node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
OGR29624.1 | OGR30640.1 | A2005_11675 | A2005_11885 | MBL fold metallo-hydrolase; Derived by automated computational analysis using gene prediction method: Protein Homology. | Peptide-methionine (R)-S-oxide reductase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the MsrB Met sulfoxide reductase family. | 0.416 |
OGR29624.1 | atpD | A2005_11675 | A2005_07960 | MBL fold metallo-hydrolase; Derived by automated computational analysis using gene prediction method: Protein Homology. | F0F1 ATP synthase subunit beta; Produces ATP from ADP in the presence of a proton gradient across the membrane. The catalytic sites are hosted primarily by the beta subunits. | 0.602 |
OGR29624.1 | clpP | A2005_11675 | A2005_06225 | MBL fold metallo-hydrolase; Derived by automated computational analysis using gene prediction method: Protein Homology. | ATP-dependent Clp endopeptidase, proteolytic subunit ClpP; 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. | 0.436 |
OGR29624.1 | clpX | A2005_11675 | A2005_06230 | MBL fold metallo-hydrolase; Derived by automated computational analysis using gene prediction method: Protein Homology. | ATP-dependent protease ATP-binding subunit ClpX; ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP. | 0.610 |
OGR29624.1 | rpoD | A2005_11675 | A2005_08275 | MBL fold metallo-hydrolase; Derived by automated computational analysis using gene prediction method: Protein Homology. | RNA polymerase sigma factor RpoD; Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released. This sigma factor is the primary sigma factor during exponential growth. | 0.552 |
OGR29624.1 | tig | A2005_11675 | A2005_06220 | MBL fold metallo-hydrolase; Derived by automated computational analysis using gene prediction method: Protein Homology. | Trigger factor; Involved in protein export. Acts as a chaperone by maintaining the newly synthesized protein in an open conformation. Functions as a peptidyl-prolyl cis-trans isomerase; Belongs to the FKBP-type PPIase family. Tig subfamily. | 0.405 |
OGR30640.1 | OGR29624.1 | A2005_11885 | A2005_11675 | Peptide-methionine (R)-S-oxide reductase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the MsrB Met sulfoxide reductase family. | MBL fold metallo-hydrolase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.416 |
OGR30640.1 | clpX | A2005_11885 | A2005_06230 | Peptide-methionine (R)-S-oxide reductase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the MsrB Met sulfoxide reductase family. | ATP-dependent protease ATP-binding subunit ClpX; ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP. | 0.619 |
atpD | OGR29624.1 | A2005_07960 | A2005_11675 | F0F1 ATP synthase subunit beta; Produces ATP from ADP in the presence of a proton gradient across the membrane. The catalytic sites are hosted primarily by the beta subunits. | MBL fold metallo-hydrolase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.602 |
atpD | clpX | A2005_07960 | A2005_06230 | F0F1 ATP synthase subunit beta; Produces ATP from ADP in the presence of a proton gradient across the membrane. The catalytic sites are hosted primarily by the beta subunits. | ATP-dependent protease ATP-binding subunit ClpX; ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP. | 0.894 |
atpD | tig | A2005_07960 | A2005_06220 | F0F1 ATP synthase subunit beta; Produces ATP from ADP in the presence of a proton gradient across the membrane. The catalytic sites are hosted primarily by the beta subunits. | Trigger factor; Involved in protein export. Acts as a chaperone by maintaining the newly synthesized protein in an open conformation. Functions as a peptidyl-prolyl cis-trans isomerase; Belongs to the FKBP-type PPIase family. Tig subfamily. | 0.723 |
clpP | OGR29624.1 | A2005_06225 | A2005_11675 | ATP-dependent Clp endopeptidase, proteolytic subunit ClpP; 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. | MBL fold metallo-hydrolase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.436 |
clpP | clpX | A2005_06225 | A2005_06230 | ATP-dependent Clp endopeptidase, proteolytic subunit ClpP; 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. | ATP-dependent protease ATP-binding subunit ClpX; ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP. | 0.999 |
clpP | hfq | A2005_06225 | A2005_05750 | ATP-dependent Clp endopeptidase, proteolytic subunit ClpP; 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. | RNA chaperone Hfq; RNA chaperone that binds small regulatory RNA (sRNAs) and mRNAs to facilitate mRNA translational regulation in response to envelope stress, environmental stress and changes in metabolite concentrations. Also binds with high specificity to tRNAs. Belongs to the Hfq family. | 0.627 |
clpP | lon-2 | A2005_06225 | A2005_06235 | ATP-dependent Clp endopeptidase, proteolytic subunit ClpP; 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. | Endopeptidase La; ATP-dependent serine protease that mediates the selective degradation of mutant and abnormal proteins as well as certain short- lived regulatory proteins. Required for cellular homeostasis and for survival from DNA damage and developmental changes induced by stress. Degrades polypeptides processively to yield small peptide fragments that are 5 to 10 amino acids long. Binds to DNA in a double-stranded, site-specific manner. | 0.824 |
clpP | lon-3 | A2005_06225 | A2005_10220 | ATP-dependent Clp endopeptidase, proteolytic subunit ClpP; 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. | Endopeptidase La; ATP-dependent serine protease that mediates the selective degradation of mutant and abnormal proteins as well as certain short- lived regulatory proteins. Required for cellular homeostasis and for survival from DNA damage and developmental changes induced by stress. Degrades polypeptides processively to yield small peptide fragments that are 5 to 10 amino acids long. Binds to DNA in a double-stranded, site-specific manner. | 0.647 |
clpP | lon-4 | A2005_06225 | A2005_11990 | ATP-dependent Clp endopeptidase, proteolytic subunit ClpP; 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. | Endopeptidase La; ATP-dependent serine protease that mediates the selective degradation of mutant and abnormal proteins as well as certain short- lived regulatory proteins. Required for cellular homeostasis and for survival from DNA damage and developmental changes induced by stress. Degrades polypeptides processively to yield small peptide fragments that are 5 to 10 amino acids long. Binds to DNA in a double-stranded, site-specific manner. | 0.633 |
clpP | tig | A2005_06225 | A2005_06220 | ATP-dependent Clp endopeptidase, proteolytic subunit ClpP; 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. | Trigger factor; Involved in protein export. Acts as a chaperone by maintaining the newly synthesized protein in an open conformation. Functions as a peptidyl-prolyl cis-trans isomerase; Belongs to the FKBP-type PPIase family. Tig subfamily. | 0.929 |
clpX | OGR29624.1 | A2005_06230 | A2005_11675 | ATP-dependent protease ATP-binding subunit ClpX; ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP. | MBL fold metallo-hydrolase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.610 |
clpX | OGR30640.1 | A2005_06230 | A2005_11885 | ATP-dependent protease ATP-binding subunit ClpX; ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP. | Peptide-methionine (R)-S-oxide reductase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the MsrB Met sulfoxide reductase family. | 0.619 |