| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| lmrB | vmlR | BSU02670 | BSU05610 | Efflux transporter; Proton-dependent transporter. May mediate the efflux of lincomycin; Belongs to the major facilitator superfamily. EmrB family. | ATP-binding cassette efflux transporter; Recognizes and binds in the vacant E-site of ribosomes stalled by some peptidyltransferase center (PTC)-targeting antibiotics. Makes contact with the PTC and both ribosomal subunits. Induces conformational changes in the P-site, which allows it to dislodge the antibiotic from its PTC binding site. Binds to ribosomes either directly following translation initation or subsequent to E tRNA release during elongation. Involved in resistance to a narrow spectrum of antibiotics (the streptogramin A antibiotic virginiamycin M, the lincosamide antibiotic [...] | 0.684 |
| lmrB | yheJ | BSU02670 | BSU09700 | Efflux transporter; Proton-dependent transporter. May mediate the efflux of lincomycin; Belongs to the major facilitator superfamily. EmrB family. | Hypothetical protein; Evidence 5: No homology to any previously reported sequences. | 0.465 |
| nhaX | yheJ | BSU09690 | BSU09700 | Stress response protein, UspA family; Evidence 2b: Function of strongly homologous gene; factor. | Hypothetical protein; Evidence 5: No homology to any previously reported sequences. | 0.516 |
| vmlR | lmrB | BSU05610 | BSU02670 | ATP-binding cassette efflux transporter; Recognizes and binds in the vacant E-site of ribosomes stalled by some peptidyltransferase center (PTC)-targeting antibiotics. Makes contact with the PTC and both ribosomal subunits. Induces conformational changes in the P-site, which allows it to dislodge the antibiotic from its PTC binding site. Binds to ribosomes either directly following translation initation or subsequent to E tRNA release during elongation. Involved in resistance to a narrow spectrum of antibiotics (the streptogramin A antibiotic virginiamycin M, the lincosamide antibiotic [...] | Efflux transporter; Proton-dependent transporter. May mediate the efflux of lincomycin; Belongs to the major facilitator superfamily. EmrB family. | 0.684 |
| vmlR | yheH | BSU05610 | BSU09720 | ATP-binding cassette efflux transporter; Recognizes and binds in the vacant E-site of ribosomes stalled by some peptidyltransferase center (PTC)-targeting antibiotics. Makes contact with the PTC and both ribosomal subunits. Induces conformational changes in the P-site, which allows it to dislodge the antibiotic from its PTC binding site. Binds to ribosomes either directly following translation initation or subsequent to E tRNA release during elongation. Involved in resistance to a narrow spectrum of antibiotics (the streptogramin A antibiotic virginiamycin M, the lincosamide antibiotic [...] | Probable multidrug resistance ABC transporter ATP-binding/permease protein YheH; Involved in the transport of four structurally unrelated drugs, including doxorubicin and mitoxantrone. Transmembrane domains (TMD) form a pore in the membrane and the ATP-binding domain (NBD) is responsible for energy generation; Belongs to the ABC transporter superfamily. | 0.429 |
| vmlR | yheJ | BSU05610 | BSU09700 | ATP-binding cassette efflux transporter; Recognizes and binds in the vacant E-site of ribosomes stalled by some peptidyltransferase center (PTC)-targeting antibiotics. Makes contact with the PTC and both ribosomal subunits. Induces conformational changes in the P-site, which allows it to dislodge the antibiotic from its PTC binding site. Binds to ribosomes either directly following translation initation or subsequent to E tRNA release during elongation. Involved in resistance to a narrow spectrum of antibiotics (the streptogramin A antibiotic virginiamycin M, the lincosamide antibiotic [...] | Hypothetical protein; Evidence 5: No homology to any previously reported sequences. | 0.485 |
| yheH | vmlR | BSU09720 | BSU05610 | Probable multidrug resistance ABC transporter ATP-binding/permease protein YheH; Involved in the transport of four structurally unrelated drugs, including doxorubicin and mitoxantrone. Transmembrane domains (TMD) form a pore in the membrane and the ATP-binding domain (NBD) is responsible for energy generation; Belongs to the ABC transporter superfamily. | ATP-binding cassette efflux transporter; Recognizes and binds in the vacant E-site of ribosomes stalled by some peptidyltransferase center (PTC)-targeting antibiotics. Makes contact with the PTC and both ribosomal subunits. Induces conformational changes in the P-site, which allows it to dislodge the antibiotic from its PTC binding site. Binds to ribosomes either directly following translation initation or subsequent to E tRNA release during elongation. Involved in resistance to a narrow spectrum of antibiotics (the streptogramin A antibiotic virginiamycin M, the lincosamide antibiotic [...] | 0.429 |
