| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| CF66_1022 | CF66_1036 | CF66_1022 | CF66_1036 | Hypothetical protein. | Hypothetical protein. | 0.728 |
| CF66_1022 | smg | CF66_1022 | CF66_3030 | Hypothetical protein. | Protein smg; Belongs to the Smg family. | 0.603 |
| CF66_1036 | CF66_1022 | CF66_1036 | CF66_1022 | Hypothetical protein. | Hypothetical protein. | 0.728 |
| CF66_1036 | CF66_2229 | CF66_1036 | CF66_2229 | Hypothetical protein. | Hypothetical protein. | 0.580 |
| CF66_1036 | ftsL | CF66_1036 | CF66_2232 | Hypothetical protein. | Cell division protein; Essential cell division protein. May link together the upstream cell division proteins, which are predominantly cytoplasmic, with the downstream cell division proteins, which are predominantly periplasmic. | 0.414 |
| CF66_1036 | smg | CF66_1036 | CF66_3030 | Hypothetical protein. | Protein smg; Belongs to the Smg family. | 0.721 |
| CF66_2229 | CF66_1036 | CF66_2229 | CF66_1036 | Hypothetical protein. | Hypothetical protein. | 0.580 |
| CF66_2229 | mreD | CF66_2229 | CF66_2227 | Hypothetical protein. | Rod shape-determining protein; Involved in formation of the rod shape of the cell. May also contribute to regulation of formation of penicillin-binding proteins. Belongs to the MreD family. | 0.753 |
| CF66_2229 | smg | CF66_2229 | CF66_3030 | Hypothetical protein. | Protein smg; Belongs to the Smg family. | 0.565 |
| def1 | fmt | CF66_3032 | CF66_3033 | Peptide deformylase 1; 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. | methionyl-tRNA formyltransferase; Attaches a formyl group to the free amino group of methionyl- tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus; Belongs to the Fmt family. | 0.981 |
| def1 | rsmB | CF66_3032 | CF66_3034 | Peptide deformylase 1; 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. | Ribosomal RNA small subunit methyltransferase B; Specifically methylates the cytosine at position 967 (m5C967) of 16S rRNA. | 0.705 |
| def1 | smg | CF66_3032 | CF66_3030 | Peptide deformylase 1; 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. | Protein smg; Belongs to the Smg family. | 0.601 |
| def1 | topA | CF66_3032 | CF66_0170 | Peptide deformylase 1; 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. | DNA topoisomerase 1; Releases the supercoiling and torsional tension of DNA, which is introduced during the DNA replication and transcription, by transiently cleaving and rejoining one strand of the DNA duplex. Introduces a single-strand break via transesterification at a target site in duplex DNA. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA- (5'-phosphotyrosyl)-enzyme intermediate and the expulsion of a 3'-OH DNA strand. The free DNA strand then undergoes passage around the unbroken strand, thus removing DNA supe [...] | 0.430 |
| fmt | def1 | CF66_3033 | CF66_3032 | methionyl-tRNA formyltransferase; Attaches a formyl group to the free amino group of methionyl- tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus; Belongs to the Fmt family. | Peptide deformylase 1; 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. | 0.981 |
| fmt | rsmB | CF66_3033 | CF66_3034 | methionyl-tRNA formyltransferase; Attaches a formyl group to the free amino group of methionyl- tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus; Belongs to the Fmt family. | Ribosomal RNA small subunit methyltransferase B; Specifically methylates the cytosine at position 967 (m5C967) of 16S rRNA. | 0.979 |
| fmt | smg | CF66_3033 | CF66_3030 | methionyl-tRNA formyltransferase; Attaches a formyl group to the free amino group of methionyl- tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus; Belongs to the Fmt family. | Protein smg; Belongs to the Smg family. | 0.565 |
| fmt | topA | CF66_3033 | CF66_0170 | methionyl-tRNA formyltransferase; Attaches a formyl group to the free amino group of methionyl- tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus; Belongs to the Fmt family. | DNA topoisomerase 1; Releases the supercoiling and torsional tension of DNA, which is introduced during the DNA replication and transcription, by transiently cleaving and rejoining one strand of the DNA duplex. Introduces a single-strand break via transesterification at a target site in duplex DNA. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA- (5'-phosphotyrosyl)-enzyme intermediate and the expulsion of a 3'-OH DNA strand. The free DNA strand then undergoes passage around the unbroken strand, thus removing DNA supe [...] | 0.768 |
| ftsL | CF66_1036 | CF66_2232 | CF66_1036 | Cell division protein; Essential cell division protein. May link together the upstream cell division proteins, which are predominantly cytoplasmic, with the downstream cell division proteins, which are predominantly periplasmic. | Hypothetical protein. | 0.414 |
| ftsL | mreD | CF66_2232 | CF66_2227 | Cell division protein; Essential cell division protein. May link together the upstream cell division proteins, which are predominantly cytoplasmic, with the downstream cell division proteins, which are predominantly periplasmic. | Rod shape-determining protein; Involved in formation of the rod shape of the cell. May also contribute to regulation of formation of penicillin-binding proteins. Belongs to the MreD family. | 0.460 |
| ftsL | smg | CF66_2232 | CF66_3030 | Cell division protein; Essential cell division protein. May link together the upstream cell division proteins, which are predominantly cytoplasmic, with the downstream cell division proteins, which are predominantly periplasmic. | Protein smg; Belongs to the Smg family. | 0.531 |