node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
dgcZ | ldtC | b1535 | b1113 | Diguanylate cyclase, zinc-sensing; Catalyzes the synthesis of cyclic-di-GMP (c-di-GMP) via the condensation of 2 GTP molecules May act as a zinc sensor that controls, via c-di-GMP, post-translational events . Overexpression leads to a strong repression of swimming; swimming returnes to normal when residues 206-207 are both mutated to Ala. Overexpression also leads to a reduction in flagellar abundance and a 20-fold increase in c-di-GMP levels in vivo. Required for aminoglycoside-mediated induction of biofilm formation, it also plays a lesser role in biofilm production in response to ot [...] | L,d-transpeptidase linking lpp to murein; Responsible, at least in part, for anchoring of the major outer membrane lipoprotein (Lpp, also known as the Braun lipoprotein) to the peptidoglycan via a meso-diaminopimelyl-L-Lys- bond on the terminal residue of Lpp | 0.478 |
dgcZ | spy | b1535 | b1743 | Diguanylate cyclase, zinc-sensing; Catalyzes the synthesis of cyclic-di-GMP (c-di-GMP) via the condensation of 2 GTP molecules May act as a zinc sensor that controls, via c-di-GMP, post-translational events . Overexpression leads to a strong repression of swimming; swimming returnes to normal when residues 206-207 are both mutated to Ala. Overexpression also leads to a reduction in flagellar abundance and a 20-fold increase in c-di-GMP levels in vivo. Required for aminoglycoside-mediated induction of biofilm formation, it also plays a lesser role in biofilm production in response to ot [...] | An ATP-independent periplasmic chaperone, decreases protein aggregation and helps protein refolding. Binds substrate over a large region of its convex inner surface . Substrate protein folds while it is bound to chaperone . Increasing Spy flexibility increases its substrate affinity and overall chaperone activity (shown for 3 different substrates) . Protects proteins in vitro against tannin inactivation; tannins have antimicrobial activity . Overexpression enhances the stability of otherwise unstable periplasmic proteins | 0.420 |
dgcZ | yebE | b1535 | b1846 | Diguanylate cyclase, zinc-sensing; Catalyzes the synthesis of cyclic-di-GMP (c-di-GMP) via the condensation of 2 GTP molecules May act as a zinc sensor that controls, via c-di-GMP, post-translational events . Overexpression leads to a strong repression of swimming; swimming returnes to normal when residues 206-207 are both mutated to Ala. Overexpression also leads to a reduction in flagellar abundance and a 20-fold increase in c-di-GMP levels in vivo. Required for aminoglycoside-mediated induction of biofilm formation, it also plays a lesser role in biofilm production in response to ot [...] | annotation not available | 0.509 |
ldtC | dgcZ | b1113 | b1535 | L,d-transpeptidase linking lpp to murein; Responsible, at least in part, for anchoring of the major outer membrane lipoprotein (Lpp, also known as the Braun lipoprotein) to the peptidoglycan via a meso-diaminopimelyl-L-Lys- bond on the terminal residue of Lpp | Diguanylate cyclase, zinc-sensing; Catalyzes the synthesis of cyclic-di-GMP (c-di-GMP) via the condensation of 2 GTP molecules May act as a zinc sensor that controls, via c-di-GMP, post-translational events . Overexpression leads to a strong repression of swimming; swimming returnes to normal when residues 206-207 are both mutated to Ala. Overexpression also leads to a reduction in flagellar abundance and a 20-fold increase in c-di-GMP levels in vivo. Required for aminoglycoside-mediated induction of biofilm formation, it also plays a lesser role in biofilm production in response to ot [...] | 0.478 |
ldtC | mdtA | b1113 | b2074 | L,d-transpeptidase linking lpp to murein; Responsible, at least in part, for anchoring of the major outer membrane lipoprotein (Lpp, also known as the Braun lipoprotein) to the peptidoglycan via a meso-diaminopimelyl-L-Lys- bond on the terminal residue of Lpp | Multidrug efflux pump membrane fusion protein mdta; The MdtABC tripartite complex confers resistance against novobiocin and deoxycholate. MdtABC requires TolC for its function | 0.594 |
