| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| CAZ94149.1 | CAZ94150.1 | ZOBELLIA_76 | ZOBELLIA_77 | Lytic murein transglycosylase, family GH23; Lytic murein transglycosylase catalyzes the cleavage of the beta-1,4-glycosidic bond between N- acetylmuramic acid and N-acetylglucosamine residues, thereby conserving the energy in a newly synthesized 1,6- anhydrobond in the muramic acid residue. It belongs to the family 23 of the glycoside hydrolases. May play a role in recycling of muropeptides during cell elongation and/or cell division. Features a signal peptide cleaved between the residues 23 and 24. Localized in the periplasm; Specificity unclear. | Conserved hypothetical protein. Localized in the cytoplasm. | 0.504 |
| CAZ94149.1 | CAZ95718.1 | ZOBELLIA_76 | ZOBELLIA_1664 | Lytic murein transglycosylase, family GH23; Lytic murein transglycosylase catalyzes the cleavage of the beta-1,4-glycosidic bond between N- acetylmuramic acid and N-acetylglucosamine residues, thereby conserving the energy in a newly synthesized 1,6- anhydrobond in the muramic acid residue. It belongs to the family 23 of the glycoside hydrolases. May play a role in recycling of muropeptides during cell elongation and/or cell division. Features a signal peptide cleaved between the residues 23 and 24. Localized in the periplasm; Specificity unclear. | Conserved hypothetical membrane protein; Protein distantly related to LolC, an permease involved in the ATP-dependent transport system lolCDE responsible for the release of lipoproteins targeted to the outer membrane from the inner membrane; Contains four transmembrane helices; Localized in the cytoplasmic membrane; Family membership. | 0.501 |
| CAZ94149.1 | CAZ95779.1 | ZOBELLIA_76 | ZOBELLIA_1726 | Lytic murein transglycosylase, family GH23; Lytic murein transglycosylase catalyzes the cleavage of the beta-1,4-glycosidic bond between N- acetylmuramic acid and N-acetylglucosamine residues, thereby conserving the energy in a newly synthesized 1,6- anhydrobond in the muramic acid residue. It belongs to the family 23 of the glycoside hydrolases. May play a role in recycling of muropeptides during cell elongation and/or cell division. Features a signal peptide cleaved between the residues 23 and 24. Localized in the periplasm; Specificity unclear. | Conserved hypothetical membrane protein; Contains a putative lipoprotein signal peptide cleaved between the residues 17 and 18; Possibly localized in the outer membrane; Conserved hypothetical protein. | 0.554 |
| CAZ94149.1 | clsA1 | ZOBELLIA_76 | ZOBELLIA_75 | Lytic murein transglycosylase, family GH23; Lytic murein transglycosylase catalyzes the cleavage of the beta-1,4-glycosidic bond between N- acetylmuramic acid and N-acetylglucosamine residues, thereby conserving the energy in a newly synthesized 1,6- anhydrobond in the muramic acid residue. It belongs to the family 23 of the glycoside hydrolases. May play a role in recycling of muropeptides during cell elongation and/or cell division. Features a signal peptide cleaved between the residues 23 and 24. Localized in the periplasm; Specificity unclear. | Cardiolipin synthetase; Catalyzes the reversible phosphatidyl group transfer from one phosphatidylglycerol molecule to another to form cardiolipin (CL) (diphosphatidylglycerol) and glycerol. | 0.550 |
| CAZ94149.1 | exbD1 | ZOBELLIA_76 | ZOBELLIA_2334 | Lytic murein transglycosylase, family GH23; Lytic murein transglycosylase catalyzes the cleavage of the beta-1,4-glycosidic bond between N- acetylmuramic acid and N-acetylglucosamine residues, thereby conserving the energy in a newly synthesized 1,6- anhydrobond in the muramic acid residue. It belongs to the family 23 of the glycoside hydrolases. May play a role in recycling of muropeptides during cell elongation and/or cell division. Features a signal peptide cleaved between the residues 23 and 24. Localized in the periplasm; Specificity unclear. | ExbD is involved in the tonB-dependent energy-dependent transport of various receptor-bound substrates. ExbD forms a complex with ExbB. This complex is required for the efficient energization of tonB from the protomotive force; Contains a N-terminal transmembrane helix; Belongs to the exbD/tolR family; Localized in the cytoplasmic membrane; High confidence in function and specificity. | 0.547 |
