| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| azo1870 | clpB2 | azo1870 | azo3903 | Endopeptidase Clp; Putative protease encoded ATP-dependent Clp protease family protein similar(30 Identity,45% similarity in function) to TrEMBL:Q8X866. IPR001907. Has pfam00574,CLP_protease, Clp protease. The Clp protease has an active site catalytic triad. In E. coli Clp protease, ser-111,his-136 and asp-185 form the catalytic triad. One member has lost all of these active site residues and is therefore inactive. Some members contain one or two large insertions. Peptidase family S49 domain present. Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a [...] | Putative ATP-dependent Clp protease, ATP-binding subunit ClpB. Homology to clpB of E. coli of 38% (sprot|CLPB_ECOLI). The protein is thought to be subunits of ATP-dependent proteases which act as chaperones to target the proteases to substrates. Pfam: ATPsae family associated with various cellular activites no signal peptide no TMHs; High confidence in function and specificity; Belongs to the ClpA/ClpB family. | 0.928 |
| clpB2 | azo1870 | azo3903 | azo1870 | Putative ATP-dependent Clp protease, ATP-binding subunit ClpB. Homology to clpB of E. coli of 38% (sprot|CLPB_ECOLI). The protein is thought to be subunits of ATP-dependent proteases which act as chaperones to target the proteases to substrates. Pfam: ATPsae family associated with various cellular activites no signal peptide no TMHs; High confidence in function and specificity; Belongs to the ClpA/ClpB family. | Endopeptidase Clp; Putative protease encoded ATP-dependent Clp protease family protein similar(30 Identity,45% similarity in function) to TrEMBL:Q8X866. IPR001907. Has pfam00574,CLP_protease, Clp protease. The Clp protease has an active site catalytic triad. In E. coli Clp protease, ser-111,his-136 and asp-185 form the catalytic triad. One member has lost all of these active site residues and is therefore inactive. Some members contain one or two large insertions. Peptidase family S49 domain present. Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a [...] | 0.928 |
| clpB2 | clpP | azo3903 | azo2071 | Putative ATP-dependent Clp protease, ATP-binding subunit ClpB. Homology to clpB of E. coli of 38% (sprot|CLPB_ECOLI). The protein is thought to be subunits of ATP-dependent proteases which act as chaperones to target the proteases to substrates. Pfam: ATPsae family associated with various cellular activites no signal peptide no TMHs; High confidence in function and specificity; Belongs to the ClpA/ClpB family. | Endopeptidase Clp; Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins. Belongs to the peptidase S14 family. | 0.937 |
| clpB2 | dnaJ1 | azo3903 | azo1062 | Putative ATP-dependent Clp protease, ATP-binding subunit ClpB. Homology to clpB of E. coli of 38% (sprot|CLPB_ECOLI). The protein is thought to be subunits of ATP-dependent proteases which act as chaperones to target the proteases to substrates. Pfam: ATPsae family associated with various cellular activites no signal peptide no TMHs; High confidence in function and specificity; Belongs to the ClpA/ClpB family. | Chaperone protein DnaJ; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, D [...] | 0.900 |
| clpB2 | dnaJ2 | azo3903 | azo1266 | Putative ATP-dependent Clp protease, ATP-binding subunit ClpB. Homology to clpB of E. coli of 38% (sprot|CLPB_ECOLI). The protein is thought to be subunits of ATP-dependent proteases which act as chaperones to target the proteases to substrates. Pfam: ATPsae family associated with various cellular activites no signal peptide no TMHs; High confidence in function and specificity; Belongs to the ClpA/ClpB family. | Putative chaperone protein dnaJ. homology to dnaJ of E. coli of 32% (sprot|DNAJ_ECOLI) Acts as a co-chaperone. Stimulates jointly with grpE the ATPase activity of dnaK (By similarity). Pfam: DnaJ domain, DnaJ central domain (4 repeats), DnaJ Cterminal region no singal peptide no TMHs; Family membership. | 0.900 |