ldtC | spy | b1113 | b1743 | L,d-transpeptidase linking lpp to murein; Responsible, at least in part, for anchoring of the major outer membrane lipoprotein (Lpp, also known as the Braun lipoprotein) to the peptidoglycan via a meso-diaminopimelyl-L-Lys- bond on the terminal residue of Lpp | An ATP-independent periplasmic chaperone, decreases protein aggregation and helps protein refolding. Binds substrate over a large region of its convex inner surface . Substrate protein folds while it is bound to chaperone . Increasing Spy flexibility increases its substrate affinity and overall chaperone activity (shown for 3 different substrates) . Protects proteins in vitro against tannin inactivation; tannins have antimicrobial activity . Overexpression enhances the stability of otherwise unstable periplasmic proteins | 0.847 |
ldtC | yebE | b1113 | b1846 | L,d-transpeptidase linking lpp to murein; Responsible, at least in part, for anchoring of the major outer membrane lipoprotein (Lpp, also known as the Braun lipoprotein) to the peptidoglycan via a meso-diaminopimelyl-L-Lys- bond on the terminal residue of Lpp | annotation not available | 0.762 |
mdtA | ldtC | b2074 | b1113 | Multidrug efflux pump membrane fusion protein mdta; The MdtABC tripartite complex confers resistance against novobiocin and deoxycholate. MdtABC requires TolC for its function | L,d-transpeptidase linking lpp to murein; Responsible, at least in part, for anchoring of the major outer membrane lipoprotein (Lpp, also known as the Braun lipoprotein) to the peptidoglycan via a meso-diaminopimelyl-L-Lys- bond on the terminal residue of Lpp | 0.594 |
mdtA | spy | b2074 | b1743 | Multidrug efflux pump membrane fusion protein mdta; The MdtABC tripartite complex confers resistance against novobiocin and deoxycholate. MdtABC requires TolC for its function | An ATP-independent periplasmic chaperone, decreases protein aggregation and helps protein refolding. Binds substrate over a large region of its convex inner surface . Substrate protein folds while it is bound to chaperone . Increasing Spy flexibility increases its substrate affinity and overall chaperone activity (shown for 3 different substrates) . Protects proteins in vitro against tannin inactivation; tannins have antimicrobial activity . Overexpression enhances the stability of otherwise unstable periplasmic proteins | 0.899 |
mdtA | yebE | b2074 | b1846 | Multidrug efflux pump membrane fusion protein mdta; The MdtABC tripartite complex confers resistance against novobiocin and deoxycholate. MdtABC requires TolC for its function | annotation not available | 0.649 |
ptrB | yebE | b1845 | b1846 | Oligopeptidase b; Cleaves peptide bonds on the C-terminal side of lysyl and argininyl residues | annotation not available | 0.482 |
spy | dgcZ | b1743 | b1535 | An ATP-independent periplasmic chaperone, decreases protein aggregation and helps protein refolding. Binds substrate over a large region of its convex inner surface . Substrate protein folds while it is bound to chaperone . Increasing Spy flexibility increases its substrate affinity and overall chaperone activity (shown for 3 different substrates) . Protects proteins in vitro against tannin inactivation; tannins have antimicrobial activity . Overexpression enhances the stability of otherwise unstable periplasmic proteins | Diguanylate cyclase, zinc-sensing; Catalyzes the synthesis of cyclic-di-GMP (c-di-GMP) via the condensation of 2 GTP molecules May act as a zinc sensor that controls, via c-di-GMP, post-translational events . Overexpression leads to a strong repression of swimming; swimming returnes to normal when residues 206-207 are both mutated to Ala. Overexpression also leads to a reduction in flagellar abundance and a 20-fold increase in c-di-GMP levels in vivo. Required for aminoglycoside-mediated induction of biofilm formation, it also plays a lesser role in biofilm production in response to ot [...] | 0.420 |
