| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| defA | yfiV | BSU15720 | BSU08410 | Peptide deformylase; Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions (By similarity). | Putative transcriptional regulator (MarR family); Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pr: putative regulator. | 0.639 |
| defA | ykoM | BSU15720 | BSU13340 | Peptide deformylase; Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions (By similarity). | Putative transcriptional regulator (MarR family); Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pr: putative regulator. | 0.639 |
| defA | ypoP | BSU15720 | BSU21700 | Peptide deformylase; Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions (By similarity). | Putative transcriptional regulator (MarR family); Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pr: putative regulator. | 0.638 |
| defB | yfiV | BSU14560 | BSU08410 | Formylmethionine deformylase A; Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions. | Putative transcriptional regulator (MarR family); Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pr: putative regulator. | 0.582 |
| defB | ykoM | BSU14560 | BSU13340 | Formylmethionine deformylase A; Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions. | Putative transcriptional regulator (MarR family); Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pr: putative regulator. | 0.582 |
| defB | ypoP | BSU14560 | BSU21700 | Formylmethionine deformylase A; Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions. | Putative transcriptional regulator (MarR family); Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pr: putative regulator. | 0.588 |
| msrA | msrB | BSU21690 | BSU21680 | Peptide methionine S-sulfoxide reductase; Has an important function as a repair enzyme for proteins that have been inactivated by oxidation. Catalyzes the reversible oxidation-reduction of methionine sulfoxide in proteins to methionine. May deal with oxidative damage to alpha/beta-type SASP in spores. | Putative capsular polysaccharide biosynthesis enzyme fragment; Evidence 7: Gene remnant; putative enzyme. | 0.999 |
| msrA | ypoP | BSU21690 | BSU21700 | Peptide methionine S-sulfoxide reductase; Has an important function as a repair enzyme for proteins that have been inactivated by oxidation. Catalyzes the reversible oxidation-reduction of methionine sulfoxide in proteins to methionine. May deal with oxidative damage to alpha/beta-type SASP in spores. | Putative transcriptional regulator (MarR family); Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pr: putative regulator. | 0.569 |
| msrB | msrA | BSU21680 | BSU21690 | Putative capsular polysaccharide biosynthesis enzyme fragment; Evidence 7: Gene remnant; putative enzyme. | Peptide methionine S-sulfoxide reductase; Has an important function as a repair enzyme for proteins that have been inactivated by oxidation. Catalyzes the reversible oxidation-reduction of methionine sulfoxide in proteins to methionine. May deal with oxidative damage to alpha/beta-type SASP in spores. | 0.999 |
| msrB | ypoP | BSU21680 | BSU21700 | Putative capsular polysaccharide biosynthesis enzyme fragment; Evidence 7: Gene remnant; putative enzyme. | Putative transcriptional regulator (MarR family); Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pr: putative regulator. | 0.539 |
| yfiV | defA | BSU08410 | BSU15720 | Putative transcriptional regulator (MarR family); Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pr: putative regulator. | Peptide deformylase; Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions (By similarity). | 0.639 |
| yfiV | defB | BSU08410 | BSU14560 | Putative transcriptional regulator (MarR family); Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pr: putative regulator. | Formylmethionine deformylase A; Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions. | 0.582 |
| yfiV | yfmP | BSU08410 | BSU07390 | Putative transcriptional regulator (MarR family); Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pr: putative regulator. | Transcriptional regulator (MerR family) of metal efflux transporter expression; Repressor of the yfmOP operon. A mutation in yfmP leads to overexpression of yfmO, probably causing a decrease in cellular copper that is eventually responsible for a reduced copper induction of copZA. | 0.563 |
| yfiV | ypoP | BSU08410 | BSU21700 | Putative transcriptional regulator (MarR family); Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pr: putative regulator. | Putative transcriptional regulator (MarR family); Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pr: putative regulator. | 0.540 |
| yfiV | yraB | BSU08410 | BSU27000 | Putative transcriptional regulator (MarR family); Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pr: putative regulator. | Putative transcriptional regulator (MerR family); Transcriptional regulator involved in the response to aldehyde stress. Binds to the promoter region of the adhA-yraA operon, the yraC and its own promoter region; binding is unchanged in the presence of aldehydes. | 0.524 |
| yfiV | ywaE | BSU08410 | BSU38450 | Putative transcriptional regulator (MarR family); Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pr: putative regulator. | Putative transcriptional regulator (MarR family); Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pr: putative regulator. | 0.826 |
| yfmP | yfiV | BSU07390 | BSU08410 | Transcriptional regulator (MerR family) of metal efflux transporter expression; Repressor of the yfmOP operon. A mutation in yfmP leads to overexpression of yfmO, probably causing a decrease in cellular copper that is eventually responsible for a reduced copper induction of copZA. | Putative transcriptional regulator (MarR family); Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pr: putative regulator. | 0.563 |
| yfmP | ykoM | BSU07390 | BSU13340 | Transcriptional regulator (MerR family) of metal efflux transporter expression; Repressor of the yfmOP operon. A mutation in yfmP leads to overexpression of yfmO, probably causing a decrease in cellular copper that is eventually responsible for a reduced copper induction of copZA. | Putative transcriptional regulator (MarR family); Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pr: putative regulator. | 0.614 |
| yfmP | ypoP | BSU07390 | BSU21700 | Transcriptional regulator (MerR family) of metal efflux transporter expression; Repressor of the yfmOP operon. A mutation in yfmP leads to overexpression of yfmO, probably causing a decrease in cellular copper that is eventually responsible for a reduced copper induction of copZA. | Putative transcriptional regulator (MarR family); Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pr: putative regulator. | 0.561 |
| ykoM | defA | BSU13340 | BSU15720 | Putative transcriptional regulator (MarR family); Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pr: putative regulator. | Peptide deformylase; Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions (By similarity). | 0.639 |