| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| azo0230 | fhuA1 | azo0230 | azo0229 | Conserved hypothetical secreted protein. Homology to RPA1846 of R.palustris of 39% (trembl:Q6N8Q7). No domains predicted. No TMHs. Signal peptide present; Conserved hypothetical protein. | In E.coli this receptor binds the ferrichrome-iron ligand. It interacts with the tonB protein, which is responsible for energy coupling of the ferrichrome-promoted iron transport system. Acts as a receptor for bacteriophage T5 as well as T1, phi80 and colicin M. Binding of T5 triggers the opening of a high conductance ion channel. Can also transport the antibiotic albomycin. Signal peptide; Specificity unclear. | 0.701 |
| azo0235 | azo1830 | azo0235 | azo1830 | Conserved hypothetical membrane protein. Homology to an orf of Rubrivivax gelatinosus of 55% (gi|47575633|ref|ZP_00245668.1|(NBCI ENTREZ)). No domains predicted. No signal peptide. 1 TMHs; Conserved hypothetical protein. | Putative TonB-denpendent receptor; Similar to FepA, an iron regulated outer membrane protein. FepA is a receptor for the siderophore complex ferric enterobactin and for colcins B and D. INVOLVED IN THE INITIAL STEP OF IRON UPTAKE BY BINDING FERRIC ENTEROBACTIN THAT ALLOWS E. COLI TO EXTRACT IRON FROM THE ENVIRONMENT. ilvC: ketol-acid reductoisomerase; Function unclear. | 0.640 |
| azo0235 | fhuA1 | azo0235 | azo0229 | Conserved hypothetical membrane protein. Homology to an orf of Rubrivivax gelatinosus of 55% (gi|47575633|ref|ZP_00245668.1|(NBCI ENTREZ)). No domains predicted. No signal peptide. 1 TMHs; Conserved hypothetical protein. | In E.coli this receptor binds the ferrichrome-iron ligand. It interacts with the tonB protein, which is responsible for energy coupling of the ferrichrome-promoted iron transport system. Acts as a receptor for bacteriophage T5 as well as T1, phi80 and colicin M. Binding of T5 triggers the opening of a high conductance ion channel. Can also transport the antibiotic albomycin. Signal peptide; Specificity unclear. | 0.692 |
| azo0649 | fhuA1 | azo0649 | azo0229 | Conserved hypothetical protein. Homology to ebA1795 of Azoarcus sp. EbN1 of 46% (gnl|keqq|eba:ebA1795(KEGG)). No domains predicted. No TMHs. | In E.coli this receptor binds the ferrichrome-iron ligand. It interacts with the tonB protein, which is responsible for energy coupling of the ferrichrome-promoted iron transport system. Acts as a receptor for bacteriophage T5 as well as T1, phi80 and colicin M. Binding of T5 triggers the opening of a high conductance ion channel. Can also transport the antibiotic albomycin. Signal peptide; Specificity unclear. | 0.584 |
| azo0708 | azo1830 | azo0708 | azo1830 | Conserved hypothetical secreted protein. Homology to ne1626 of N. europaea of 46% (trembl|Q82U75) no domains predicted signal peptide TMH in signal peptide; Conserved hypothetical protein. | Putative TonB-denpendent receptor; Similar to FepA, an iron regulated outer membrane protein. FepA is a receptor for the siderophore complex ferric enterobactin and for colcins B and D. INVOLVED IN THE INITIAL STEP OF IRON UPTAKE BY BINDING FERRIC ENTEROBACTIN THAT ALLOWS E. COLI TO EXTRACT IRON FROM THE ENVIRONMENT. ilvC: ketol-acid reductoisomerase; Function unclear. | 0.640 |
| azo0708 | fhuA1 | azo0708 | azo0229 | Conserved hypothetical secreted protein. Homology to ne1626 of N. europaea of 46% (trembl|Q82U75) no domains predicted signal peptide TMH in signal peptide; Conserved hypothetical protein. | In E.coli this receptor binds the ferrichrome-iron ligand. It interacts with the tonB protein, which is responsible for energy coupling of the ferrichrome-promoted iron transport system. Acts as a receptor for bacteriophage T5 as well as T1, phi80 and colicin M. Binding of T5 triggers the opening of a high conductance ion channel. Can also transport the antibiotic albomycin. Signal peptide; Specificity unclear. | 0.692 |
| azo1830 | azo0235 | azo1830 | azo0235 | Putative TonB-denpendent receptor; Similar to FepA, an iron regulated outer membrane protein. FepA is a receptor for the siderophore complex ferric enterobactin and for colcins B and D. INVOLVED IN THE INITIAL STEP OF IRON UPTAKE BY BINDING FERRIC ENTEROBACTIN THAT ALLOWS E. COLI TO EXTRACT IRON FROM THE ENVIRONMENT. ilvC: ketol-acid reductoisomerase; Function unclear. | Conserved hypothetical membrane protein. Homology to an orf of Rubrivivax gelatinosus of 55% (gi|47575633|ref|ZP_00245668.1|(NBCI ENTREZ)). No domains predicted. No signal peptide. 1 TMHs; Conserved hypothetical protein. | 0.640 |