| CAZ94149.1 | exbD2 | ZOBELLIA_76 | ZOBELLIA_2335 | Lytic murein transglycosylase, family GH23; Lytic murein transglycosylase catalyzes the cleavage of the beta-1,4-glycosidic bond between N- acetylmuramic acid and N-acetylglucosamine residues, thereby conserving the energy in a newly synthesized 1,6- anhydrobond in the muramic acid residue. It belongs to the family 23 of the glycoside hydrolases. May play a role in recycling of muropeptides during cell elongation and/or cell division. Features a signal peptide cleaved between the residues 23 and 24. Localized in the periplasm; Specificity unclear. | ExbD is involved in the tonB-dependent energy-dependent transport of various receptor-bound substrates. ExbD forms a complex with ExbB. This complex is required for the efficient energization of tonB from the protomotive force; Contains a N-terminal transmembrane helix; Belongs to the exbD/tolR family; Localized in the cytoplasmic membrane; High confidence in function and specificity. | 0.540 |
| CAZ94149.1 | mrdA | ZOBELLIA_76 | ZOBELLIA_1175 | Lytic murein transglycosylase, family GH23; Lytic murein transglycosylase catalyzes the cleavage of the beta-1,4-glycosidic bond between N- acetylmuramic acid and N-acetylglucosamine residues, thereby conserving the energy in a newly synthesized 1,6- anhydrobond in the muramic acid residue. It belongs to the family 23 of the glycoside hydrolases. May play a role in recycling of muropeptides during cell elongation and/or cell division. Features a signal peptide cleaved between the residues 23 and 24. Localized in the periplasm; Specificity unclear. | Penicillin-binding protein 2, Family GT51; PBP-2 is responsible for the determination of the rod shape of the cel. Synthetizes the cross-linked peptidoglycan from the lipid intermediates; Contains in its N-terminal half part a transmembrane segment and an penicillin insensitive transglycosylase domain (formation of linear glycan strands). In its C-terminal half part, a penicillin- sensitive transpeptidase domain (cross-linking of the peptide subunits) is present; Belongs to the family 51 of glycosyl transferases (GT51); Except for the cytoplasmic membrane anchor region, The bulk of the [...] | 0.586 |
| CAZ94149.1 | pbp1A | ZOBELLIA_76 | ZOBELLIA_1807 | Lytic murein transglycosylase, family GH23; Lytic murein transglycosylase catalyzes the cleavage of the beta-1,4-glycosidic bond between N- acetylmuramic acid and N-acetylglucosamine residues, thereby conserving the energy in a newly synthesized 1,6- anhydrobond in the muramic acid residue. It belongs to the family 23 of the glycoside hydrolases. May play a role in recycling of muropeptides during cell elongation and/or cell division. Features a signal peptide cleaved between the residues 23 and 24. Localized in the periplasm; Specificity unclear. | Penicillin-binding protein 1A, family GT51; Penicillin-binding protein 1A is a class A PBP involved in the synthesis of cross-linked peptidoglycan from the lipid II intermediates. The enzyme has a penicillin-insensitive transglycosylase N-terminal domain (formation of linear glycan strands) and a penicillin-sensitive transpeptidase C-terminal domain (cross-linking of the peptide subunits). The N-terminal domain belongs to the family 51 of the glycosyltransferases. Features an uncleaved signal peptide. Localized in the periplasm, anchored to the cytoplasmic membrane; High confidence in [...] | 0.465 |
| CAZ94149.1 | tonB1 | ZOBELLIA_76 | ZOBELLIA_861 | Lytic murein transglycosylase, family GH23; Lytic murein transglycosylase catalyzes the cleavage of the beta-1,4-glycosidic bond between N- acetylmuramic acid and N-acetylglucosamine residues, thereby conserving the energy in a newly synthesized 1,6- anhydrobond in the muramic acid residue. It belongs to the family 23 of the glycoside hydrolases. May play a role in recycling of muropeptides during cell elongation and/or cell division. Features a signal peptide cleaved between the residues 23 and 24. Localized in the periplasm; Specificity unclear. | TonB protein; Interacts with outer membrane receptor proteins that carry out high-affinity binding and energy dependent uptake into the periplasmic space of specific substrates. It could act to transduce energy from the cytoplasmic membrane to specific energy-requiring processes in the outer membrane, resulting in the release into the periplasm of ligands bound by these outer membrane proteins. Belongs to the TonB family. | 0.596 |
