| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| gapA | nmpC | STM1290 | STM1572 | Glyceraldehyde-3-phosphate dehydrogenase A; Catalyzes the oxidative phosphorylation of glyceraldehyde 3- phosphate (G3P) to 1,3-bisphosphoglycerate (BPG) using the cofactor NAD. The first reaction step involves the formation of a hemiacetal intermediate between G3P and a cysteine residue, and this hemiacetal intermediate is then oxidized to a thioester, with concomitant reduction of NAD to NADH. The reduced NADH is then exchanged with the second NAD, and the thioester is attacked by a nucleophilic inorganic phosphate to produce BPG. | New outer membrane protein; Forms pores that allow passive diffusion of small molecules across the outer membrane; Belongs to the Gram-negative porin family. | 0.415 |
| gapA | ompA | STM1290 | STM1070 | Glyceraldehyde-3-phosphate dehydrogenase A; Catalyzes the oxidative phosphorylation of glyceraldehyde 3- phosphate (G3P) to 1,3-bisphosphoglycerate (BPG) using the cofactor NAD. The first reaction step involves the formation of a hemiacetal intermediate between G3P and a cysteine residue, and this hemiacetal intermediate is then oxidized to a thioester, with concomitant reduction of NAD to NADH. The reduced NADH is then exchanged with the second NAD, and the thioester is attacked by a nucleophilic inorganic phosphate to produce BPG. | Putative membrane component hydrogenase; With TolR probably plays a role in maintaining the position of the peptidoglycan cell wall in the periplasm. Acts as a porin with low permeability that allows slow penetration of small solutes; an internal gate slows down solute passage. | 0.953 |
| gapA | ompC | STM1290 | STM2267 | Glyceraldehyde-3-phosphate dehydrogenase A; Catalyzes the oxidative phosphorylation of glyceraldehyde 3- phosphate (G3P) to 1,3-bisphosphoglycerate (BPG) using the cofactor NAD. The first reaction step involves the formation of a hemiacetal intermediate between G3P and a cysteine residue, and this hemiacetal intermediate is then oxidized to a thioester, with concomitant reduction of NAD to NADH. The reduced NADH is then exchanged with the second NAD, and the thioester is attacked by a nucleophilic inorganic phosphate to produce BPG. | Outer membrane protein 1b (ib;c); Forms pores that allow passive diffusion of small molecules across the outer membrane. | 0.873 |
| hlpA | htrA | STM0225 | STM0209 | Histone-like protein, located in outer membrane; Molecular chaperone that interacts specifically with outer membrane proteins, thus maintaining the solubility of early folding intermediates during passage through the periplasm. | Periplasmic serine protease Do, heat shock protein; DegP acts as a chaperone at low temperatures but switches to a peptidase (heat shock protein) at higher temperatures. It degrades transiently denatured and unfolded proteins which accumulate in the periplasm following heat shock or other stress conditions. DegP is efficient with Val-Xaa and Ile-Xaa peptide bonds, suggesting a preference for beta-branched side chain amino acids. Only unfolded proteins devoid of disulfide bonds appear capable of being cleaved, thereby preventing non-specific proteolysis of folded proteins. Its proteolyt [...] | 0.914 |
| hlpA | lamB | STM0225 | STM4231 | Histone-like protein, located in outer membrane; Molecular chaperone that interacts specifically with outer membrane proteins, thus maintaining the solubility of early folding intermediates during passage through the periplasm. | Phage lambda receptor protein; Involved in the transport of maltose and maltodextrins. Does not act as a receptor for phages; Belongs to the porin LamB (TC 1.B.3) family. | 0.412 |
| hlpA | ompA | STM0225 | STM1070 | Histone-like protein, located in outer membrane; Molecular chaperone that interacts specifically with outer membrane proteins, thus maintaining the solubility of early folding intermediates during passage through the periplasm. | Putative membrane component hydrogenase; With TolR probably plays a role in maintaining the position of the peptidoglycan cell wall in the periplasm. Acts as a porin with low permeability that allows slow penetration of small solutes; an internal gate slows down solute passage. | 0.982 |
| hlpA | ompC | STM0225 | STM2267 | Histone-like protein, located in outer membrane; Molecular chaperone that interacts specifically with outer membrane proteins, thus maintaining the solubility of early folding intermediates during passage through the periplasm. | Outer membrane protein 1b (ib;c); Forms pores that allow passive diffusion of small molecules across the outer membrane. | 0.663 |