spy | ldtC | b1743 | b1113 | An ATP-independent periplasmic chaperone, decreases protein aggregation and helps protein refolding. Binds substrate over a large region of its convex inner surface . Substrate protein folds while it is bound to chaperone . Increasing Spy flexibility increases its substrate affinity and overall chaperone activity (shown for 3 different substrates) . Protects proteins in vitro against tannin inactivation; tannins have antimicrobial activity . Overexpression enhances the stability of otherwise unstable periplasmic proteins | L,d-transpeptidase linking lpp to murein; Responsible, at least in part, for anchoring of the major outer membrane lipoprotein (Lpp, also known as the Braun lipoprotein) to the peptidoglycan via a meso-diaminopimelyl-L-Lys- bond on the terminal residue of Lpp | 0.847 |
spy | mdtA | b1743 | b2074 | An ATP-independent periplasmic chaperone, decreases protein aggregation and helps protein refolding. Binds substrate over a large region of its convex inner surface . Substrate protein folds while it is bound to chaperone . Increasing Spy flexibility increases its substrate affinity and overall chaperone activity (shown for 3 different substrates) . Protects proteins in vitro against tannin inactivation; tannins have antimicrobial activity . Overexpression enhances the stability of otherwise unstable periplasmic proteins | Multidrug efflux pump membrane fusion protein mdta; The MdtABC tripartite complex confers resistance against novobiocin and deoxycholate. MdtABC requires TolC for its function | 0.899 |
spy | yebE | b1743 | b1846 | An ATP-independent periplasmic chaperone, decreases protein aggregation and helps protein refolding. Binds substrate over a large region of its convex inner surface . Substrate protein folds while it is bound to chaperone . Increasing Spy flexibility increases its substrate affinity and overall chaperone activity (shown for 3 different substrates) . Protects proteins in vitro against tannin inactivation; tannins have antimicrobial activity . Overexpression enhances the stability of otherwise unstable periplasmic proteins | annotation not available | 0.815 |
spy | yncJ | b1743 | b1436 | An ATP-independent periplasmic chaperone, decreases protein aggregation and helps protein refolding. Binds substrate over a large region of its convex inner surface . Substrate protein folds while it is bound to chaperone . Increasing Spy flexibility increases its substrate affinity and overall chaperone activity (shown for 3 different substrates) . Protects proteins in vitro against tannin inactivation; tannins have antimicrobial activity . Overexpression enhances the stability of otherwise unstable periplasmic proteins | annotation not available | 0.455 |
trxA | yebE | b3781 | b1846 | Thioredoxin 1; Participates in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyzes dithiol-disulfide exchange reactions | annotation not available | 0.637 |
ybgS | yebE | b0753 | b1846 | Putative periplasmic protein; Uncharacterized protein YbgS; Putative homeobox protein | annotation not available | 0.494 |
yebE | dgcZ | b1846 | b1535 | annotation not available | Diguanylate cyclase, zinc-sensing; Catalyzes the synthesis of cyclic-di-GMP (c-di-GMP) via the condensation of 2 GTP molecules May act as a zinc sensor that controls, via c-di-GMP, post-translational events . Overexpression leads to a strong repression of swimming; swimming returnes to normal when residues 206-207 are both mutated to Ala. Overexpression also leads to a reduction in flagellar abundance and a 20-fold increase in c-di-GMP levels in vivo. Required for aminoglycoside-mediated induction of biofilm formation, it also plays a lesser role in biofilm production in response to ot [...] | 0.509 |
yebE | ldtC | b1846 | b1113 | annotation not available | L,d-transpeptidase linking lpp to murein; Responsible, at least in part, for anchoring of the major outer membrane lipoprotein (Lpp, also known as the Braun lipoprotein) to the peptidoglycan via a meso-diaminopimelyl-L-Lys- bond on the terminal residue of Lpp | 0.762 |