| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| ANQ21661.1 | pepT | BA893_08255 | BA893_18955 | NAD-glutamate dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology. | Peptidase T; Cleaves the N-terminal amino acid of tripeptides. Belongs to the peptidase M20B family. | 0.518 |
| ANQ22787.1 | clpP | BA893_14445 | BA893_04690 | Bacterioferritin; Iron-storage protein, whose ferroxidase center binds Fe(2+) ions, oxidizes them by dioxygen to Fe(3+), and participates in the subsequent Fe(3+) oxide mineral core formation within the central cavity of the protein complex; Belongs to the bacterioferritin family. | 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. | 0.511 |
| ANQ22787.1 | cyaY | BA893_14445 | BA893_15525 | Bacterioferritin; Iron-storage protein, whose ferroxidase center binds Fe(2+) ions, oxidizes them by dioxygen to Fe(3+), and participates in the subsequent Fe(3+) oxide mineral core formation within the central cavity of the protein complex; Belongs to the bacterioferritin family. | Iron donor protein CyaY; Involved in iron-sulfur (Fe-S) cluster assembly. May act as a regulator of Fe-S biogenesis. | 0.654 |
| ANQ22787.1 | hslV | BA893_14445 | BA893_01515 | Bacterioferritin; Iron-storage protein, whose ferroxidase center binds Fe(2+) ions, oxidizes them by dioxygen to Fe(3+), and participates in the subsequent Fe(3+) oxide mineral core formation within the central cavity of the protein complex; Belongs to the bacterioferritin family. | HslU--HslV peptidase proteolytic subunit; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.464 |
| ANQ22787.1 | htpG | BA893_14445 | BA893_04245 | Bacterioferritin; Iron-storage protein, whose ferroxidase center binds Fe(2+) ions, oxidizes them by dioxygen to Fe(3+), and participates in the subsequent Fe(3+) oxide mineral core formation within the central cavity of the protein complex; Belongs to the bacterioferritin family. | Molecular chaperone HtpG; Molecular chaperone. Has ATPase activity. | 0.512 |
| ANQ22787.1 | htpX | BA893_14445 | BA893_06070 | Bacterioferritin; Iron-storage protein, whose ferroxidase center binds Fe(2+) ions, oxidizes them by dioxygen to Fe(3+), and participates in the subsequent Fe(3+) oxide mineral core formation within the central cavity of the protein complex; Belongs to the bacterioferritin family. | Zinc metalloprotease HtpX; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the peptidase M48B family. | 0.464 |
| ANQ22787.1 | pepT | BA893_14445 | BA893_18955 | Bacterioferritin; Iron-storage protein, whose ferroxidase center binds Fe(2+) ions, oxidizes them by dioxygen to Fe(3+), and participates in the subsequent Fe(3+) oxide mineral core formation within the central cavity of the protein complex; Belongs to the bacterioferritin family. | Peptidase T; Cleaves the N-terminal amino acid of tripeptides. Belongs to the peptidase M20B family. | 0.468 |
| ANQ24773.1 | pepT | BA893_24635 | BA893_18955 | Mechanosensitive ion channel protein MscS; Derived by automated computational analysis using gene prediction method: Protein Homology. | Peptidase T; Cleaves the N-terminal amino acid of tripeptides. Belongs to the peptidase M20B family. | 0.490 |
| ANQ24881.1 | pepT | BA893_18950 | BA893_18955 | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | Peptidase T; Cleaves the N-terminal amino acid of tripeptides. Belongs to the peptidase M20B family. | 0.530 |
| argE | pepT | BA893_14405 | BA893_18955 | Acetylornithine deacetylase; Catalyzes the formation of L-ornithine from N(2)-acetyl-L-ornithine in arginine biosynthesis; Derived by automated computational analysis using gene prediction method: Protein Homology. | Peptidase T; Cleaves the N-terminal amino acid of tripeptides. Belongs to the peptidase M20B family. | 0.603 |
| clpP | ANQ22787.1 | BA893_04690 | BA893_14445 | 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. | Bacterioferritin; Iron-storage protein, whose ferroxidase center binds Fe(2+) ions, oxidizes them by dioxygen to Fe(3+), and participates in the subsequent Fe(3+) oxide mineral core formation within the central cavity of the protein complex; Belongs to the bacterioferritin family. | 0.511 |
| clpP | cyaY | BA893_04690 | BA893_15525 | 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. | Iron donor protein CyaY; Involved in iron-sulfur (Fe-S) cluster assembly. May act as a regulator of Fe-S biogenesis. | 0.489 |
| clpP | hslV | BA893_04690 | BA893_01515 | 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. | HslU--HslV peptidase proteolytic subunit; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.854 |
| clpP | htpG | BA893_04690 | BA893_04245 | 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. | Molecular chaperone HtpG; Molecular chaperone. Has ATPase activity. | 0.824 |
| clpP | htpX | BA893_04690 | BA893_06070 | 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. | Zinc metalloprotease HtpX; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the peptidase M48B family. | 0.607 |
| clpP | pepT | BA893_04690 | BA893_18955 | 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. | Peptidase T; Cleaves the N-terminal amino acid of tripeptides. Belongs to the peptidase M20B family. | 0.495 |
| cyaY | ANQ22787.1 | BA893_15525 | BA893_14445 | Iron donor protein CyaY; Involved in iron-sulfur (Fe-S) cluster assembly. May act as a regulator of Fe-S biogenesis. | Bacterioferritin; Iron-storage protein, whose ferroxidase center binds Fe(2+) ions, oxidizes them by dioxygen to Fe(3+), and participates in the subsequent Fe(3+) oxide mineral core formation within the central cavity of the protein complex; Belongs to the bacterioferritin family. | 0.654 |
| cyaY | clpP | BA893_15525 | BA893_04690 | Iron donor protein CyaY; Involved in iron-sulfur (Fe-S) cluster assembly. May act as a regulator of Fe-S biogenesis. | 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. | 0.489 |
| cyaY | hslV | BA893_15525 | BA893_01515 | Iron donor protein CyaY; Involved in iron-sulfur (Fe-S) cluster assembly. May act as a regulator of Fe-S biogenesis. | HslU--HslV peptidase proteolytic subunit; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.471 |
| cyaY | htpG | BA893_15525 | BA893_04245 | Iron donor protein CyaY; Involved in iron-sulfur (Fe-S) cluster assembly. May act as a regulator of Fe-S biogenesis. | Molecular chaperone HtpG; Molecular chaperone. Has ATPase activity. | 0.465 |