| hlpA | ompF | STM0225 | STM0999 | Histone-like protein, located in outer membrane; Molecular chaperone that interacts specifically with outer membrane proteins, thus maintaining the solubility of early folding intermediates during passage through the periplasm. | Outer membrane protein 1a (ia;b;f), porin; Forms pores that allow passive diffusion of small molecules across the outer membrane. It is also a receptor for the bacteriophage T2 (By similarity). | 0.505 |
| hlpA | ompX | STM0225 | STM0833 | Histone-like protein, located in outer membrane; Molecular chaperone that interacts specifically with outer membrane proteins, thus maintaining the solubility of early folding intermediates during passage through the periplasm. | Outer membrane protease, receptor for phage OX2; Similar to E. coli outer membrane protein X (AAC73901.1); Blastp hit to AAC73901.1 (171 aa), 91% identity in aa 1 - 171. | 0.610 |
| hlpA | pal | STM0225 | STM0749 | Histone-like protein, located in outer membrane; Molecular chaperone that interacts specifically with outer membrane proteins, thus maintaining the solubility of early folding intermediates during passage through the periplasm. | Tol protein required for outer membrane integrity; Part of the Tol-Pal system, which plays a role in outer membrane invagination during cell division and is important for maintaining outer membrane integrity. | 0.837 |
| hlpA | yaeT | STM0225 | STM0224 | Histone-like protein, located in outer membrane; Molecular chaperone that interacts specifically with outer membrane proteins, thus maintaining the solubility of early folding intermediates during passage through the periplasm. | Putative outer membrane antigen; Part of the outer membrane protein assembly complex, which is involved in assembly and insertion of beta-barrel proteins into the outer membrane. Constitutes, with BamD, the core component of the assembly machinery. | 0.991 |
| htrA | hlpA | STM0209 | STM0225 | Periplasmic serine protease Do, heat shock protein; DegP acts as a chaperone at low temperatures but switches to a peptidase (heat shock protein) at higher temperatures. It degrades transiently denatured and unfolded proteins which accumulate in the periplasm following heat shock or other stress conditions. DegP is efficient with Val-Xaa and Ile-Xaa peptide bonds, suggesting a preference for beta-branched side chain amino acids. Only unfolded proteins devoid of disulfide bonds appear capable of being cleaved, thereby preventing non-specific proteolysis of folded proteins. Its proteolyt [...] | Histone-like protein, located in outer membrane; Molecular chaperone that interacts specifically with outer membrane proteins, thus maintaining the solubility of early folding intermediates during passage through the periplasm. | 0.914 |
| htrA | lamB | STM0209 | STM4231 | Periplasmic serine protease Do, heat shock protein; DegP acts as a chaperone at low temperatures but switches to a peptidase (heat shock protein) at higher temperatures. It degrades transiently denatured and unfolded proteins which accumulate in the periplasm following heat shock or other stress conditions. DegP is efficient with Val-Xaa and Ile-Xaa peptide bonds, suggesting a preference for beta-branched side chain amino acids. Only unfolded proteins devoid of disulfide bonds appear capable of being cleaved, thereby preventing non-specific proteolysis of folded proteins. Its proteolyt [...] | Phage lambda receptor protein; Involved in the transport of maltose and maltodextrins. Does not act as a receptor for phages; Belongs to the porin LamB (TC 1.B.3) family. | 0.699 |
| htrA | nmpC | STM0209 | STM1572 | Periplasmic serine protease Do, heat shock protein; DegP acts as a chaperone at low temperatures but switches to a peptidase (heat shock protein) at higher temperatures. It degrades transiently denatured and unfolded proteins which accumulate in the periplasm following heat shock or other stress conditions. DegP is efficient with Val-Xaa and Ile-Xaa peptide bonds, suggesting a preference for beta-branched side chain amino acids. Only unfolded proteins devoid of disulfide bonds appear capable of being cleaved, thereby preventing non-specific proteolysis of folded proteins. Its proteolyt [...] | New outer membrane protein; Forms pores that allow passive diffusion of small molecules across the outer membrane; Belongs to the Gram-negative porin family. | 0.433 |
