node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
STM1228 | pepT | STM1228 | STM1227 | Putative periplasmic protein. | Putative peptidase T; Cleaves the N-terminal amino acid of tripeptides. Hydrolyzes tripeptides containing N-terminal methionine, leucine, or phenylalanine. Displays little or no activity against dipeptides, N- blocked or C-blocked tripeptides, and tetrapeptides. Belongs to the peptidase M20B family. | 0.778 |
STM1228 | potA | STM1228 | STM1226 | Putative periplasmic protein. | Spermidine/putrescine transporter; Part of the ABC transporter complex PotABCD involved in spermidine/putrescine import. Responsible for energy coupling to the transport system; Belongs to the ABC transporter superfamily. Spermidine/putrescine importer (TC 3.A.1.11.1) family. | 0.469 |
STM1228 | potB | STM1228 | STM1225 | Putative periplasmic protein. | Spermidine/putrescine transporter; Required for the activity of the bacterial periplasmic transport system of putrescine and spermidine; Belongs to the binding-protein-dependent transport system permease family. CysTW subfamily. | 0.469 |
ligT | pepT | STM0188 | STM1227 | 2'-5' RNA ligase; Hydrolyzes RNA 2',3'-cyclic phosphodiester to an RNA 2'- phosphomonoester; Belongs to the 2H phosphoesterase superfamily. ThpR family. | Putative peptidase T; Cleaves the N-terminal amino acid of tripeptides. Hydrolyzes tripeptides containing N-terminal methionine, leucine, or phenylalanine. Displays little or no activity against dipeptides, N- blocked or C-blocked tripeptides, and tetrapeptides. Belongs to the peptidase M20B family. | 0.456 |
ligT | ynfK | STM0188 | STM1489 | 2'-5' RNA ligase; Hydrolyzes RNA 2',3'-cyclic phosphodiester to an RNA 2'- phosphomonoester; Belongs to the 2H phosphoesterase superfamily. ThpR family. | Putative dethiobiotin synthase; Catalyzes a mechanistically unusual reaction, the ATP- dependent insertion of CO2 between the N7 and N8 nitrogen atoms of 7,8- diaminopelargonic acid (DAPA) to form an ureido ring. Belongs to the dethiobiotin synthetase family. | 0.503 |
nifJ | pepP | STM1651 | STM3058 | Similar to E. coli putative oxidoreductase, Fe-S subunit (AAC74460.1); Blastp hit to AAC74460.1 (1174 aa), 92% identity in aa 1 - 1174. | Similar to E. coli proline aminopeptidase P II (AAC75946.1); Blastp hit to AAC75946.1 (441 aa), 91% identity in aa 4 - 441. | 0.510 |
nifJ | pepQ | STM1651 | STM3984 | Similar to E. coli putative oxidoreductase, Fe-S subunit (AAC74460.1); Blastp hit to AAC74460.1 (1174 aa), 92% identity in aa 1 - 1174. | Proline dipeptidase; Splits dipeptides with a prolyl residue in the C-terminal position. | 0.514 |
nifJ | pepT | STM1651 | STM1227 | Similar to E. coli putative oxidoreductase, Fe-S subunit (AAC74460.1); Blastp hit to AAC74460.1 (1174 aa), 92% identity in aa 1 - 1174. | Putative peptidase T; Cleaves the N-terminal amino acid of tripeptides. Hydrolyzes tripeptides containing N-terminal methionine, leucine, or phenylalanine. Displays little or no activity against dipeptides, N- blocked or C-blocked tripeptides, and tetrapeptides. Belongs to the peptidase M20B family. | 0.474 |
pepE | pepP | STM4190 | STM3058 | (alpha)-aspartyl dipeptidase; Hydrolyzes dipeptides containing N-terminal aspartate residues. May play a role in allowing the cell to use peptide aspartate to spare carbon otherwise required for the synthesis of the aspartate family of amino acids. | Similar to E. coli proline aminopeptidase P II (AAC75946.1); Blastp hit to AAC75946.1 (441 aa), 91% identity in aa 4 - 441. | 0.484 |
pepE | pepQ | STM4190 | STM3984 | (alpha)-aspartyl dipeptidase; Hydrolyzes dipeptides containing N-terminal aspartate residues. May play a role in allowing the cell to use peptide aspartate to spare carbon otherwise required for the synthesis of the aspartate family of amino acids. | Proline dipeptidase; Splits dipeptides with a prolyl residue in the C-terminal position. | 0.493 |