| azo1830 | azo0708 | azo1830 | azo0708 | Putative TonB-denpendent receptor; Similar to FepA, an iron regulated outer membrane protein. FepA is a receptor for the siderophore complex ferric enterobactin and for colcins B and D. INVOLVED IN THE INITIAL STEP OF IRON UPTAKE BY BINDING FERRIC ENTEROBACTIN THAT ALLOWS E. COLI TO EXTRACT IRON FROM THE ENVIRONMENT. ilvC: ketol-acid reductoisomerase; Function unclear. | Conserved hypothetical secreted protein. Homology to ne1626 of N. europaea of 46% (trembl|Q82U75) no domains predicted signal peptide TMH in signal peptide; Conserved hypothetical protein. | 0.640 |
| azo1830 | azo3746 | azo1830 | azo3746 | Putative TonB-denpendent receptor; Similar to FepA, an iron regulated outer membrane protein. FepA is a receptor for the siderophore complex ferric enterobactin and for colcins B and D. INVOLVED IN THE INITIAL STEP OF IRON UPTAKE BY BINDING FERRIC ENTEROBACTIN THAT ALLOWS E. COLI TO EXTRACT IRON FROM THE ENVIRONMENT. ilvC: ketol-acid reductoisomerase; Function unclear. | Hypothetical secreted protein. No homology to the data bank. No domains predicted. signal peptide no TMHs. | 0.600 |
| azo1830 | fhuA1 | azo1830 | azo0229 | Putative TonB-denpendent receptor; Similar to FepA, an iron regulated outer membrane protein. FepA is a receptor for the siderophore complex ferric enterobactin and for colcins B and D. INVOLVED IN THE INITIAL STEP OF IRON UPTAKE BY BINDING FERRIC ENTEROBACTIN THAT ALLOWS E. COLI TO EXTRACT IRON FROM THE ENVIRONMENT. ilvC: ketol-acid reductoisomerase; Function unclear. | In E.coli this receptor binds the ferrichrome-iron ligand. It interacts with the tonB protein, which is responsible for energy coupling of the ferrichrome-promoted iron transport system. Acts as a receptor for bacteriophage T5 as well as T1, phi80 and colicin M. Binding of T5 triggers the opening of a high conductance ion channel. Can also transport the antibiotic albomycin. Signal peptide; Specificity unclear. | 0.611 |
| azo1830 | tolA | azo1830 | azo0418 | Putative TonB-denpendent receptor; Similar to FepA, an iron regulated outer membrane protein. FepA is a receptor for the siderophore complex ferric enterobactin and for colcins B and D. INVOLVED IN THE INITIAL STEP OF IRON UPTAKE BY BINDING FERRIC ENTEROBACTIN THAT ALLOWS E. COLI TO EXTRACT IRON FROM THE ENVIRONMENT. ilvC: ketol-acid reductoisomerase; Function unclear. | Conserved hypothetical membrane protein. Homology to tolA of N. europaea of 39% (trembl|Q82XP0). no domains predicted InterPro: Proline-rich region (IPR000694) no signal peptide 1 TMHs; Conserved hypothetical protein. | 0.640 |
| azo1830 | tonB1 | azo1830 | azo0615 | Putative TonB-denpendent receptor; Similar to FepA, an iron regulated outer membrane protein. FepA is a receptor for the siderophore complex ferric enterobactin and for colcins B and D. INVOLVED IN THE INITIAL STEP OF IRON UPTAKE BY BINDING FERRIC ENTEROBACTIN THAT ALLOWS E. COLI TO EXTRACT IRON FROM THE ENVIRONMENT. ilvC: ketol-acid reductoisomerase; Function unclear. | Putative TonB protein. Homology to tonb2 of P. aeruginosa of 39% (TREMBL:Q9RMT3). To complete transport of bound iron across the inner membrane, a second receptor complex is needed. The major component of this is tonB, a 27kDa protein that facilitates energy transfer from the proton motive force to outer receptors Pfam: Gram-negative bacterial TonB protein no signal peptide 1 TMH; Function unclear. | 0.640 |
| azo1830 | tonB2 | azo1830 | azo2329 | Putative TonB-denpendent receptor; Similar to FepA, an iron regulated outer membrane protein. FepA is a receptor for the siderophore complex ferric enterobactin and for colcins B and D. INVOLVED IN THE INITIAL STEP OF IRON UPTAKE BY BINDING FERRIC ENTEROBACTIN THAT ALLOWS E. COLI TO EXTRACT IRON FROM THE ENVIRONMENT. ilvC: ketol-acid reductoisomerase; Function unclear. | Periplasmic biopolymer transport protein linking inner and outer membranes; Interacts with outer membrane receptor proteins that carry out high-affinity binding and energy dependent uptake into the periplasmic space of specific substrates. It could act to transduce energy from the cytoplasmic membrane to specific energy-requiring processes in the outer membrane, resulting in the release into the periplasm of ligands bound by these outer membrane proteins. Belongs to the TonB family. | 0.640 |
