| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| LBAT_0002 | LBAT_1323 | LBAT_0002 | LBAT_1323 | DNA polymerase III beta subunit; Confers DNA tethering and processivity to DNA polymerases and other proteins. Acts as a clamp, forming a ring around DNA (a reaction catalyzed by the clamp-loading complex) which diffuses in an ATP- independent manner freely and bidirectionally along dsDNA. Initially characterized for its ability to contact the catalytic subunit of DNA polymerase III (Pol III), a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria; Pol III exhibits 3'-5' exonuclease proofreading activity. The beta chain is required for initiation of [...] | Conserved hypothetical protein. | 0.642 |
| LBAT_0002 | recA | LBAT_0002 | LBAT_1172 | DNA polymerase III beta subunit; Confers DNA tethering and processivity to DNA polymerases and other proteins. Acts as a clamp, forming a ring around DNA (a reaction catalyzed by the clamp-loading complex) which diffuses in an ATP- independent manner freely and bidirectionally along dsDNA. Initially characterized for its ability to contact the catalytic subunit of DNA polymerase III (Pol III), a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria; Pol III exhibits 3'-5' exonuclease proofreading activity. The beta chain is required for initiation of [...] | Recombinase A; Can catalyze the hydrolysis of ATP in the presence of single- stranded DNA, the ATP-dependent uptake of single-stranded DNA by duplex DNA, and the ATP-dependent hybridization of homologous single-stranded DNAs. It interacts with LexA causing its activation and leading to its autocatalytic cleavage; Belongs to the RecA family. | 0.911 |
| LBAT_0534 | LBAT_1323 | LBAT_0534 | LBAT_1323 | Thioredoxin. | Conserved hypothetical protein. | 0.703 |
| LBAT_0534 | dnaJ | LBAT_0534 | LBAT_0714 | 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 [...] | 0.787 |
| LBAT_0534 | dnaK | LBAT_0534 | LBAT_0713 | Thioredoxin. | Molecular chaperone DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.810 |
| LBAT_0534 | pcp | LBAT_0534 | LBAT_0123 | Thioredoxin. | Pyrrolidone carboxyl peptidase; Removes 5-oxoproline from various penultimate amino acid residues except L-proline; Belongs to the peptidase C15 family. | 0.580 |
| LBAT_1322 | LBAT_1323 | LBAT_1322 | LBAT_1323 | Transcriptional regulator. | Conserved hypothetical protein. | 0.554 |
| LBAT_1323 | LBAT_0002 | LBAT_1323 | LBAT_0002 | Conserved hypothetical protein. | DNA polymerase III beta subunit; Confers DNA tethering and processivity to DNA polymerases and other proteins. Acts as a clamp, forming a ring around DNA (a reaction catalyzed by the clamp-loading complex) which diffuses in an ATP- independent manner freely and bidirectionally along dsDNA. Initially characterized for its ability to contact the catalytic subunit of DNA polymerase III (Pol III), a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria; Pol III exhibits 3'-5' exonuclease proofreading activity. The beta chain is required for initiation of [...] | 0.642 |
| LBAT_1323 | LBAT_0534 | LBAT_1323 | LBAT_0534 | Conserved hypothetical protein. | Thioredoxin. | 0.703 |
| LBAT_1323 | LBAT_1322 | LBAT_1323 | LBAT_1322 | Conserved hypothetical protein. | Transcriptional regulator. | 0.554 |
| LBAT_1323 | dnaJ | LBAT_1323 | LBAT_0714 | Conserved hypothetical 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 [...] | 0.793 |
| LBAT_1323 | dnaK | LBAT_1323 | LBAT_0713 | Conserved hypothetical protein. | Molecular chaperone DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.755 |
| LBAT_1323 | glpK | LBAT_1323 | LBAT_0779 | Conserved hypothetical protein. | Glycerol kinase; Key enzyme in the regulation of glycerol uptake and metabolism. Catalyzes the phosphorylation of glycerol to yield sn- glycerol 3-phosphate; Belongs to the FGGY kinase family. | 0.629 |
| LBAT_1323 | glpK-2 | LBAT_1323 | LBAT_1524 | Conserved hypothetical protein. | Glycerol kinase; Key enzyme in the regulation of glycerol uptake and metabolism. Catalyzes the phosphorylation of glycerol to yield sn- glycerol 3-phosphate. | 0.629 |
| LBAT_1323 | pcp | LBAT_1323 | LBAT_0123 | Conserved hypothetical protein. | Pyrrolidone carboxyl peptidase; Removes 5-oxoproline from various penultimate amino acid residues except L-proline; Belongs to the peptidase C15 family. | 0.773 |
| LBAT_1323 | recA | LBAT_1323 | LBAT_1172 | Conserved hypothetical protein. | Recombinase A; Can catalyze the hydrolysis of ATP in the presence of single- stranded DNA, the ATP-dependent uptake of single-stranded DNA by duplex DNA, and the ATP-dependent hybridization of homologous single-stranded DNAs. It interacts with LexA causing its activation and leading to its autocatalytic cleavage; Belongs to the RecA family. | 0.692 |
| LBAT_1323 | rplC | LBAT_1323 | LBAT_0355 | Conserved hypothetical protein. | 50S ribosomal protein L3; One of the primary rRNA binding proteins, it binds directly near the 3'-end of the 23S rRNA, where it nucleates assembly of the 50S subunit; Belongs to the universal ribosomal protein uL3 family. | 0.567 |
| dnaJ | LBAT_0534 | LBAT_0714 | LBAT_0534 | 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 [...] | Thioredoxin. | 0.787 |
| dnaJ | LBAT_1323 | LBAT_0714 | LBAT_1323 | 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 [...] | Conserved hypothetical protein. | 0.793 |
| dnaJ | dnaK | LBAT_0714 | LBAT_0713 | 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 [...] | Molecular chaperone DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.999 |