| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| alaS | mspH | MARTH_orf202 | MARTH_orf653 | alanyl-tRNA synthetase; Catalyzes the attachment of alanine to tRNA(Ala) in a two- step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain. | Massive surface protein MspH. | 0.957 |
| dnaJ | mspH | MARTH_orf297 | MARTH_orf653 | Heat shock 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, [...] | Massive surface protein MspH. | 0.919 |
| dnaJ | mspK | MARTH_orf297 | MARTH_orf727 | Heat shock 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, [...] | Massive surface protein MspK. | 0.842 |
| dnaJ | rplE | MARTH_orf297 | MARTH_orf430 | Heat shock 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, [...] | Ribosomal protein L5; This is 1 of the proteins that binds and probably mediates the attachment of the 5S RNA into the large ribosomal subunit, where it forms part of the central protuberance. In the 70S ribosome it contacts protein S13 of the 30S subunit (bridge B1b), connecting the 2 subunits; this bridge is implicated in subunit movement. Contacts the P site tRNA; the 5S rRNA and some of its associated proteins might help stabilize positioning of ribosome-bound tRNAs. | 0.751 |
| dnaJ | rplF | MARTH_orf297 | MARTH_orf426 | Heat shock 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, [...] | Ribosomal protein L6; This protein binds to the 23S rRNA, and is important in its secondary structure. It is located near the subunit interface in the base of the L7/L12 stalk, and near the tRNA binding site of the peptidyltransferase center; Belongs to the universal ribosomal protein uL6 family. | 0.790 |
| dnaJ | rplJ | MARTH_orf297 | MARTH_orf208 | Heat shock 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, [...] | Ribosomal protein L10; Forms part of the ribosomal stalk, playing a central role in the interaction of the ribosome with GTP-bound translation factors. Belongs to the universal ribosomal protein uL10 family. | 0.434 |
| dnaJ | rplW | MARTH_orf297 | MARTH_orf441 | Heat shock 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, [...] | Ribosomal protein L23; One of the early assembly proteins it binds 23S rRNA. One of the proteins that surrounds the polypeptide exit tunnel on the outside of the ribosome. Forms the main docking site for trigger factor binding to the ribosome; Belongs to the universal ribosomal protein uL23 family. | 0.743 |
| dnaJ | ylqF | MARTH_orf297 | MARTH_orf365 | Heat shock 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, [...] | GTPase protein YlqF; Required for a late step of 50S ribosomal subunit assembly. Has GTPase activity; Belongs to the TRAFAC class YlqF/YawG GTPase family. MTG1 subfamily. | 0.786 |
| mspH | alaS | MARTH_orf653 | MARTH_orf202 | Massive surface protein MspH. | alanyl-tRNA synthetase; Catalyzes the attachment of alanine to tRNA(Ala) in a two- step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain. | 0.957 |
| mspH | dnaJ | MARTH_orf653 | MARTH_orf297 | Massive surface protein MspH. | Heat shock 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, [...] | 0.919 |
| mspH | mspK | MARTH_orf653 | MARTH_orf727 | Massive surface protein MspH. | Massive surface protein MspK. | 0.963 |
| mspH | pgm | MARTH_orf653 | MARTH_orf597 | Massive surface protein MspH. | Phosphoglyceromutase; Catalyzes the interconversion of 2-phosphoglycerate and 3- phosphoglycerate. | 0.954 |
| mspH | rplA | MARTH_orf653 | MARTH_orf143 | Massive surface protein MspH. | Ribosomal protein L1; Binds directly to 23S rRNA. The L1 stalk is quite mobile in the ribosome, and is involved in E site tRNA release. | 0.936 |
| mspH | rplE | MARTH_orf653 | MARTH_orf430 | Massive surface protein MspH. | Ribosomal protein L5; This is 1 of the proteins that binds and probably mediates the attachment of the 5S RNA into the large ribosomal subunit, where it forms part of the central protuberance. In the 70S ribosome it contacts protein S13 of the 30S subunit (bridge B1b), connecting the 2 subunits; this bridge is implicated in subunit movement. Contacts the P site tRNA; the 5S rRNA and some of its associated proteins might help stabilize positioning of ribosome-bound tRNAs. | 0.930 |
| mspH | rplF | MARTH_orf653 | MARTH_orf426 | Massive surface protein MspH. | Ribosomal protein L6; This protein binds to the 23S rRNA, and is important in its secondary structure. It is located near the subunit interface in the base of the L7/L12 stalk, and near the tRNA binding site of the peptidyltransferase center; Belongs to the universal ribosomal protein uL6 family. | 0.930 |
| mspH | rplJ | MARTH_orf653 | MARTH_orf208 | Massive surface protein MspH. | Ribosomal protein L10; Forms part of the ribosomal stalk, playing a central role in the interaction of the ribosome with GTP-bound translation factors. Belongs to the universal ribosomal protein uL10 family. | 0.918 |
| mspH | rplW | MARTH_orf653 | MARTH_orf441 | Massive surface protein MspH. | Ribosomal protein L23; One of the early assembly proteins it binds 23S rRNA. One of the proteins that surrounds the polypeptide exit tunnel on the outside of the ribosome. Forms the main docking site for trigger factor binding to the ribosome; Belongs to the universal ribosomal protein uL23 family. | 0.927 |
| mspH | ylqF | MARTH_orf653 | MARTH_orf365 | Massive surface protein MspH. | GTPase protein YlqF; Required for a late step of 50S ribosomal subunit assembly. Has GTPase activity; Belongs to the TRAFAC class YlqF/YawG GTPase family. MTG1 subfamily. | 0.948 |
| mspK | dnaJ | MARTH_orf727 | MARTH_orf297 | Massive surface protein MspK. | Heat shock 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, [...] | 0.842 |
| mspK | mspH | MARTH_orf727 | MARTH_orf653 | Massive surface protein MspK. | Massive surface protein MspH. | 0.963 |