| CAZ94149.1 | tonB2 | ZOBELLIA_76 | ZOBELLIA_2380 | Lytic murein transglycosylase, family GH23; Lytic murein transglycosylase catalyzes the cleavage of the beta-1,4-glycosidic bond between N- acetylmuramic acid and N-acetylglucosamine residues, thereby conserving the energy in a newly synthesized 1,6- anhydrobond in the muramic acid residue. It belongs to the family 23 of the glycoside hydrolases. May play a role in recycling of muropeptides during cell elongation and/or cell division. Features a signal peptide cleaved between the residues 23 and 24. Localized in the periplasm; Specificity unclear. | TonB protein; Interacts with outer membrane receptor proteins that carry out high-affinity binding and energy dependent uptake into the periplasmic space of specific substrates. It could act to transduce energy from the cytoplasmic membrane to specific energy-requiring processes in the outer membrane, resulting in the release into the periplasm of ligands bound by these outer membrane proteins. Belongs to the TonB family. | 0.556 |
| CAZ94150.1 | CAZ94149.1 | ZOBELLIA_77 | ZOBELLIA_76 | Conserved hypothetical protein. Localized in the cytoplasm. | Lytic murein transglycosylase, family GH23; Lytic murein transglycosylase catalyzes the cleavage of the beta-1,4-glycosidic bond between N- acetylmuramic acid and N-acetylglucosamine residues, thereby conserving the energy in a newly synthesized 1,6- anhydrobond in the muramic acid residue. It belongs to the family 23 of the glycoside hydrolases. May play a role in recycling of muropeptides during cell elongation and/or cell division. Features a signal peptide cleaved between the residues 23 and 24. Localized in the periplasm; Specificity unclear. | 0.504 |
| CAZ95718.1 | CAZ94149.1 | ZOBELLIA_1664 | ZOBELLIA_76 | Conserved hypothetical membrane protein; Protein distantly related to LolC, an permease involved in the ATP-dependent transport system lolCDE responsible for the release of lipoproteins targeted to the outer membrane from the inner membrane; Contains four transmembrane helices; Localized in the cytoplasmic membrane; Family membership. | Lytic murein transglycosylase, family GH23; Lytic murein transglycosylase catalyzes the cleavage of the beta-1,4-glycosidic bond between N- acetylmuramic acid and N-acetylglucosamine residues, thereby conserving the energy in a newly synthesized 1,6- anhydrobond in the muramic acid residue. It belongs to the family 23 of the glycoside hydrolases. May play a role in recycling of muropeptides during cell elongation and/or cell division. Features a signal peptide cleaved between the residues 23 and 24. Localized in the periplasm; Specificity unclear. | 0.501 |
| CAZ95779.1 | CAZ94149.1 | ZOBELLIA_1726 | ZOBELLIA_76 | Conserved hypothetical membrane protein; Contains a putative lipoprotein signal peptide cleaved between the residues 17 and 18; Possibly localized in the outer membrane; Conserved hypothetical protein. | Lytic murein transglycosylase, family GH23; Lytic murein transglycosylase catalyzes the cleavage of the beta-1,4-glycosidic bond between N- acetylmuramic acid and N-acetylglucosamine residues, thereby conserving the energy in a newly synthesized 1,6- anhydrobond in the muramic acid residue. It belongs to the family 23 of the glycoside hydrolases. May play a role in recycling of muropeptides during cell elongation and/or cell division. Features a signal peptide cleaved between the residues 23 and 24. Localized in the periplasm; Specificity unclear. | 0.554 |
| CAZ95779.1 | exbD1 | ZOBELLIA_1726 | ZOBELLIA_2334 | Conserved hypothetical membrane protein; Contains a putative lipoprotein signal peptide cleaved between the residues 17 and 18; Possibly localized in the outer membrane; Conserved hypothetical protein. | ExbD is involved in the tonB-dependent energy-dependent transport of various receptor-bound substrates. ExbD forms a complex with ExbB. This complex is required for the efficient energization of tonB from the protomotive force; Contains a N-terminal transmembrane helix; Belongs to the exbD/tolR family; Localized in the cytoplasmic membrane; High confidence in function and specificity. | 0.778 |