| yheH | yheI | BSU09720 | BSU09710 | Probable multidrug resistance ABC transporter ATP-binding/permease protein YheH; Involved in the transport of four structurally unrelated drugs, including doxorubicin and mitoxantrone. Transmembrane domains (TMD) form a pore in the membrane and the ATP-binding domain (NBD) is responsible for energy generation; Belongs to the ABC transporter superfamily. | Probable multidrug resistance ABC transporter ATP-binding/permease protein YheI; Involved in the transport of four structurally unrelated drugs, including doxorubicin and mitoxantrone. Transmembrane domains (TMD) form a pore in the membrane and the ATP-binding domain (NBD) is responsible for energy generation; Belongs to the ABC transporter superfamily. | 0.999 |
| yheH | yheJ | BSU09720 | BSU09700 | Probable multidrug resistance ABC transporter ATP-binding/permease protein YheH; Involved in the transport of four structurally unrelated drugs, including doxorubicin and mitoxantrone. Transmembrane domains (TMD) form a pore in the membrane and the ATP-binding domain (NBD) is responsible for energy generation; Belongs to the ABC transporter superfamily. | Hypothetical protein; Evidence 5: No homology to any previously reported sequences. | 0.686 |
| yheI | yheH | BSU09710 | BSU09720 | Probable multidrug resistance ABC transporter ATP-binding/permease protein YheI; Involved in the transport of four structurally unrelated drugs, including doxorubicin and mitoxantrone. Transmembrane domains (TMD) form a pore in the membrane and the ATP-binding domain (NBD) is responsible for energy generation; Belongs to the ABC transporter superfamily. | Probable multidrug resistance ABC transporter ATP-binding/permease protein YheH; Involved in the transport of four structurally unrelated drugs, including doxorubicin and mitoxantrone. Transmembrane domains (TMD) form a pore in the membrane and the ATP-binding domain (NBD) is responsible for energy generation; Belongs to the ABC transporter superfamily. | 0.999 |
| yheI | yheJ | BSU09710 | BSU09700 | Probable multidrug resistance ABC transporter ATP-binding/permease protein YheI; Involved in the transport of four structurally unrelated drugs, including doxorubicin and mitoxantrone. Transmembrane domains (TMD) form a pore in the membrane and the ATP-binding domain (NBD) is responsible for energy generation; Belongs to the ABC transporter superfamily. | Hypothetical protein; Evidence 5: No homology to any previously reported sequences. | 0.682 |
| yheJ | lmrB | BSU09700 | BSU02670 | Hypothetical protein; Evidence 5: No homology to any previously reported sequences. | Efflux transporter; Proton-dependent transporter. May mediate the efflux of lincomycin; Belongs to the major facilitator superfamily. EmrB family. | 0.465 |
| yheJ | nhaX | BSU09700 | BSU09690 | Hypothetical protein; Evidence 5: No homology to any previously reported sequences. | Stress response protein, UspA family; Evidence 2b: Function of strongly homologous gene; factor. | 0.516 |
| yheJ | vmlR | BSU09700 | BSU05610 | Hypothetical protein; Evidence 5: No homology to any previously reported sequences. | ATP-binding cassette efflux transporter; Recognizes and binds in the vacant E-site of ribosomes stalled by some peptidyltransferase center (PTC)-targeting antibiotics. Makes contact with the PTC and both ribosomal subunits. Induces conformational changes in the P-site, which allows it to dislodge the antibiotic from its PTC binding site. Binds to ribosomes either directly following translation initation or subsequent to E tRNA release during elongation. Involved in resistance to a narrow spectrum of antibiotics (the streptogramin A antibiotic virginiamycin M, the lincosamide antibiotic [...] | 0.485 |
| yheJ | yheH | BSU09700 | BSU09720 | Hypothetical protein; Evidence 5: No homology to any previously reported sequences. | Probable multidrug resistance ABC transporter ATP-binding/permease protein YheH; Involved in the transport of four structurally unrelated drugs, including doxorubicin and mitoxantrone. Transmembrane domains (TMD) form a pore in the membrane and the ATP-binding domain (NBD) is responsible for energy generation; Belongs to the ABC transporter superfamily. | 0.686 |
| yheJ | yheI | BSU09700 | BSU09710 | Hypothetical protein; Evidence 5: No homology to any previously reported sequences. | Probable multidrug resistance ABC transporter ATP-binding/permease protein YheI; Involved in the transport of four structurally unrelated drugs, including doxorubicin and mitoxantrone. Transmembrane domains (TMD) form a pore in the membrane and the ATP-binding domain (NBD) is responsible for energy generation; Belongs to the ABC transporter superfamily. | 0.682 |