| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| azo0358 | azo3617 | azo0358 | azo3617 | Putative two-component sensor kinase; Region start changed from 382943 to 383189 (246 bases). | Putative calcium binding protein,40% similarity to TrEMBL;O22845. Has 3 EFh|EF-hand, calcium binding motif;(SMART|SM00054):Many calcium-binding proteins belong to the same evolutionary family and share a type of calcium-binding domain known as the EF-hand. This type of domain consists of a twelve residue loop flanked on both side by a twelve residue alpha-helical domain. In an EF-hand loop the calcium ion is coordinated in a pentagonal bipyramidal configuration. The six residues involved in the binding are in positions 1, 3, 5, 7, 9 and 12; these residues are denoted by X, Y, Z, -Y, -X [...] | 0.767 |
| azo0358 | dnaK | azo0358 | azo1063 | Putative two-component sensor kinase; Region start changed from 382943 to 383189 (246 bases). | Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.987 |
| azo0358 | fkbP | azo0358 | azo3319 | Putative two-component sensor kinase; Region start changed from 382943 to 383189 (246 bases). | Peptidyl-prolyl cis-trans isomerase. Homology to fkbP of N. meningitidis of 69% (sprot|FKBP_NEIMB) PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. InterPro: FKBP-type peptidyl-prolyl cis-trans isomerase (PPIase)(IPR001179) Pfam: FKBP-type peptidyl-prolyl cis-trans isomerase no signal peptide no TMHs; High confidence in function and specificity. | 0.965 |
| azo0358 | hscA | azo0358 | azo2012 | Putative two-component sensor kinase; Region start changed from 382943 to 383189 (246 bases). | Probable chaperone protein; Chaperone involved in the maturation of iron-sulfur cluster- containing proteins. Has a low intrinsic ATPase activity which is markedly stimulated by HscB. | 0.987 |
| azo3617 | azo0358 | azo3617 | azo0358 | Putative calcium binding protein,40% similarity to TrEMBL;O22845. Has 3 EFh|EF-hand, calcium binding motif;(SMART|SM00054):Many calcium-binding proteins belong to the same evolutionary family and share a type of calcium-binding domain known as the EF-hand. This type of domain consists of a twelve residue loop flanked on both side by a twelve residue alpha-helical domain. In an EF-hand loop the calcium ion is coordinated in a pentagonal bipyramidal configuration. The six residues involved in the binding are in positions 1, 3, 5, 7, 9 and 12; these residues are denoted by X, Y, Z, -Y, -X [...] | Putative two-component sensor kinase; Region start changed from 382943 to 383189 (246 bases). | 0.767 |
| azo3617 | dnaK | azo3617 | azo1063 | Putative calcium binding protein,40% similarity to TrEMBL;O22845. Has 3 EFh|EF-hand, calcium binding motif;(SMART|SM00054):Many calcium-binding proteins belong to the same evolutionary family and share a type of calcium-binding domain known as the EF-hand. This type of domain consists of a twelve residue loop flanked on both side by a twelve residue alpha-helical domain. In an EF-hand loop the calcium ion is coordinated in a pentagonal bipyramidal configuration. The six residues involved in the binding are in positions 1, 3, 5, 7, 9 and 12; these residues are denoted by X, Y, Z, -Y, -X [...] | Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.635 |
| azo3617 | fkbP | azo3617 | azo3319 | Putative calcium binding protein,40% similarity to TrEMBL;O22845. Has 3 EFh|EF-hand, calcium binding motif;(SMART|SM00054):Many calcium-binding proteins belong to the same evolutionary family and share a type of calcium-binding domain known as the EF-hand. This type of domain consists of a twelve residue loop flanked on both side by a twelve residue alpha-helical domain. In an EF-hand loop the calcium ion is coordinated in a pentagonal bipyramidal configuration. The six residues involved in the binding are in positions 1, 3, 5, 7, 9 and 12; these residues are denoted by X, Y, Z, -Y, -X [...] | Peptidyl-prolyl cis-trans isomerase. Homology to fkbP of N. meningitidis of 69% (sprot|FKBP_NEIMB) PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. InterPro: FKBP-type peptidyl-prolyl cis-trans isomerase (PPIase)(IPR001179) Pfam: FKBP-type peptidyl-prolyl cis-trans isomerase no signal peptide no TMHs; High confidence in function and specificity. | 0.928 |
