node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
Pmen_2376 | ftsH | Pmen_2376 | Pmen_3615 | PFAM: protein of unknown function UPF0005; Belongs to the BI1 family. | 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. | 0.442 |
Pmen_2376 | htpX | Pmen_2376 | Pmen_2524 | PFAM: protein of unknown function UPF0005; Belongs to the BI1 family. | Heat shock protein, Metallo peptidase, MEROPS family M48B; PFAM: peptidase M48, Ste24p; HtpX domain protein; Belongs to the peptidase M48B family. | 0.651 |
Pmen_2522 | Pmen_2523 | Pmen_2522 | Pmen_2523 | PFAM: aminotransferase, class I and II. | Hypothetical protein. | 0.800 |
Pmen_2522 | htpX | Pmen_2522 | Pmen_2524 | PFAM: aminotransferase, class I and II. | Heat shock protein, Metallo peptidase, MEROPS family M48B; PFAM: peptidase M48, Ste24p; HtpX domain protein; Belongs to the peptidase M48B family. | 0.627 |
Pmen_2523 | Pmen_2522 | Pmen_2523 | Pmen_2522 | Hypothetical protein. | PFAM: aminotransferase, class I and II. | 0.800 |
Pmen_2523 | htpX | Pmen_2523 | Pmen_2524 | Hypothetical protein. | Heat shock protein, Metallo peptidase, MEROPS family M48B; PFAM: peptidase M48, Ste24p; HtpX domain protein; Belongs to the peptidase M48B family. | 0.595 |
Pmen_3375 | htpX | Pmen_3375 | Pmen_2524 | PFAM: protein of unknown function DUF533. | Heat shock protein, Metallo peptidase, MEROPS family M48B; PFAM: peptidase M48, Ste24p; HtpX domain protein; Belongs to the peptidase M48B family. | 0.599 |
Pmen_3861 | dnaJ | Pmen_3861 | Pmen_3623 | TIGRFAM: thioredoxin; PFAM: Thioredoxin domain. | 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 [...] | 0.794 |
Pmen_3861 | groS | Pmen_3861 | Pmen_3687 | TIGRFAM: thioredoxin; PFAM: Thioredoxin domain. | Chaperonin Cpn10; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.600 |
Pmen_3861 | grpE | Pmen_3861 | Pmen_3625 | TIGRFAM: thioredoxin; PFAM: Thioredoxin domain. | 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 [...] | 0.891 |
Pmen_3861 | htpX | Pmen_3861 | Pmen_2524 | TIGRFAM: thioredoxin; PFAM: Thioredoxin domain. | Heat shock protein, Metallo peptidase, MEROPS family M48B; PFAM: peptidase M48, Ste24p; HtpX domain protein; Belongs to the peptidase M48B family. | 0.623 |
Pmen_4154 | htpX | Pmen_4154 | Pmen_2524 | GTPase (dynamin-related)-like protein. | Heat shock protein, Metallo peptidase, MEROPS family M48B; PFAM: peptidase M48, Ste24p; HtpX domain protein; Belongs to the peptidase M48B family. | 0.626 |
dnaJ | Pmen_3861 | Pmen_3623 | Pmen_3861 | 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. | 0.794 |
dnaJ | ftsH | Pmen_3623 | Pmen_3615 | 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. | 0.700 |
dnaJ | groS | Pmen_3623 | Pmen_3687 | 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. | 0.874 |
dnaJ | grpE | Pmen_3623 | Pmen_3625 | 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 [...] | 0.989 |
dnaJ | htpX | Pmen_3623 | Pmen_2524 | 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, Metallo peptidase, MEROPS family M48B; PFAM: peptidase M48, Ste24p; HtpX domain protein; Belongs to the peptidase M48B family. | 0.544 |
ftsH | Pmen_2376 | Pmen_3615 | Pmen_2376 | 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. | PFAM: protein of unknown function UPF0005; Belongs to the BI1 family. | 0.442 |
ftsH | dnaJ | Pmen_3615 | Pmen_3623 | 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. | 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 [...] | 0.700 |
ftsH | grpE | Pmen_3615 | Pmen_3625 | 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. | 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 [...] | 0.682 |