| clpB2 | dnaK | azo3903 | azo1063 | Putative ATP-dependent Clp protease, ATP-binding subunit ClpB. Homology to clpB of E. coli of 38% (sprot|CLPB_ECOLI). The protein is thought to be subunits of ATP-dependent proteases which act as chaperones to target the proteases to substrates. Pfam: ATPsae family associated with various cellular activites no signal peptide no TMHs; High confidence in function and specificity; Belongs to the ClpA/ClpB family. | Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.880 |
| clpB2 | hsp18 | azo3903 | azo3243 | Putative ATP-dependent Clp protease, ATP-binding subunit ClpB. Homology to clpB of E. coli of 38% (sprot|CLPB_ECOLI). The protein is thought to be subunits of ATP-dependent proteases which act as chaperones to target the proteases to substrates. Pfam: ATPsae family associated with various cellular activites no signal peptide no TMHs; High confidence in function and specificity; Belongs to the ClpA/ClpB family. | Putative small heat shock protein. Homology to hsp18 of C. acetobutylicum of 35% (sprot|HS18_CLOAB) InterPro: Heat shock hsp20 (alpha crystallin) proteins family (IPR002068) Pfam: Hsp20/alpa cystallin family no signal peptide no TMHs; Function unclear. | 0.895 |
| clpB2 | sciB | azo3903 | azo3902 | Putative ATP-dependent Clp protease, ATP-binding subunit ClpB. Homology to clpB of E. coli of 38% (sprot|CLPB_ECOLI). The protein is thought to be subunits of ATP-dependent proteases which act as chaperones to target the proteases to substrates. Pfam: ATPsae family associated with various cellular activites no signal peptide no TMHs; High confidence in function and specificity; Belongs to the ClpA/ClpB family. | Putative cytoplasmic protein, sciB. TrEMBl;Q93IT4(36% identity) Has PF06996;Protein of unknown function (DUF1305);IPR010732; This family consists of several hypothetical bacterial proteins of around 300 residues in length. The function of this family is unknown although one member (Q93IT4) from Salmonella enterica is thought to be involved in virulence; Conserved hypothetical protein. | 0.935 |
| clpB2 | sciC | azo3903 | azo3901 | Putative ATP-dependent Clp protease, ATP-binding subunit ClpB. Homology to clpB of E. coli of 38% (sprot|CLPB_ECOLI). The protein is thought to be subunits of ATP-dependent proteases which act as chaperones to target the proteases to substrates. Pfam: ATPsae family associated with various cellular activites no signal peptide no TMHs; High confidence in function and specificity; Belongs to the ClpA/ClpB family. | Putative cytoplasmic protein, sciC, 42% identity (57% similarity) to TrEMBL; Q93IT3. Has PF05947, Bacterial protein of unknown function (DUF879);IPR010272; This family consists of several hypothetical bacterial proteins of unknown function; Function unclear. | 0.916 |
| clpB2 | sciD | azo3903 | azo3900 | Putative ATP-dependent Clp protease, ATP-binding subunit ClpB. Homology to clpB of E. coli of 38% (sprot|CLPB_ECOLI). The protein is thought to be subunits of ATP-dependent proteases which act as chaperones to target the proteases to substrates. Pfam: ATPsae family associated with various cellular activites no signal peptide no TMHs; High confidence in function and specificity; Belongs to the ClpA/ClpB family. | Putative cytoplasmic protein, sciD,34% identity (50% similarity) to TrEMBL; Q7AXZ4. Has PF07025, Protein of unknown function (DUF1316);IPR010745;This family consists of several hypothetical bacterial proteins of around 150 residues in length. The function of this family is unknown; Conserved hypothetical protein. | 0.883 |
| clpB2 | sciK | azo3903 | azo3898 | Putative ATP-dependent Clp protease, ATP-binding subunit ClpB. Homology to clpB of E. coli of 38% (sprot|CLPB_ECOLI). The protein is thought to be subunits of ATP-dependent proteases which act as chaperones to target the proteases to substrates. Pfam: ATPsae family associated with various cellular activites no signal peptide no TMHs; High confidence in function and specificity; Belongs to the ClpA/ClpB family. | Putative cytoplasmic protein,sciK, 33% identity to TrEMBL;Q7AXZ0. Has PF05638, Protein of unknown function (DUF796);This family consists of several bacterial proteins of unknown function. Signal Peptide or TMH absent; Conserved hypothetical protein. | 0.886 |
