| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| STM1328 | lpxO | STM1328 | STM4286 | Putative outer membrane protein. | Putative dioxygenase for synthesis of lipid; Putative dioxygenase; LpxO (gi|9454389). | 0.900 |
| STM1328 | msbB | STM1328 | STM1889 | Putative outer membrane protein. | Myristoyl transferase in lipid A biosynthesis; Catalyzes the transfer of myristate from myristoyl-acyl carrier protein (ACP) to Kdo(2)-(lauroyl)-lipid IV(A) to form Kdo(2)- lipid A. | 0.921 |
| STM1328 | pagP | STM1328 | STM0628 | Putative outer membrane protein. | PhoPQ-activated gene; Transfers a palmitate residue from the sn-1 position of a phospholipid to the N-linked hydroxymyristate on the proximal unit of lipid A or its precursors. Required for resistance to cationic antimicrobial peptides (CAMPs). Modifications of lipid A with a palmitate chain allow to evade host immune defenses by resisting antimicrobial peptides and attenuating the inflammatory response to infection triggered by lipopolysaccharide through the Toll-like receptor 4 (TLR4) signal transduction pathway. | 0.972 |
| STM1328 | phoP | STM1328 | STM1231 | Putative outer membrane protein. | Response regulator in two-component regulatory system with PhoQ; Member of the two-component regulatory system PhoP/PhoQ which regulates the expression of genes involved in virulence, adaptation to acidic and low Mg(2+) environments and resistance to host defense antimicrobial peptides. Essential for intramacrophage survival of S.typhimurium. In low periplasmic Mg(2+), PhoQ phosphorylates PhoP, resulting in the expression of PhoP-activated genes (PAG) and repression of PhoP-repressed genes (PRG). In high periplasmic Mg(2+), PhoQ dephosphorylates phospho-PhoP, resulting in the repressio [...] | 0.480 |
| STM1328 | pqaB | STM1328 | STM2301 | Putative outer membrane protein. | Putative melittin resistance protein; Catalyzes the transfer of the L-Ara4N moiety of the glycolipid undecaprenyl phosphate-alpha-L-Ara4N to lipid A. The modified arabinose is attached to lipid A and is required for resistance to polymyxin and cationic antimicrobial peptides. Belongs to the glycosyltransferase 83 family. | 0.900 |
| STM1328 | yeiU | STM1328 | STM2213 | Putative outer membrane protein. | Putative permease; Involved in the modification of the lipid A domain of lipopolysaccharides (LPS). Transfers a phosphate group from undecaprenyl pyrophosphate (C55-PP) to lipid A to form lipid A 1- diphosphate. Contributes to the recycling of undecaprenyl phosphate (C55-P); Belongs to the LpxT phosphotransferase family. | 0.916 |
| STM1328 | yhjW | STM1328 | STM3635 | Putative outer membrane protein. | Putative membrane-associated metal-dependent hydrolase; Catalyzes the addition of a phosphoethanolamine (pEtN) moiety to the outer 3-deoxy-D-manno-octulosonic acid (Kdo) residue of a Kdo(2)-lipid A. Phosphatidylethanolamines with one unsaturated acyl group functions as pEtN donors and the reaction releases diacylglycerol. | 0.900 |
| STM1328 | yjdB | STM1328 | STM4293 | Putative outer membrane protein. | Putative integral membrane protein; Catalyzes the addition of a phosphoethanolamine moiety to the lipid A. The phosphoethanolamine modification is required for resistance to polymyxin; Belongs to the phosphoethanolamine transferase family. EptA subfamily. | 0.900 |
| basS | lpxO | STM4291 | STM4286 | Sensory kinase in two-component regulatory system with BasR; Member of the two-component regulatory system BasS/BasR. Autophosphorylates and activates BasR by phosphorylation. Plays a role in the adaptation of the organism to the host environment, in particular to neutrophils, and therefore it plays a role in virulence as well. | Putative dioxygenase for synthesis of lipid; Putative dioxygenase; LpxO (gi|9454389). | 0.718 |
| basS | msbB | STM4291 | STM1889 | Sensory kinase in two-component regulatory system with BasR; Member of the two-component regulatory system BasS/BasR. Autophosphorylates and activates BasR by phosphorylation. Plays a role in the adaptation of the organism to the host environment, in particular to neutrophils, and therefore it plays a role in virulence as well. | Myristoyl transferase in lipid A biosynthesis; Catalyzes the transfer of myristate from myristoyl-acyl carrier protein (ACP) to Kdo(2)-(lauroyl)-lipid IV(A) to form Kdo(2)- lipid A. | 0.616 |
| basS | pagP | STM4291 | STM0628 | Sensory kinase in two-component regulatory system with BasR; Member of the two-component regulatory system BasS/BasR. Autophosphorylates and activates BasR by phosphorylation. Plays a role in the adaptation of the organism to the host environment, in particular to neutrophils, and therefore it plays a role in virulence as well. | PhoPQ-activated gene; Transfers a palmitate residue from the sn-1 position of a phospholipid to the N-linked hydroxymyristate on the proximal unit of lipid A or its precursors. Required for resistance to cationic antimicrobial peptides (CAMPs). Modifications of lipid A with a palmitate chain allow to evade host immune defenses by resisting antimicrobial peptides and attenuating the inflammatory response to infection triggered by lipopolysaccharide through the Toll-like receptor 4 (TLR4) signal transduction pathway. | 0.858 |