| azo2042 | fhuA1 | azo2042 | azo0229 | Conserved hypothetical membrane protein. Homology to ebA436 of Azoarcus sp. EbN1 of 49% (gnl|keqq|eba:ebA436(KEGG)). No domains predicted. No signal peptide. TMHMM2 reporting presence of 2 TMH's; Conserved hypothetical protein. | In E.coli this receptor binds the ferrichrome-iron ligand. It interacts with the tonB protein, which is responsible for energy coupling of the ferrichrome-promoted iron transport system. Acts as a receptor for bacteriophage T5 as well as T1, phi80 and colicin M. Binding of T5 triggers the opening of a high conductance ion channel. Can also transport the antibiotic albomycin. Signal peptide; Specificity unclear. | 0.584 |
| azo3746 | azo1830 | azo3746 | azo1830 | Hypothetical secreted protein. No homology to the data bank. No domains predicted. signal peptide no TMHs. | Putative TonB-denpendent receptor; Similar to FepA, an iron regulated outer membrane protein. FepA is a receptor for the siderophore complex ferric enterobactin and for colcins B and D. INVOLVED IN THE INITIAL STEP OF IRON UPTAKE BY BINDING FERRIC ENTEROBACTIN THAT ALLOWS E. COLI TO EXTRACT IRON FROM THE ENVIRONMENT. ilvC: ketol-acid reductoisomerase; Function unclear. | 0.600 |
| azo3746 | fhuA1 | azo3746 | azo0229 | Hypothetical secreted protein. No homology to the data bank. No domains predicted. signal peptide no TMHs. | In E.coli this receptor binds the ferrichrome-iron ligand. It interacts with the tonB protein, which is responsible for energy coupling of the ferrichrome-promoted iron transport system. Acts as a receptor for bacteriophage T5 as well as T1, phi80 and colicin M. Binding of T5 triggers the opening of a high conductance ion channel. Can also transport the antibiotic albomycin. Signal peptide; Specificity unclear. | 0.617 |
| fhuA1 | azo0230 | azo0229 | azo0230 | In E.coli this receptor binds the ferrichrome-iron ligand. It interacts with the tonB protein, which is responsible for energy coupling of the ferrichrome-promoted iron transport system. Acts as a receptor for bacteriophage T5 as well as T1, phi80 and colicin M. Binding of T5 triggers the opening of a high conductance ion channel. Can also transport the antibiotic albomycin. Signal peptide; Specificity unclear. | Conserved hypothetical secreted protein. Homology to RPA1846 of R.palustris of 39% (trembl:Q6N8Q7). No domains predicted. No TMHs. Signal peptide present; Conserved hypothetical protein. | 0.701 |
| fhuA1 | azo0235 | azo0229 | azo0235 | In E.coli this receptor binds the ferrichrome-iron ligand. It interacts with the tonB protein, which is responsible for energy coupling of the ferrichrome-promoted iron transport system. Acts as a receptor for bacteriophage T5 as well as T1, phi80 and colicin M. Binding of T5 triggers the opening of a high conductance ion channel. Can also transport the antibiotic albomycin. Signal peptide; Specificity unclear. | Conserved hypothetical membrane protein. Homology to an orf of Rubrivivax gelatinosus of 55% (gi|47575633|ref|ZP_00245668.1|(NBCI ENTREZ)). No domains predicted. No signal peptide. 1 TMHs; Conserved hypothetical protein. | 0.692 |
| fhuA1 | azo0649 | azo0229 | azo0649 | In E.coli this receptor binds the ferrichrome-iron ligand. It interacts with the tonB protein, which is responsible for energy coupling of the ferrichrome-promoted iron transport system. Acts as a receptor for bacteriophage T5 as well as T1, phi80 and colicin M. Binding of T5 triggers the opening of a high conductance ion channel. Can also transport the antibiotic albomycin. Signal peptide; Specificity unclear. | Conserved hypothetical protein. Homology to ebA1795 of Azoarcus sp. EbN1 of 46% (gnl|keqq|eba:ebA1795(KEGG)). No domains predicted. No TMHs. | 0.584 |
| fhuA1 | azo0708 | azo0229 | azo0708 | In E.coli this receptor binds the ferrichrome-iron ligand. It interacts with the tonB protein, which is responsible for energy coupling of the ferrichrome-promoted iron transport system. Acts as a receptor for bacteriophage T5 as well as T1, phi80 and colicin M. Binding of T5 triggers the opening of a high conductance ion channel. Can also transport the antibiotic albomycin. Signal peptide; Specificity unclear. | Conserved hypothetical secreted protein. Homology to ne1626 of N. europaea of 46% (trembl|Q82U75) no domains predicted signal peptide TMH in signal peptide; Conserved hypothetical protein. | 0.692 |