pepE | pepT | STM4190 | STM1227 | (alpha)-aspartyl dipeptidase; Hydrolyzes dipeptides containing N-terminal aspartate residues. May play a role in allowing the cell to use peptide aspartate to spare carbon otherwise required for the synthesis of the aspartate family of amino acids. | Putative peptidase T; Cleaves the N-terminal amino acid of tripeptides. Hydrolyzes tripeptides containing N-terminal methionine, leucine, or phenylalanine. Displays little or no activity against dipeptides, N- blocked or C-blocked tripeptides, and tetrapeptides. Belongs to the peptidase M20B family. | 0.578 |
pepE | ynfK | STM4190 | STM1489 | (alpha)-aspartyl dipeptidase; Hydrolyzes dipeptides containing N-terminal aspartate residues. May play a role in allowing the cell to use peptide aspartate to spare carbon otherwise required for the synthesis of the aspartate family of amino acids. | Putative dethiobiotin synthase; Catalyzes a mechanistically unusual reaction, the ATP- dependent insertion of CO2 between the N7 and N8 nitrogen atoms of 7,8- diaminopelargonic acid (DAPA) to form an ureido ring. Belongs to the dethiobiotin synthetase family. | 0.401 |
pepN | pepP | STM1057 | STM3058 | Similar to E. coli aminopeptidase N (AAC74018.1); Blastp hit to AAC74018.1 (870 aa), 94% identity in aa 1 - 870. | Similar to E. coli proline aminopeptidase P II (AAC75946.1); Blastp hit to AAC75946.1 (441 aa), 91% identity in aa 4 - 441. | 0.813 |
pepN | pepQ | STM1057 | STM3984 | Similar to E. coli aminopeptidase N (AAC74018.1); Blastp hit to AAC74018.1 (870 aa), 94% identity in aa 1 - 870. | Proline dipeptidase; Splits dipeptides with a prolyl residue in the C-terminal position. | 0.876 |
pepN | pepT | STM1057 | STM1227 | Similar to E. coli aminopeptidase N (AAC74018.1); Blastp hit to AAC74018.1 (870 aa), 94% identity in aa 1 - 870. | Putative peptidase T; Cleaves the N-terminal amino acid of tripeptides. Hydrolyzes tripeptides containing N-terminal methionine, leucine, or phenylalanine. Displays little or no activity against dipeptides, N- blocked or C-blocked tripeptides, and tetrapeptides. Belongs to the peptidase M20B family. | 0.828 |
pepP | nifJ | STM3058 | STM1651 | Similar to E. coli proline aminopeptidase P II (AAC75946.1); Blastp hit to AAC75946.1 (441 aa), 91% identity in aa 4 - 441. | Similar to E. coli putative oxidoreductase, Fe-S subunit (AAC74460.1); Blastp hit to AAC74460.1 (1174 aa), 92% identity in aa 1 - 1174. | 0.510 |
pepP | pepE | STM3058 | STM4190 | Similar to E. coli proline aminopeptidase P II (AAC75946.1); Blastp hit to AAC75946.1 (441 aa), 91% identity in aa 4 - 441. | (alpha)-aspartyl dipeptidase; Hydrolyzes dipeptides containing N-terminal aspartate residues. May play a role in allowing the cell to use peptide aspartate to spare carbon otherwise required for the synthesis of the aspartate family of amino acids. | 0.484 |
pepP | pepN | STM3058 | STM1057 | Similar to E. coli proline aminopeptidase P II (AAC75946.1); Blastp hit to AAC75946.1 (441 aa), 91% identity in aa 4 - 441. | Similar to E. coli aminopeptidase N (AAC74018.1); Blastp hit to AAC74018.1 (870 aa), 94% identity in aa 1 - 870. | 0.813 |
pepP | pepQ | STM3058 | STM3984 | Similar to E. coli proline aminopeptidase P II (AAC75946.1); Blastp hit to AAC75946.1 (441 aa), 91% identity in aa 4 - 441. | Proline dipeptidase; Splits dipeptides with a prolyl residue in the C-terminal position. | 0.544 |
pepP | pepT | STM3058 | STM1227 | Similar to E. coli proline aminopeptidase P II (AAC75946.1); Blastp hit to AAC75946.1 (441 aa), 91% identity in aa 4 - 441. | Putative peptidase T; Cleaves the N-terminal amino acid of tripeptides. Hydrolyzes tripeptides containing N-terminal methionine, leucine, or phenylalanine. Displays little or no activity against dipeptides, N- blocked or C-blocked tripeptides, and tetrapeptides. Belongs to the peptidase M20B family. | 0.807 |