node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
ACS17510.1 | ACS17511.1 | Vapar_0857 | Vapar_0858 | PFAM: protein of unknown function DUF88; KEGG: mpt:Mpe_A0449 hypothetical protein. | KEGG: aav:Aave_4317 putative transmembrane protein. | 0.808 |
ACS17510.1 | htpX | Vapar_0857 | Vapar_0859 | PFAM: protein of unknown function DUF88; KEGG: mpt:Mpe_A0449 hypothetical protein. | PFAM: peptidase M48 Ste24p; HtpX domain protein; KEGG: pna:Pnap_3448 heat shock protein HtpX; Belongs to the peptidase M48B family. | 0.543 |
ACS17510.1 | pyrC | Vapar_0857 | Vapar_0854 | PFAM: protein of unknown function DUF88; KEGG: mpt:Mpe_A0449 hypothetical protein. | Dihydroorotase, homodimeric type; Catalyzes the reversible cyclization of carbamoyl aspartate to dihydroorotate. | 0.453 |
ACS17511.1 | ACS17510.1 | Vapar_0858 | Vapar_0857 | KEGG: aav:Aave_4317 putative transmembrane protein. | PFAM: protein of unknown function DUF88; KEGG: mpt:Mpe_A0449 hypothetical protein. | 0.808 |
ACS17511.1 | htpX | Vapar_0858 | Vapar_0859 | KEGG: aav:Aave_4317 putative transmembrane protein. | PFAM: peptidase M48 Ste24p; HtpX domain protein; KEGG: pna:Pnap_3448 heat shock protein HtpX; Belongs to the peptidase M48B family. | 0.657 |
ACS17511.1 | pyrC | Vapar_0858 | Vapar_0854 | KEGG: aav:Aave_4317 putative transmembrane protein. | Dihydroorotase, homodimeric type; Catalyzes the reversible cyclization of carbamoyl aspartate to dihydroorotate. | 0.615 |
ACS18452.1 | ftsH | Vapar_1802 | Vapar_2624 | PFAM: protein of unknown function UPF0005; KEGG: aav:Aave_3316 hypothetical protein; Belongs to the BI1 family. | ATP-dependent metalloprotease FtsH; 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. | 0.450 |
ACS18452.1 | htpX | Vapar_1802 | Vapar_0859 | PFAM: protein of unknown function UPF0005; KEGG: aav:Aave_3316 hypothetical protein; Belongs to the BI1 family. | PFAM: peptidase M48 Ste24p; HtpX domain protein; KEGG: pna:Pnap_3448 heat shock protein HtpX; Belongs to the peptidase M48B family. | 0.551 |
ACS21696.1 | dnaJ | Vapar_5094 | Vapar_1711 | TIGRFAM: thioredoxin; PFAM: Thioredoxin domain; KEGG: dia:Dtpsy_3279 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 [...] | 0.860 |
ACS21696.1 | ftsH | Vapar_5094 | Vapar_2624 | TIGRFAM: thioredoxin; PFAM: Thioredoxin domain; KEGG: dia:Dtpsy_3279 thioredoxin. | ATP-dependent metalloprotease FtsH; 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. | 0.404 |
ACS21696.1 | groS | Vapar_5094 | Vapar_1119 | TIGRFAM: thioredoxin; PFAM: Thioredoxin domain; KEGG: dia:Dtpsy_3279 thioredoxin. | Chaperonin Cpn10; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.651 |
ACS21696.1 | grpE | Vapar_5094 | Vapar_1713 | TIGRFAM: thioredoxin; PFAM: Thioredoxin domain; KEGG: dia:Dtpsy_3279 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 [...] | 0.909 |
ACS21696.1 | htpX | Vapar_5094 | Vapar_0859 | TIGRFAM: thioredoxin; PFAM: Thioredoxin domain; KEGG: dia:Dtpsy_3279 thioredoxin. | PFAM: peptidase M48 Ste24p; HtpX domain protein; KEGG: pna:Pnap_3448 heat shock protein HtpX; Belongs to the peptidase M48B family. | 0.645 |
ACS21696.1 | lon | Vapar_5094 | Vapar_2513 | TIGRFAM: thioredoxin; PFAM: Thioredoxin domain; KEGG: dia:Dtpsy_3279 thioredoxin. | ATP-dependent protease La; 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. | 0.699 |
dnaJ | ACS21696.1 | Vapar_1711 | Vapar_5094 | 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: dia:Dtpsy_3279 thioredoxin. | 0.860 |
dnaJ | ftsH | Vapar_1711 | Vapar_2624 | 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 [...] | ATP-dependent metalloprotease FtsH; 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. | 0.799 |
dnaJ | groS | Vapar_1711 | Vapar_1119 | 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. | 0.926 |
dnaJ | grpE | Vapar_1711 | Vapar_1713 | 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 [...] | 0.993 |
dnaJ | htpX | Vapar_1711 | Vapar_0859 | 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: peptidase M48 Ste24p; HtpX domain protein; KEGG: pna:Pnap_3448 heat shock protein HtpX; Belongs to the peptidase M48B family. | 0.537 |
dnaJ | lon | Vapar_1711 | Vapar_2513 | 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 [...] | ATP-dependent protease La; 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. | 0.905 |