| CAZ95779.1 | exbD2 | ZOBELLIA_1726 | ZOBELLIA_2335 | Conserved hypothetical membrane protein; Contains a putative lipoprotein signal peptide cleaved between the residues 17 and 18; Possibly localized in the outer membrane; Conserved hypothetical protein. | ExbD is involved in the tonB-dependent energy-dependent transport of various receptor-bound substrates. ExbD forms a complex with ExbB. This complex is required for the efficient energization of tonB from the protomotive force; Contains a N-terminal transmembrane helix; Belongs to the exbD/tolR family; Localized in the cytoplasmic membrane; High confidence in function and specificity. | 0.778 |
| CAZ95779.1 | pbp1A | ZOBELLIA_1726 | ZOBELLIA_1807 | Conserved hypothetical membrane protein; Contains a putative lipoprotein signal peptide cleaved between the residues 17 and 18; Possibly localized in the outer membrane; Conserved hypothetical protein. | Penicillin-binding protein 1A, family GT51; Penicillin-binding protein 1A is a class A PBP involved in the synthesis of cross-linked peptidoglycan from the lipid II intermediates. The enzyme has a penicillin-insensitive transglycosylase N-terminal domain (formation of linear glycan strands) and a penicillin-sensitive transpeptidase C-terminal domain (cross-linking of the peptide subunits). The N-terminal domain belongs to the family 51 of the glycosyltransferases. Features an uncleaved signal peptide. Localized in the periplasm, anchored to the cytoplasmic membrane; High confidence in [...] | 0.423 |
| CAZ95779.1 | tonB1 | ZOBELLIA_1726 | ZOBELLIA_861 | Conserved hypothetical membrane protein; Contains a putative lipoprotein signal peptide cleaved between the residues 17 and 18; Possibly localized in the outer membrane; Conserved hypothetical protein. | TonB protein; Interacts with outer membrane receptor proteins that carry out high-affinity binding and energy dependent uptake into the periplasmic space of specific substrates. It could act to transduce energy from the cytoplasmic membrane to specific energy-requiring processes in the outer membrane, resulting in the release into the periplasm of ligands bound by these outer membrane proteins. Belongs to the TonB family. | 0.766 |
| CAZ95779.1 | tonB2 | ZOBELLIA_1726 | ZOBELLIA_2380 | Conserved hypothetical membrane protein; Contains a putative lipoprotein signal peptide cleaved between the residues 17 and 18; Possibly localized in the outer membrane; Conserved hypothetical protein. | TonB protein; Interacts with outer membrane receptor proteins that carry out high-affinity binding and energy dependent uptake into the periplasmic space of specific substrates. It could act to transduce energy from the cytoplasmic membrane to specific energy-requiring processes in the outer membrane, resulting in the release into the periplasm of ligands bound by these outer membrane proteins. Belongs to the TonB family. | 0.767 |
| clsA1 | CAZ94149.1 | ZOBELLIA_75 | ZOBELLIA_76 | Cardiolipin synthetase; Catalyzes the reversible phosphatidyl group transfer from one phosphatidylglycerol molecule to another to form cardiolipin (CL) (diphosphatidylglycerol) and glycerol. | Lytic murein transglycosylase, family GH23; Lytic murein transglycosylase catalyzes the cleavage of the beta-1,4-glycosidic bond between N- acetylmuramic acid and N-acetylglucosamine residues, thereby conserving the energy in a newly synthesized 1,6- anhydrobond in the muramic acid residue. It belongs to the family 23 of the glycoside hydrolases. May play a role in recycling of muropeptides during cell elongation and/or cell division. Features a signal peptide cleaved between the residues 23 and 24. Localized in the periplasm; Specificity unclear. | 0.550 |
| exbD1 | CAZ94149.1 | ZOBELLIA_2334 | ZOBELLIA_76 | ExbD is involved in the tonB-dependent energy-dependent transport of various receptor-bound substrates. ExbD forms a complex with ExbB. This complex is required for the efficient energization of tonB from the protomotive force; Contains a N-terminal transmembrane helix; Belongs to the exbD/tolR family; Localized in the cytoplasmic membrane; High confidence in function and specificity. | Lytic murein transglycosylase, family GH23; Lytic murein transglycosylase catalyzes the cleavage of the beta-1,4-glycosidic bond between N- acetylmuramic acid and N-acetylglucosamine residues, thereby conserving the energy in a newly synthesized 1,6- anhydrobond in the muramic acid residue. It belongs to the family 23 of the glycoside hydrolases. May play a role in recycling of muropeptides during cell elongation and/or cell division. Features a signal peptide cleaved between the residues 23 and 24. Localized in the periplasm; Specificity unclear. | 0.547 |
STRING v12.5 is now available!
