana3_2271 | Shewana3_2659 | PFAM: heat shock protein Hsp20; KEGG: son:SO2277 16 kDa heat shock protein A; Belongs to the small heat shock protein (HSP20) family. | Lon-A peptidase. Serine peptidase. MEROPS family S16; 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. | 0.563 |
dnaJ | ABK46393.1 | Shewana3_0960 | Shewana3_0149 | 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 [...] | PFAM: RNA-binding S4 domain protein; KEGG: son:SO0164 heat shock protein 15; Belongs to the HSP15 family. | 0.533 |
dnaJ | ABK48500.1 | Shewana3_0960 | Shewana3_2271 | 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 [...] | PFAM: heat shock protein Hsp20; KEGG: son:SO2277 16 kDa heat shock protein A; Belongs to the small heat shock protein (HSP20) family. | 0.566 |
dnaJ | ftsH | Shewana3_0960 | Shewana3_1023 | 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 [...] | 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. | 0.582 |
dnaJ | groL | Shewana3_0960 | Shewana3_3567 | 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 [...] | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.923 |
dnaJ | grpE | Shewana3_0960 | Shewana3_2902 | 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 [...] | GrpE 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. Several rounds of ATP-dependent i [...] | 0.969 |
dnaJ | hslO | Shewana3_0960 | Shewana3_0148 | 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 [...] | Hsp33 protein; Redox regulated molecular chaperone. Protects both thermally unfolding and oxidatively damaged proteins from irreversible aggregation. Plays an important role in the bacterial defense system toward oxidative stress. | 0.562 |
dnaJ | hslU | Shewana3_0960 | Shewana3_3700 | 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 [...] | Heat shock protein HslVU, ATPase subunit HslU; 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. | 0.869 |