| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| btuB | lamB | STM4130 | STM4231 | Outer membrane receptor for transport of vitamin B12, E colicins, and bacteriophage BF23; Involved in the active translocation of vitamin B12 (cyanocobalamin) across the outer membrane to the periplasmic space. It derives its energy for transport by interacting with the trans- periplasmic membrane protein TonB; Belongs to the TonB-dependent receptor family. BtuB (TC 1.B.14.3.1) subfamily. | 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. | 0.876 |
| btuB | ompA | STM4130 | STM1070 | Outer membrane receptor for transport of vitamin B12, E colicins, and bacteriophage BF23; Involved in the active translocation of vitamin B12 (cyanocobalamin) across the outer membrane to the periplasmic space. It derives its energy for transport by interacting with the trans- periplasmic membrane protein TonB; Belongs to the TonB-dependent receptor family. BtuB (TC 1.B.14.3.1) subfamily. | 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. | 0.825 |
| btuB | ompC | STM4130 | STM2267 | Outer membrane receptor for transport of vitamin B12, E colicins, and bacteriophage BF23; Involved in the active translocation of vitamin B12 (cyanocobalamin) across the outer membrane to the periplasmic space. It derives its energy for transport by interacting with the trans- periplasmic membrane protein TonB; Belongs to the TonB-dependent receptor family. BtuB (TC 1.B.14.3.1) subfamily. | Outer membrane protein 1b (ib;c); Forms pores that allow passive diffusion of small molecules across the outer membrane. | 0.921 |
| btuB | ompF | STM4130 | STM0999 | Outer membrane receptor for transport of vitamin B12, E colicins, and bacteriophage BF23; Involved in the active translocation of vitamin B12 (cyanocobalamin) across the outer membrane to the periplasmic space. It derives its energy for transport by interacting with the trans- periplasmic membrane protein TonB; Belongs to the TonB-dependent receptor family. BtuB (TC 1.B.14.3.1) subfamily. | 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). | 0.914 |
| btuB | tolC | STM4130 | STM3186 | Outer membrane receptor for transport of vitamin B12, E colicins, and bacteriophage BF23; Involved in the active translocation of vitamin B12 (cyanocobalamin) across the outer membrane to the periplasmic space. It derives its energy for transport by interacting with the trans- periplasmic membrane protein TonB; Belongs to the TonB-dependent receptor family. BtuB (TC 1.B.14.3.1) subfamily. | Outer membrane channel; Specific tolerance to colicin E1; segregation of daughter chromosomes; role in organic solvent tolerance; similar to E. coli outer membrane channel; specific tolerance to colicin E1; segregation of daughter chromosomes (AAC76071.1); Blastp hit to AAC76071.1 (495 aa), 89% identity in aa 1 - 495. | 0.778 |
| btuB | tsx | STM4130 | STM0413 | Outer membrane receptor for transport of vitamin B12, E colicins, and bacteriophage BF23; Involved in the active translocation of vitamin B12 (cyanocobalamin) across the outer membrane to the periplasmic space. It derives its energy for transport by interacting with the trans- periplasmic membrane protein TonB; Belongs to the TonB-dependent receptor family. BtuB (TC 1.B.14.3.1) subfamily. | Nucleoside channel; Functions as substrate-specific channel for nucleosides and deoxynucleosides. Functions also in albicidin uptake and as receptor for colicin K; Belongs to the nucleoside-specific channel-forming outer membrane porin (Tsx) (TC 1.B.10) family. | 0.773 |
| btuB | yaeT | STM4130 | STM0224 | Outer membrane receptor for transport of vitamin B12, E colicins, and bacteriophage BF23; Involved in the active translocation of vitamin B12 (cyanocobalamin) across the outer membrane to the periplasmic space. It derives its energy for transport by interacting with the trans- periplasmic membrane protein TonB; Belongs to the TonB-dependent receptor family. BtuB (TC 1.B.14.3.1) subfamily. | 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. | 0.554 |
| envZ | htrA | STM3501 | STM0209 | Sensory histidine kinase in two-component regulatory system with OmpR; Member of the two-component regulatory system EnvZ/OmpR involved in osmoregulation (particularly of genes ompF and ompC) as well as other genes (By similarity). EnvZ functions as a membrane- associated protein kinase that phosphorylates OmpR in response to environmental signals; at low osmolarity OmpR activates ompF transcription, while at high osmolarity it represses ompF and activates ompC transcription (By similarity). | 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 [...] | 0.518 |