| azo3617 | hscA | azo3617 | azo2012 | Putative calcium binding protein,40% similarity to TrEMBL;O22845. Has 3 EFh|EF-hand, calcium binding motif;(SMART|SM00054):Many calcium-binding proteins belong to the same evolutionary family and share a type of calcium-binding domain known as the EF-hand. This type of domain consists of a twelve residue loop flanked on both side by a twelve residue alpha-helical domain. In an EF-hand loop the calcium ion is coordinated in a pentagonal bipyramidal configuration. The six residues involved in the binding are in positions 1, 3, 5, 7, 9 and 12; these residues are denoted by X, Y, Z, -Y, -X [...] | Probable chaperone protein; Chaperone involved in the maturation of iron-sulfur cluster- containing proteins. Has a low intrinsic ATPase activity which is markedly stimulated by HscB. | 0.635 |
| azo3617 | htpG | azo3617 | azo1425 | Putative calcium binding protein,40% similarity to TrEMBL;O22845. Has 3 EFh|EF-hand, calcium binding motif;(SMART|SM00054):Many calcium-binding proteins belong to the same evolutionary family and share a type of calcium-binding domain known as the EF-hand. This type of domain consists of a twelve residue loop flanked on both side by a twelve residue alpha-helical domain. In an EF-hand loop the calcium ion is coordinated in a pentagonal bipyramidal configuration. The six residues involved in the binding are in positions 1, 3, 5, 7, 9 and 12; these residues are denoted by X, Y, Z, -Y, -X [...] | Probable chaperon protein HtpG; Molecular chaperone. Has ATPase activity. | 0.627 |
| azo3956 | fkbP | azo3956 | azo3319 | Conserved hypothetical protein, has weak homlogs in the Database. TrEMBL;Q88I83(25% Identity). gi|46140644|ref|ZP_00152253.2|, 30% Identity to Dechloromonas aromatica RCB,Nucleotidyltransferase/DNA polymerase involved in DNA repair Has PF00817,impB/mucB/samB family; IPR001126, UMUC_like; These proteins are involved in UV protection.In Escherichia coli, UV and many chemicals appear to cause mutagenesis by a process of translesion synthesis that requires DNA polymerase III and the SOS-regulated proteins UmuD, UmuC and RecA. This machinery allows the replication to continue through DNA le [...] | Peptidyl-prolyl cis-trans isomerase. Homology to fkbP of N. meningitidis of 69% (sprot|FKBP_NEIMB) PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. InterPro: FKBP-type peptidyl-prolyl cis-trans isomerase (PPIase)(IPR001179) Pfam: FKBP-type peptidyl-prolyl cis-trans isomerase no signal peptide no TMHs; High confidence in function and specificity. | 0.827 |
| dinP | fkbP | azo2786 | azo3319 | DNA-directed DNA polymerase; Poorly processive, error-prone DNA polymerase involved in untargeted mutagenesis. Copies undamaged DNA at stalled replication forks, which arise in vivo from mismatched or misaligned primer ends. These misaligned primers can be extended by PolIV. Exhibits no 3'-5' exonuclease (proofreading) activity. May be involved in translesional synthesis, in conjunction with the beta clamp from PolIII. | Peptidyl-prolyl cis-trans isomerase. Homology to fkbP of N. meningitidis of 69% (sprot|FKBP_NEIMB) PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. InterPro: FKBP-type peptidyl-prolyl cis-trans isomerase (PPIase)(IPR001179) Pfam: FKBP-type peptidyl-prolyl cis-trans isomerase no signal peptide no TMHs; High confidence in function and specificity. | 0.827 |
| dnaK | azo0358 | azo1063 | azo0358 | Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | Putative two-component sensor kinase; Region start changed from 382943 to 383189 (246 bases). | 0.987 |
| dnaK | azo3617 | azo1063 | azo3617 | Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | Putative calcium binding protein,40% similarity to TrEMBL;O22845. Has 3 EFh|EF-hand, calcium binding motif;(SMART|SM00054):Many calcium-binding proteins belong to the same evolutionary family and share a type of calcium-binding domain known as the EF-hand. This type of domain consists of a twelve residue loop flanked on both side by a twelve residue alpha-helical domain. In an EF-hand loop the calcium ion is coordinated in a pentagonal bipyramidal configuration. The six residues involved in the binding are in positions 1, 3, 5, 7, 9 and 12; these residues are denoted by X, Y, Z, -Y, -X [...] | 0.635 |
