node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
EIC29018.1 | EIC29478.1 | Metal_1209 | Metal_1708 | Molybdate ABC transporter, permease protein; Part of the binding-protein-dependent transport system for molybdenum; probably responsible for the translocation of the substrate across the membrane; Belongs to the binding-protein-dependent transport system permease family. CysTW subfamily. | ABC-type antimicrobial peptide transport system, ATPase component; PFAM: ABC transporter. | 0.752 |
EIC29107.1 | EIC29478.1 | Metal_1309 | Metal_1708 | PFAM: Predicted permease; TIGRFAM: lipoprotein releasing system, transmembrane protein, LolC/E family. | ABC-type antimicrobial peptide transport system, ATPase component; PFAM: ABC transporter. | 0.942 |
EIC29107.1 | lolA | Metal_1309 | Metal_1876 | PFAM: Predicted permease; TIGRFAM: lipoprotein releasing system, transmembrane protein, LolC/E family. | Periplasmic chaperone LolA; Participates in the translocation of lipoproteins from the inner membrane to the outer membrane. Only forms a complex with a lipoprotein if the residue after the N-terminal Cys is not an aspartate (The Asp acts as a targeting signal to indicate that the lipoprotein should stay in the inner membrane). | 0.958 |
EIC29107.1 | macB | Metal_1309 | Metal_1824 | PFAM: Predicted permease; TIGRFAM: lipoprotein releasing system, transmembrane protein, LolC/E family. | ABC-type antimicrobial peptide transport system, ATPase component; Part of the tripartite efflux system MacAB-TolC. MacB is a non-canonical ABC transporter that contains transmembrane domains (TMD), which form a pore in the inner membrane, and an ATP-binding domain (NBD), which is responsible for energy generation. Confers resistance against macrolides. | 0.983 |
EIC29476.1 | EIC29477.1 | Metal_1706 | Metal_1707 | Putative secreted hydrolase; PFAM: Hydroxyneurosporene synthase (CrtC). | PFAM: Predicted permease. | 0.978 |
EIC29476.1 | EIC29478.1 | Metal_1706 | Metal_1708 | Putative secreted hydrolase; PFAM: Hydroxyneurosporene synthase (CrtC). | ABC-type antimicrobial peptide transport system, ATPase component; PFAM: ABC transporter. | 0.859 |
EIC29477.1 | EIC29476.1 | Metal_1707 | Metal_1706 | PFAM: Predicted permease. | Putative secreted hydrolase; PFAM: Hydroxyneurosporene synthase (CrtC). | 0.978 |
EIC29477.1 | EIC29478.1 | Metal_1707 | Metal_1708 | PFAM: Predicted permease. | ABC-type antimicrobial peptide transport system, ATPase component; PFAM: ABC transporter. | 0.994 |
EIC29477.1 | lolA | Metal_1707 | Metal_1876 | PFAM: Predicted permease. | Periplasmic chaperone LolA; Participates in the translocation of lipoproteins from the inner membrane to the outer membrane. Only forms a complex with a lipoprotein if the residue after the N-terminal Cys is not an aspartate (The Asp acts as a targeting signal to indicate that the lipoprotein should stay in the inner membrane). | 0.918 |
EIC29477.1 | macB | Metal_1707 | Metal_1824 | PFAM: Predicted permease. | ABC-type antimicrobial peptide transport system, ATPase component; Part of the tripartite efflux system MacAB-TolC. MacB is a non-canonical ABC transporter that contains transmembrane domains (TMD), which form a pore in the inner membrane, and an ATP-binding domain (NBD), which is responsible for energy generation. Confers resistance against macrolides. | 0.983 |
EIC29478.1 | EIC29018.1 | Metal_1708 | Metal_1209 | ABC-type antimicrobial peptide transport system, ATPase component; PFAM: ABC transporter. | Molybdate ABC transporter, permease protein; Part of the binding-protein-dependent transport system for molybdenum; probably responsible for the translocation of the substrate across the membrane; Belongs to the binding-protein-dependent transport system permease family. CysTW subfamily. | 0.752 |
EIC29478.1 | EIC29107.1 | Metal_1708 | Metal_1309 | ABC-type antimicrobial peptide transport system, ATPase component; PFAM: ABC transporter. | PFAM: Predicted permease; TIGRFAM: lipoprotein releasing system, transmembrane protein, LolC/E family. | 0.942 |
EIC29478.1 | EIC29476.1 | Metal_1708 | Metal_1706 | ABC-type antimicrobial peptide transport system, ATPase component; PFAM: ABC transporter. | Putative secreted hydrolase; PFAM: Hydroxyneurosporene synthase (CrtC). | 0.859 |
EIC29478.1 | EIC29477.1 | Metal_1708 | Metal_1707 | ABC-type antimicrobial peptide transport system, ATPase component; PFAM: ABC transporter. | PFAM: Predicted permease. | 0.994 |
EIC29478.1 | EIC30403.1 | Metal_1708 | Metal_2697 | ABC-type antimicrobial peptide transport system, ATPase component; PFAM: ABC transporter. | ABC-type nitrate/sulfonate/bicarbonate transport system, periplasmic component; PFAM: NMT1/THI5 like. | 0.855 |
EIC29478.1 | EIC30808.1 | Metal_1708 | Metal_3132 | ABC-type antimicrobial peptide transport system, ATPase component; PFAM: ABC transporter. | ABC-type antimicrobial peptide transport system, permease component; PFAM: Predicted permease. | 0.728 |
EIC29478.1 | EIC31306.1 | Metal_1708 | Metal_3659 | ABC-type antimicrobial peptide transport system, ATPase component; PFAM: ABC transporter. | ABC-type antimicrobial peptide transport system, permease component; PFAM: Predicted permease. | 0.977 |
EIC29478.1 | EIC31307.1 | Metal_1708 | Metal_3660 | ABC-type antimicrobial peptide transport system, ATPase component; PFAM: ABC transporter. | ABC-type antimicrobial peptide transport system, permease component; PFAM: Predicted permease. | 0.976 |
EIC29478.1 | lolA | Metal_1708 | Metal_1876 | ABC-type antimicrobial peptide transport system, ATPase component; PFAM: ABC transporter. | Periplasmic chaperone LolA; Participates in the translocation of lipoproteins from the inner membrane to the outer membrane. Only forms a complex with a lipoprotein if the residue after the N-terminal Cys is not an aspartate (The Asp acts as a targeting signal to indicate that the lipoprotein should stay in the inner membrane). | 0.934 |
EIC29478.1 | macB | Metal_1708 | Metal_1824 | ABC-type antimicrobial peptide transport system, ATPase component; PFAM: ABC transporter. | ABC-type antimicrobial peptide transport system, ATPase component; Part of the tripartite efflux system MacAB-TolC. MacB is a non-canonical ABC transporter that contains transmembrane domains (TMD), which form a pore in the inner membrane, and an ATP-binding domain (NBD), which is responsible for energy generation. Confers resistance against macrolides. | 0.802 |