| clpP | clpB2 | azo2071 | azo3903 | Endopeptidase Clp; Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins. Belongs to the peptidase S14 family. | Putative ATP-dependent Clp protease, ATP-binding subunit ClpB. Homology to clpB of E. coli of 38% (sprot|CLPB_ECOLI). The protein is thought to be subunits of ATP-dependent proteases which act as chaperones to target the proteases to substrates. Pfam: ATPsae family associated with various cellular activites no signal peptide no TMHs; High confidence in function and specificity; Belongs to the ClpA/ClpB family. | 0.937 |
| dnaJ1 | clpB2 | azo1062 | azo3903 | Chaperone protein DnaJ; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, D [...] | Putative ATP-dependent Clp protease, ATP-binding subunit ClpB. Homology to clpB of E. coli of 38% (sprot|CLPB_ECOLI). The protein is thought to be subunits of ATP-dependent proteases which act as chaperones to target the proteases to substrates. Pfam: ATPsae family associated with various cellular activites no signal peptide no TMHs; High confidence in function and specificity; Belongs to the ClpA/ClpB family. | 0.900 |
| dnaJ1 | dnaK | azo1062 | azo1063 | Chaperone protein DnaJ; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, D [...] | Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.997 |
| dnaJ1 | hsp18 | azo1062 | azo3243 | Chaperone protein DnaJ; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, D [...] | Putative small heat shock protein. Homology to hsp18 of C. acetobutylicum of 35% (sprot|HS18_CLOAB) InterPro: Heat shock hsp20 (alpha crystallin) proteins family (IPR002068) Pfam: Hsp20/alpa cystallin family no signal peptide no TMHs; Function unclear. | 0.629 |
| dnaJ2 | clpB2 | azo1266 | azo3903 | Putative chaperone protein dnaJ. homology to dnaJ of E. coli of 32% (sprot|DNAJ_ECOLI) Acts as a co-chaperone. Stimulates jointly with grpE the ATPase activity of dnaK (By similarity). Pfam: DnaJ domain, DnaJ central domain (4 repeats), DnaJ Cterminal region no singal peptide no TMHs; Family membership. | Putative ATP-dependent Clp protease, ATP-binding subunit ClpB. Homology to clpB of E. coli of 38% (sprot|CLPB_ECOLI). The protein is thought to be subunits of ATP-dependent proteases which act as chaperones to target the proteases to substrates. Pfam: ATPsae family associated with various cellular activites no signal peptide no TMHs; High confidence in function and specificity; Belongs to the ClpA/ClpB family. | 0.900 |
| dnaJ2 | dnaK | azo1266 | azo1063 | Putative chaperone protein dnaJ. homology to dnaJ of E. coli of 32% (sprot|DNAJ_ECOLI) Acts as a co-chaperone. Stimulates jointly with grpE the ATPase activity of dnaK (By similarity). Pfam: DnaJ domain, DnaJ central domain (4 repeats), DnaJ Cterminal region no singal peptide no TMHs; Family membership. | Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.990 |
| dnaJ2 | hsp18 | azo1266 | azo3243 | Putative chaperone protein dnaJ. homology to dnaJ of E. coli of 32% (sprot|DNAJ_ECOLI) Acts as a co-chaperone. Stimulates jointly with grpE the ATPase activity of dnaK (By similarity). Pfam: DnaJ domain, DnaJ central domain (4 repeats), DnaJ Cterminal region no singal peptide no TMHs; Family membership. | Putative small heat shock protein. Homology to hsp18 of C. acetobutylicum of 35% (sprot|HS18_CLOAB) InterPro: Heat shock hsp20 (alpha crystallin) proteins family (IPR002068) Pfam: Hsp20/alpa cystallin family no signal peptide no TMHs; Function unclear. | 0.629 |
| dnaK | clpB2 | azo1063 | azo3903 | Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | Putative ATP-dependent Clp protease, ATP-binding subunit ClpB. Homology to clpB of E. coli of 38% (sprot|CLPB_ECOLI). The protein is thought to be subunits of ATP-dependent proteases which act as chaperones to target the proteases to substrates. Pfam: ATPsae family associated with various cellular activites no signal peptide no TMHs; High confidence in function and specificity; Belongs to the ClpA/ClpB family. | 0.880 |
| dnaK | dnaJ1 | azo1063 | azo1062 | Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | Chaperone protein DnaJ; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, D [...] | 0.997 |