| dnaK | fkbP | azo1063 | azo3319 | Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | Peptidyl-prolyl cis-trans isomerase. Homology to fkbP of N. meningitidis of 69% (sprot|FKBP_NEIMB) PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. InterPro: FKBP-type peptidyl-prolyl cis-trans isomerase (PPIase)(IPR001179) Pfam: FKBP-type peptidyl-prolyl cis-trans isomerase no signal peptide no TMHs; High confidence in function and specificity. | 0.750 |
| dnaK | htpG | azo1063 | azo1425 | Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | Probable chaperon protein HtpG; Molecular chaperone. Has ATPase activity. | 0.989 |
| fkbP | azo0358 | azo3319 | azo0358 | Peptidyl-prolyl cis-trans isomerase. Homology to fkbP of N. meningitidis of 69% (sprot|FKBP_NEIMB) PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. InterPro: FKBP-type peptidyl-prolyl cis-trans isomerase (PPIase)(IPR001179) Pfam: FKBP-type peptidyl-prolyl cis-trans isomerase no signal peptide no TMHs; High confidence in function and specificity. | Putative two-component sensor kinase; Region start changed from 382943 to 383189 (246 bases). | 0.965 |
| fkbP | azo3617 | azo3319 | azo3617 | Peptidyl-prolyl cis-trans isomerase. Homology to fkbP of N. meningitidis of 69% (sprot|FKBP_NEIMB) PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. InterPro: FKBP-type peptidyl-prolyl cis-trans isomerase (PPIase)(IPR001179) Pfam: FKBP-type peptidyl-prolyl cis-trans isomerase no signal peptide no TMHs; High confidence in function and specificity. | Putative calcium binding protein,40% similarity to TrEMBL;O22845. Has 3 EFh|EF-hand, calcium binding motif;(SMART|SM00054):Many calcium-binding proteins belong to the same evolutionary family and share a type of calcium-binding domain known as the EF-hand. This type of domain consists of a twelve residue loop flanked on both side by a twelve residue alpha-helical domain. In an EF-hand loop the calcium ion is coordinated in a pentagonal bipyramidal configuration. The six residues involved in the binding are in positions 1, 3, 5, 7, 9 and 12; these residues are denoted by X, Y, Z, -Y, -X [...] | 0.928 |
| fkbP | azo3956 | azo3319 | azo3956 | Peptidyl-prolyl cis-trans isomerase. Homology to fkbP of N. meningitidis of 69% (sprot|FKBP_NEIMB) PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. InterPro: FKBP-type peptidyl-prolyl cis-trans isomerase (PPIase)(IPR001179) Pfam: FKBP-type peptidyl-prolyl cis-trans isomerase no signal peptide no TMHs; High confidence in function and specificity. | Conserved hypothetical protein, has weak homlogs in the Database. TrEMBL;Q88I83(25% Identity). gi|46140644|ref|ZP_00152253.2|, 30% Identity to Dechloromonas aromatica RCB,Nucleotidyltransferase/DNA polymerase involved in DNA repair Has PF00817,impB/mucB/samB family; IPR001126, UMUC_like; These proteins are involved in UV protection.In Escherichia coli, UV and many chemicals appear to cause mutagenesis by a process of translesion synthesis that requires DNA polymerase III and the SOS-regulated proteins UmuD, UmuC and RecA. This machinery allows the replication to continue through DNA le [...] | 0.827 |
| fkbP | dinP | azo3319 | azo2786 | Peptidyl-prolyl cis-trans isomerase. Homology to fkbP of N. meningitidis of 69% (sprot|FKBP_NEIMB) PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. InterPro: FKBP-type peptidyl-prolyl cis-trans isomerase (PPIase)(IPR001179) Pfam: FKBP-type peptidyl-prolyl cis-trans isomerase no signal peptide no TMHs; High confidence in function and specificity. | DNA-directed DNA polymerase; Poorly processive, error-prone DNA polymerase involved in untargeted mutagenesis. Copies undamaged DNA at stalled replication forks, which arise in vivo from mismatched or misaligned primer ends. These misaligned primers can be extended by PolIV. Exhibits no 3'-5' exonuclease (proofreading) activity. May be involved in translesional synthesis, in conjunction with the beta clamp from PolIII. | 0.827 |
| fkbP | dnaK | azo3319 | azo1063 | Peptidyl-prolyl cis-trans isomerase. Homology to fkbP of N. meningitidis of 69% (sprot|FKBP_NEIMB) PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. InterPro: FKBP-type peptidyl-prolyl cis-trans isomerase (PPIase)(IPR001179) Pfam: FKBP-type peptidyl-prolyl cis-trans isomerase no signal peptide no TMHs; High confidence in function and specificity. | Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.750 |