| envZ | ompC | STM3501 | STM2267 | Sensory histidine kinase in two-component regulatory system with OmpR; Member of the two-component regulatory system EnvZ/OmpR involved in osmoregulation (particularly of genes ompF and ompC) as well as other genes (By similarity). EnvZ functions as a membrane- associated protein kinase that phosphorylates OmpR in response to environmental signals; at low osmolarity OmpR activates ompF transcription, while at high osmolarity it represses ompF and activates ompC transcription (By similarity). | Outer membrane protein 1b (ib;c); Forms pores that allow passive diffusion of small molecules across the outer membrane. | 0.923 |
| envZ | ompF | STM3501 | STM0999 | Sensory histidine kinase in two-component regulatory system with OmpR; Member of the two-component regulatory system EnvZ/OmpR involved in osmoregulation (particularly of genes ompF and ompC) as well as other genes (By similarity). EnvZ functions as a membrane- associated protein kinase that phosphorylates OmpR in response to environmental signals; at low osmolarity OmpR activates ompF transcription, while at high osmolarity it represses ompF and activates ompC transcription (By similarity). | 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). | 0.913 |
| envZ | ompR | STM3501 | STM3502 | Sensory histidine kinase in two-component regulatory system with OmpR; Member of the two-component regulatory system EnvZ/OmpR involved in osmoregulation (particularly of genes ompF and ompC) as well as other genes (By similarity). EnvZ functions as a membrane- associated protein kinase that phosphorylates OmpR in response to environmental signals; at low osmolarity OmpR activates ompF transcription, while at high osmolarity it represses ompF and activates ompC transcription (By similarity). | Response regulator in two-component regulatory system with EnvZ; Member of the two-component regulatory system EnvZ/OmpR involved in osmoregulation (particularly of genes ompF and ompC) as well as other genes (By similarity). Plays a central role in both acid and osmotic stress responses. Binds to the promoter of both ompC and ompF; at low osmolarity it activates ompF transcription, while at high osmolarity it represses ompF and activates ompC transcription (By similarity). | 0.999 |
| envZ | tolC | STM3501 | STM3186 | Sensory histidine kinase in two-component regulatory system with OmpR; Member of the two-component regulatory system EnvZ/OmpR involved in osmoregulation (particularly of genes ompF and ompC) as well as other genes (By similarity). EnvZ functions as a membrane- associated protein kinase that phosphorylates OmpR in response to environmental signals; at low osmolarity OmpR activates ompF transcription, while at high osmolarity it represses ompF and activates ompC transcription (By similarity). | Outer membrane channel; Specific tolerance to colicin E1; segregation of daughter chromosomes; role in organic solvent tolerance; similar to E. coli outer membrane channel; specific tolerance to colicin E1; segregation of daughter chromosomes (AAC76071.1); Blastp hit to AAC76071.1 (495 aa), 89% identity in aa 1 - 495. | 0.450 |
| htrA | envZ | STM0209 | STM3501 | 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 [...] | Sensory histidine kinase in two-component regulatory system with OmpR; Member of the two-component regulatory system EnvZ/OmpR involved in osmoregulation (particularly of genes ompF and ompC) as well as other genes (By similarity). EnvZ functions as a membrane- associated protein kinase that phosphorylates OmpR in response to environmental signals; at low osmolarity OmpR activates ompF transcription, while at high osmolarity it represses ompF and activates ompC transcription (By similarity). | 0.518 |
| 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. | 0.650 |
| 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. | 0.929 |
| 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. | 0.918 |
| 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). | 0.800 |
| htrA | ompR | STM0209 | STM3502 | 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 [...] | Response regulator in two-component regulatory system with EnvZ; Member of the two-component regulatory system EnvZ/OmpR involved in osmoregulation (particularly of genes ompF and ompC) as well as other genes (By similarity). Plays a central role in both acid and osmotic stress responses. Binds to the promoter of both ompC and ompF; at low osmolarity it activates ompF transcription, while at high osmolarity it represses ompF and activates ompC transcription (By similarity). | 0.554 |
| htrA | tolC | STM0209 | STM3186 | 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 channel; Specific tolerance to colicin E1; segregation of daughter chromosomes; role in organic solvent tolerance; similar to E. coli outer membrane channel; specific tolerance to colicin E1; segregation of daughter chromosomes (AAC76071.1); Blastp hit to AAC76071.1 (495 aa), 89% identity in aa 1 - 495. | 0.455 |
| 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. | 0.897 |