| basS | phoP | STM4291 | STM1231 | Sensory kinase in two-component regulatory system with BasR; Member of the two-component regulatory system BasS/BasR. Autophosphorylates and activates BasR by phosphorylation. Plays a role in the adaptation of the organism to the host environment, in particular to neutrophils, and therefore it plays a role in virulence as well. | Response regulator in two-component regulatory system with PhoQ; Member of the two-component regulatory system PhoP/PhoQ which regulates the expression of genes involved in virulence, adaptation to acidic and low Mg(2+) environments and resistance to host defense antimicrobial peptides. Essential for intramacrophage survival of S.typhimurium. In low periplasmic Mg(2+), PhoQ phosphorylates PhoP, resulting in the expression of PhoP-activated genes (PAG) and repression of PhoP-repressed genes (PRG). In high periplasmic Mg(2+), PhoQ dephosphorylates phospho-PhoP, resulting in the repressio [...] | 0.989 |
| basS | pqaB | STM4291 | STM2301 | Sensory kinase in two-component regulatory system with BasR; Member of the two-component regulatory system BasS/BasR. Autophosphorylates and activates BasR by phosphorylation. Plays a role in the adaptation of the organism to the host environment, in particular to neutrophils, and therefore it plays a role in virulence as well. | Putative melittin resistance protein; Catalyzes the transfer of the L-Ara4N moiety of the glycolipid undecaprenyl phosphate-alpha-L-Ara4N to lipid A. The modified arabinose is attached to lipid A and is required for resistance to polymyxin and cationic antimicrobial peptides. Belongs to the glycosyltransferase 83 family. | 0.900 |
| basS | yeiU | STM4291 | STM2213 | Sensory kinase in two-component regulatory system with BasR; Member of the two-component regulatory system BasS/BasR. Autophosphorylates and activates BasR by phosphorylation. Plays a role in the adaptation of the organism to the host environment, in particular to neutrophils, and therefore it plays a role in virulence as well. | Putative permease; Involved in the modification of the lipid A domain of lipopolysaccharides (LPS). Transfers a phosphate group from undecaprenyl pyrophosphate (C55-PP) to lipid A to form lipid A 1- diphosphate. Contributes to the recycling of undecaprenyl phosphate (C55-P); Belongs to the LpxT phosphotransferase family. | 0.860 |
| basS | yhjW | STM4291 | STM3635 | Sensory kinase in two-component regulatory system with BasR; Member of the two-component regulatory system BasS/BasR. Autophosphorylates and activates BasR by phosphorylation. Plays a role in the adaptation of the organism to the host environment, in particular to neutrophils, and therefore it plays a role in virulence as well. | Putative membrane-associated metal-dependent hydrolase; Catalyzes the addition of a phosphoethanolamine (pEtN) moiety to the outer 3-deoxy-D-manno-octulosonic acid (Kdo) residue of a Kdo(2)-lipid A. Phosphatidylethanolamines with one unsaturated acyl group functions as pEtN donors and the reaction releases diacylglycerol. | 0.857 |
| basS | yjdB | STM4291 | STM4293 | Sensory kinase in two-component regulatory system with BasR; Member of the two-component regulatory system BasS/BasR. Autophosphorylates and activates BasR by phosphorylation. Plays a role in the adaptation of the organism to the host environment, in particular to neutrophils, and therefore it plays a role in virulence as well. | Putative integral membrane protein; Catalyzes the addition of a phosphoethanolamine moiety to the lipid A. The phosphoethanolamine modification is required for resistance to polymyxin; Belongs to the phosphoethanolamine transferase family. EptA subfamily. | 0.997 |
| lpxO | STM1328 | STM4286 | STM1328 | Putative dioxygenase for synthesis of lipid; Putative dioxygenase; LpxO (gi|9454389). | Putative outer membrane protein. | 0.900 |
| lpxO | basS | STM4286 | STM4291 | Putative dioxygenase for synthesis of lipid; Putative dioxygenase; LpxO (gi|9454389). | Sensory kinase in two-component regulatory system with BasR; Member of the two-component regulatory system BasS/BasR. Autophosphorylates and activates BasR by phosphorylation. Plays a role in the adaptation of the organism to the host environment, in particular to neutrophils, and therefore it plays a role in virulence as well. | 0.718 |
| lpxO | msbB | STM4286 | STM1889 | Putative dioxygenase for synthesis of lipid; Putative dioxygenase; LpxO (gi|9454389). | Myristoyl transferase in lipid A biosynthesis; Catalyzes the transfer of myristate from myristoyl-acyl carrier protein (ACP) to Kdo(2)-(lauroyl)-lipid IV(A) to form Kdo(2)- lipid A. | 0.978 |
| lpxO | pagP | STM4286 | STM0628 | Putative dioxygenase for synthesis of lipid; Putative dioxygenase; LpxO (gi|9454389). | PhoPQ-activated gene; Transfers a palmitate residue from the sn-1 position of a phospholipid to the N-linked hydroxymyristate on the proximal unit of lipid A or its precursors. Required for resistance to cationic antimicrobial peptides (CAMPs). Modifications of lipid A with a palmitate chain allow to evade host immune defenses by resisting antimicrobial peptides and attenuating the inflammatory response to infection triggered by lipopolysaccharide through the Toll-like receptor 4 (TLR4) signal transduction pathway. | 0.994 |
