node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
Veis_1547 | Veis_1557 | Veis_1547 | Veis_1557 | TIGRFAM: thioredoxin; PFAM: Thioredoxin domain; KEGG: pol:Bpro_4628 thioredoxin. | PFAM: AAA ATPase, central domain protein; ATPase associated with various cellular activities, AAA_5; SMART: AAA ATPase; KEGG: bam:Bamb_3094 AAA ATPase, central domain protein. | 0.488 |
Veis_1547 | dnaJ | Veis_1547 | Veis_0978 | TIGRFAM: thioredoxin; PFAM: Thioredoxin domain; KEGG: pol:Bpro_4628 thioredoxin. | 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 [...] | 0.769 |
Veis_1547 | groS | Veis_1547 | Veis_2566 | TIGRFAM: thioredoxin; PFAM: Thioredoxin domain; KEGG: pol:Bpro_4628 thioredoxin. | Chaperonin Cpn10; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.551 |
Veis_1547 | grpE | Veis_1547 | Veis_0980 | TIGRFAM: thioredoxin; PFAM: Thioredoxin domain; KEGG: pol:Bpro_4628 thioredoxin. | 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 [...] | 0.803 |
Veis_1547 | hslU | Veis_1547 | Veis_4560 | TIGRFAM: thioredoxin; PFAM: Thioredoxin domain; KEGG: pol:Bpro_4628 thioredoxin. | 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. | 0.821 |
Veis_1547 | htpX | Veis_1547 | Veis_1214 | TIGRFAM: thioredoxin; PFAM: Thioredoxin domain; KEGG: pol:Bpro_4628 thioredoxin. | HtpX peptidase. Metallo peptidase. MEROPS family M48B; PFAM: peptidase M48, Ste24p; HtpX domain protein; KEGG: pol:Bpro_1032 peptidase M48, Ste24p; Belongs to the peptidase M48B family. | 0.574 |
Veis_1547 | lon | Veis_1547 | Veis_4373 | TIGRFAM: thioredoxin; PFAM: Thioredoxin domain; KEGG: pol:Bpro_4628 thioredoxin. | 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. | 0.488 |
Veis_1557 | Veis_1547 | Veis_1557 | Veis_1547 | PFAM: AAA ATPase, central domain protein; ATPase associated with various cellular activities, AAA_5; SMART: AAA ATPase; KEGG: bam:Bamb_3094 AAA ATPase, central domain protein. | TIGRFAM: thioredoxin; PFAM: Thioredoxin domain; KEGG: pol:Bpro_4628 thioredoxin. | 0.488 |
Veis_1557 | dnaJ | Veis_1557 | Veis_0978 | PFAM: AAA ATPase, central domain protein; ATPase associated with various cellular activities, AAA_5; SMART: AAA ATPase; KEGG: bam:Bamb_3094 AAA ATPase, central domain protein. | 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 [...] | 0.720 |
Veis_1557 | ftsH | Veis_1557 | Veis_0211 | PFAM: AAA ATPase, central domain protein; ATPase associated with various cellular activities, AAA_5; SMART: AAA ATPase; KEGG: bam:Bamb_3094 AAA ATPase, central domain protein. | 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. | 0.539 |
Veis_1557 | groS | Veis_1557 | Veis_2566 | PFAM: AAA ATPase, central domain protein; ATPase associated with various cellular activities, AAA_5; SMART: AAA ATPase; KEGG: bam:Bamb_3094 AAA ATPase, central domain protein. | Chaperonin Cpn10; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.450 |
Veis_1557 | grpE | Veis_1557 | Veis_0980 | PFAM: AAA ATPase, central domain protein; ATPase associated with various cellular activities, AAA_5; SMART: AAA ATPase; KEGG: bam:Bamb_3094 AAA ATPase, central domain protein. | 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 [...] | 0.695 |
Veis_1557 | hslU | Veis_1557 | Veis_4560 | PFAM: AAA ATPase, central domain protein; ATPase associated with various cellular activities, AAA_5; SMART: AAA ATPase; KEGG: bam:Bamb_3094 AAA ATPase, central domain protein. | 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. | 0.706 |
Veis_1557 | htpX | Veis_1557 | Veis_1214 | PFAM: AAA ATPase, central domain protein; ATPase associated with various cellular activities, AAA_5; SMART: AAA ATPase; KEGG: bam:Bamb_3094 AAA ATPase, central domain protein. | HtpX peptidase. Metallo peptidase. MEROPS family M48B; PFAM: peptidase M48, Ste24p; HtpX domain protein; KEGG: pol:Bpro_1032 peptidase M48, Ste24p; Belongs to the peptidase M48B family. | 0.424 |
Veis_3069 | htpX | Veis_3069 | Veis_1214 | PFAM: protein of unknown function UPF0005; KEGG: rfr:Rfer_2776 protein of unknown function UPF0005; Belongs to the BI1 family. | HtpX peptidase. Metallo peptidase. MEROPS family M48B; PFAM: peptidase M48, Ste24p; HtpX domain protein; KEGG: pol:Bpro_1032 peptidase M48, Ste24p; Belongs to the peptidase M48B family. | 0.489 |
dnaJ | Veis_1547 | Veis_0978 | Veis_1547 | 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 [...] | TIGRFAM: thioredoxin; PFAM: Thioredoxin domain; KEGG: pol:Bpro_4628 thioredoxin. | 0.769 |
dnaJ | Veis_1557 | Veis_0978 | Veis_1557 | 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: AAA ATPase, central domain protein; ATPase associated with various cellular activities, AAA_5; SMART: AAA ATPase; KEGG: bam:Bamb_3094 AAA ATPase, central domain protein. | 0.720 |
dnaJ | ftsH | Veis_0978 | Veis_0211 | 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. | 0.695 |
dnaJ | groS | Veis_0978 | Veis_2566 | 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 Cpn10; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.811 |
dnaJ | grpE | Veis_0978 | Veis_0980 | 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 [...] | 0.994 |