| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| STM4191 | pepE | STM4191 | STM4190 | Putative cytoplasmic protein. | (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. | 0.558 |
| iadA | pepE | STM4512 | STM4190 | Isoaspartyl dipeptidase; Catalyzes the hydrolytic cleavage of a subset of L- isoaspartyl (L-beta-aspartyl) dipeptides. Used to degrade proteins damaged by L-isoaspartyl residues formation. | (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. | 0.903 |
| iadA | ybiK | STM4512 | STM0847 | Isoaspartyl dipeptidase; Catalyzes the hydrolytic cleavage of a subset of L- isoaspartyl (L-beta-aspartyl) dipeptides. Used to degrade proteins damaged by L-isoaspartyl residues formation. | Putative asparaginase; Degrades proteins damaged by L-isoaspartyl residue formation (also known as beta-Asp residues). Degrades L-isoaspartyl-containing di- and tripeptides. Acts best on iso-Asp-Leu, followed by iso-Asp-Ala, -His and to a lesser extent iso-Asp-Lys, -Phe and iso-Asp-Leu-Ala. Does not act on internal iso-Asp bonds (Als-iso-Asp-Leu-Ala). Does not act on alpha-Asp bonds. Has poor L-asparaginase activity. Belongs to the Ntn-hydrolase family. | 0.931 |
| pepE | STM4191 | STM4190 | STM4191 | (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 cytoplasmic protein. | 0.558 |
| pepE | iadA | STM4190 | STM4512 | (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. | Isoaspartyl dipeptidase; Catalyzes the hydrolytic cleavage of a subset of L- isoaspartyl (L-beta-aspartyl) dipeptides. Used to degrade proteins damaged by L-isoaspartyl residues formation. | 0.903 |
| 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 | priA | STM4190 | STM4095 | (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. | Primosomal protein N; Involved in the restart of stalled replication forks. Recognizes and binds the arrested nascent DNA chain at stalled replication forks. It can open the DNA duplex, via its helicase activity, and promote assembly of the primosome and loading of the major replicative helicase DnaB onto DNA; Belongs to the helicase family. PriA subfamily. | 0.658 |
| pepE | purN | STM4190 | STM2500 | (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. | Polyphosphate kinase; Catalyzes the transfer of a formyl group from 10- formyltetrahydrofolate to 5-phospho-ribosyl-glycinamide (GAR), producing 5-phospho-ribosyl-N-formylglycinamide (FGAR) and tetrahydrofolate. | 0.604 |
| pepE | sspA | STM4190 | STM3342 | (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. | Stringent starvation protein A; Regulator of transcription; similar to E. coli regulator of transcription; stringent starvation protein A (AAC76261.1); Blastp hit to AAC76261.1 (212 aa), 98% identity in aa 1 - 211; Belongs to the GST superfamily. | 0.509 |
| pepE | ybeK | STM4190 | STM0661 | (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 purine nucleoside hydrolase; Hydrolyzes cytidine or uridine to ribose and cytosine or uracil, respectively. | 0.788 |
| pepE | ybiK | STM4190 | STM0847 | (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 asparaginase; Degrades proteins damaged by L-isoaspartyl residue formation (also known as beta-Asp residues). Degrades L-isoaspartyl-containing di- and tripeptides. Acts best on iso-Asp-Leu, followed by iso-Asp-Ala, -His and to a lesser extent iso-Asp-Lys, -Phe and iso-Asp-Leu-Ala. Does not act on internal iso-Asp bonds (Als-iso-Asp-Leu-Ala). Does not act on alpha-Asp bonds. Has poor L-asparaginase activity. Belongs to the Ntn-hydrolase family. | 0.583 |
| pepE | yjjU | STM4190 | STM4563 | (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 phosphoesterase; Similar to E. coli orf, hypothetical protein (AAC77330.1); Blastp hit to AAC77330.1 (357 aa), 85% identity in aa 1 - 357. | 0.716 |
| pepE | ytjA | STM4190 | STM4562 | (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 inner membrane protein. | 0.572 |
| pepT | pepE | STM1227 | STM4190 | 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. | (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. | 0.578 |
| priA | pepE | STM4095 | STM4190 | Primosomal protein N; Involved in the restart of stalled replication forks. Recognizes and binds the arrested nascent DNA chain at stalled replication forks. It can open the DNA duplex, via its helicase activity, and promote assembly of the primosome and loading of the major replicative helicase DnaB onto DNA; Belongs to the helicase family. PriA subfamily. | (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. | 0.658 |
| priA | ybeK | STM4095 | STM0661 | Primosomal protein N; Involved in the restart of stalled replication forks. Recognizes and binds the arrested nascent DNA chain at stalled replication forks. It can open the DNA duplex, via its helicase activity, and promote assembly of the primosome and loading of the major replicative helicase DnaB onto DNA; Belongs to the helicase family. PriA subfamily. | Putative purine nucleoside hydrolase; Hydrolyzes cytidine or uridine to ribose and cytosine or uracil, respectively. | 0.895 |
| priA | yjjU | STM4095 | STM4563 | Primosomal protein N; Involved in the restart of stalled replication forks. Recognizes and binds the arrested nascent DNA chain at stalled replication forks. It can open the DNA duplex, via its helicase activity, and promote assembly of the primosome and loading of the major replicative helicase DnaB onto DNA; Belongs to the helicase family. PriA subfamily. | Putative phosphoesterase; Similar to E. coli orf, hypothetical protein (AAC77330.1); Blastp hit to AAC77330.1 (357 aa), 85% identity in aa 1 - 357. | 0.892 |
| priA | ytjA | STM4095 | STM4562 | Primosomal protein N; Involved in the restart of stalled replication forks. Recognizes and binds the arrested nascent DNA chain at stalled replication forks. It can open the DNA duplex, via its helicase activity, and promote assembly of the primosome and loading of the major replicative helicase DnaB onto DNA; Belongs to the helicase family. PriA subfamily. | Putative inner membrane protein. | 0.762 |
| purN | pepE | STM2500 | STM4190 | Polyphosphate kinase; Catalyzes the transfer of a formyl group from 10- formyltetrahydrofolate to 5-phospho-ribosyl-glycinamide (GAR), producing 5-phospho-ribosyl-N-formylglycinamide (FGAR) and tetrahydrofolate. | (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. | 0.604 |
| sspA | pepE | STM3342 | STM4190 | Stringent starvation protein A; Regulator of transcription; similar to E. coli regulator of transcription; stringent starvation protein A (AAC76261.1); Blastp hit to AAC76261.1 (212 aa), 98% identity in aa 1 - 211; Belongs to the GST superfamily. | (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. | 0.509 |
STRING v12.5 is now available!