| htrA | ompA | STM0209 | STM1070 | Periplasmic serine protease Do, heat shock protein; DegP acts as a chaperone at low temperatures but switches to a peptidase (heat shock protein) at higher temperatures. It degrades transiently denatured and unfolded proteins which accumulate in the periplasm following heat shock or other stress conditions. DegP is efficient with Val-Xaa and Ile-Xaa peptide bonds, suggesting a preference for beta-branched side chain amino acids. Only unfolded proteins devoid of disulfide bonds appear capable of being cleaved, thereby preventing non-specific proteolysis of folded proteins. Its proteolyt [...] | Putative membrane component hydrogenase; With TolR probably plays a role in maintaining the position of the peptidoglycan cell wall in the periplasm. Acts as a porin with low permeability that allows slow penetration of small solutes; an internal gate slows down solute passage. | 0.981 |
| htrA | ompC | STM0209 | STM2267 | Periplasmic serine protease Do, heat shock protein; DegP acts as a chaperone at low temperatures but switches to a peptidase (heat shock protein) at higher temperatures. It degrades transiently denatured and unfolded proteins which accumulate in the periplasm following heat shock or other stress conditions. DegP is efficient with Val-Xaa and Ile-Xaa peptide bonds, suggesting a preference for beta-branched side chain amino acids. Only unfolded proteins devoid of disulfide bonds appear capable of being cleaved, thereby preventing non-specific proteolysis of folded proteins. Its proteolyt [...] | Outer membrane protein 1b (ib;c); Forms pores that allow passive diffusion of small molecules across the outer membrane. | 0.915 |
| htrA | ompF | STM0209 | STM0999 | Periplasmic serine protease Do, heat shock protein; DegP acts as a chaperone at low temperatures but switches to a peptidase (heat shock protein) at higher temperatures. It degrades transiently denatured and unfolded proteins which accumulate in the periplasm following heat shock or other stress conditions. DegP is efficient with Val-Xaa and Ile-Xaa peptide bonds, suggesting a preference for beta-branched side chain amino acids. Only unfolded proteins devoid of disulfide bonds appear capable of being cleaved, thereby preventing non-specific proteolysis of folded proteins. Its proteolyt [...] | Outer membrane protein 1a (ia;b;f), porin; Forms pores that allow passive diffusion of small molecules across the outer membrane. It is also a receptor for the bacteriophage T2 (By similarity). | 0.781 |
| htrA | pal | STM0209 | STM0749 | Periplasmic serine protease Do, heat shock protein; DegP acts as a chaperone at low temperatures but switches to a peptidase (heat shock protein) at higher temperatures. It degrades transiently denatured and unfolded proteins which accumulate in the periplasm following heat shock or other stress conditions. DegP is efficient with Val-Xaa and Ile-Xaa peptide bonds, suggesting a preference for beta-branched side chain amino acids. Only unfolded proteins devoid of disulfide bonds appear capable of being cleaved, thereby preventing non-specific proteolysis of folded proteins. Its proteolyt [...] | Tol protein required for outer membrane integrity; Part of the Tol-Pal system, which plays a role in outer membrane invagination during cell division and is important for maintaining outer membrane integrity. | 0.615 |
| htrA | yaeT | STM0209 | STM0224 | Periplasmic serine protease Do, heat shock protein; DegP acts as a chaperone at low temperatures but switches to a peptidase (heat shock protein) at higher temperatures. It degrades transiently denatured and unfolded proteins which accumulate in the periplasm following heat shock or other stress conditions. DegP is efficient with Val-Xaa and Ile-Xaa peptide bonds, suggesting a preference for beta-branched side chain amino acids. Only unfolded proteins devoid of disulfide bonds appear capable of being cleaved, thereby preventing non-specific proteolysis of folded proteins. Its proteolyt [...] | Putative outer membrane antigen; Part of the outer membrane protein assembly complex, which is involved in assembly and insertion of beta-barrel proteins into the outer membrane. Constitutes, with BamD, the core component of the assembly machinery. | 0.903 |
| lamB | hlpA | STM4231 | STM0225 | Phage lambda receptor protein; Involved in the transport of maltose and maltodextrins. Does not act as a receptor for phages; Belongs to the porin LamB (TC 1.B.3) family. | Histone-like protein, located in outer membrane; Molecular chaperone that interacts specifically with outer membrane proteins, thus maintaining the solubility of early folding intermediates during passage through the periplasm. | 0.412 |
