TonB-like protein; TonB is an energy-transducer for TonB-dependent receptors of Gram-negative bacteria. Energy flows from the cytoplasmic membrane into the outer membrane via a complex consisting of TonB, ExbB and ExbD proteins which are anchored in the cytoplasmic membrane. TonB interacts with outer membrane receptor proteins that carry out high-affinity binding and energy dependent uptake into the periplasmic space of specific substrates; Although belonging to the TonB family, this protein seems to contain a signal peptide cleaved between the residues 17 and 18, which is unsual for c [...]

Beta-helix fold protein; This protein likely adopts a right handed parallel beta-helix fold. Displays also a C-terminal PKD domain; Signal peptide cleaved between the residues 28 and 29; Localized in the periplasmic space; Function unclear.

TonB-like protein; TonB is an energy-transducer for TonB-dependent receptors of Gram-negative bacteria. Energy flows from the cytoplasmic membrane into the outer membrane via a complex consisting of TonB, ExbB and ExbD proteins which are anchored in the cytoplasmic membrane. TonB interacts with outer membrane receptor proteins that carry out high-affinity binding and energy dependent uptake into the periplasmic space of specific substrates; Although belonging to the TonB family, this protein seems to contain a signal peptide cleaved between the residues 17 and 18, which is unsual for c [...]

Modular protein containing a N-terminal domain adopting a parallel beta-helix fold and a C-terminal carbohydrate binding module of the family 13 (CBM13). The N-terminal domain is distantly related to the polysaccharide lyases of the family 9 (PL9). Features a signal peptide cleaved between residues 26 and 27. Localized in the periplasm; Specificity unclear.

TonB-like protein; TonB is an energy-transducer for TonB-dependent receptors of Gram-negative bacteria. Energy flows from the cytoplasmic membrane into the outer membrane via a complex consisting of TonB, ExbB and ExbD proteins which are anchored in the cytoplasmic membrane. TonB interacts with outer membrane receptor proteins that carry out high-affinity binding and energy dependent uptake into the periplasmic space of specific substrates; Although belonging to the TonB family, this protein seems to contain a signal peptide cleaved between the residues 17 and 18, which is unsual for c [...]

TonB-dependent Transducer; Protein localized in the outer membrane involved in uptake of macromolecules that are too large to diffuse via the outer membrane porins; The presence of an additional N-terminal extension (Secretin/TonB (STN) domain (50-101)) that probably interacts with an anti-sigma factor, would be responsible of the signal transduction; Contains a carboxypeptidase regulatory domain (106-180) and a Plug module (197-327) acting as the channel gate; The signal peptide is cleaved between the residue 22 and 23; Family membership.

TonB-like protein; TonB is an energy-transducer for TonB-dependent receptors of Gram-negative bacteria. Energy flows from the cytoplasmic membrane into the outer membrane via a complex consisting of TonB, ExbB and ExbD proteins which are anchored in the cytoplasmic membrane. TonB interacts with outer membrane receptor proteins that carry out high-affinity binding and energy dependent uptake into the periplasmic space of specific substrates; Although belonging to the TonB family, this protein seems to contain a signal peptide cleaved between the residues 17 and 18, which is unsual for c [...]

TonB-dependent Receptor; Protein localized in the outer membrane involved in uptake of macromolecules that are too large to diffuse via the outer membrane porins channels or are encountered at very low concentrations; Contains a carboxypeptidase regulatory domain (34-108) and the Plug module (124-231) acting as a channel gate; The signal peptide is cleaved between the residues 30 and 31; Family membership.

TonB-like protein; TonB is an energy-transducer for TonB-dependent receptors of Gram-negative bacteria. Energy flows from the cytoplasmic membrane into the outer membrane via a complex consisting of TonB, ExbB and ExbD proteins which are anchored in the cytoplasmic membrane. TonB interacts with outer membrane receptor proteins that carry out high-affinity binding and energy dependent uptake into the periplasmic space of specific substrates; Although belonging to the TonB family, this protein seems to contain a signal peptide cleaved between the residues 17 and 18, which is unsual for c [...]

TonB-dependent Receptor; Protein localized in the outer membrane involved in uptake of macromolecules that are too large to diffuse via the outer membrane porins channels or are encountered at very low concentrations; Contains a carboxypeptidase regulatory domain (22-108) and the Plug module (122-217) acting as a channel gate; The signal peptide is putatively cleaved between the residues 25 and 26; Family membership.

TonB-like protein; TonB is an energy-transducer for TonB-dependent receptors of Gram-negative bacteria. Energy flows from the cytoplasmic membrane into the outer membrane via a complex consisting of TonB, ExbB and ExbD proteins which are anchored in the cytoplasmic membrane. TonB interacts with outer membrane receptor proteins that carry out high-affinity binding and energy dependent uptake into the periplasmic space of specific substrates; Although belonging to the TonB family, this protein seems to contain a signal peptide cleaved between the residues 17 and 18, which is unsual for c [...]

ExbB is involved in the tonB-dependent energy-dependent transport of various receptor-bound substrates. ExbB protects ExbD from proteolytic degradation and functionally stabilizes tonB. TonB is coupled to the protomotive force by the ExbB/ExbD complex which is required for the energization of TonB; Contains four transmembrane segments; Belongs to the ExbB/TolQ family; Signal peptide cleaved between residues 23 and 24; Localized in the cytoplasmic membrane; High confidence in function and specificity.

TonB-like protein; TonB is an energy-transducer for TonB-dependent receptors of Gram-negative bacteria. Energy flows from the cytoplasmic membrane into the outer membrane via a complex consisting of TonB, ExbB and ExbD proteins which are anchored in the cytoplasmic membrane. TonB interacts with outer membrane receptor proteins that carry out high-affinity binding and energy dependent uptake into the periplasmic space of specific substrates; Although belonging to the TonB family, this protein seems to contain a signal peptide cleaved between the residues 17 and 18, which is unsual for c [...]

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.

TonB-like protein; TonB is an energy-transducer for TonB-dependent receptors of Gram-negative bacteria. Energy flows from the cytoplasmic membrane into the outer membrane via a complex consisting of TonB, ExbB and ExbD proteins which are anchored in the cytoplasmic membrane. TonB interacts with outer membrane receptor proteins that carry out high-affinity binding and energy dependent uptake into the periplasmic space of specific substrates; Although belonging to the TonB family, this protein seems to contain a signal peptide cleaved between the residues 17 and 18, which is unsual for c [...]

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.

TonB-like protein; TonB is an energy-transducer for TonB-dependent receptors of Gram-negative bacteria. Energy flows from the cytoplasmic membrane into the outer membrane via a complex consisting of TonB, ExbB and ExbD proteins which are anchored in the cytoplasmic membrane. TonB interacts with outer membrane receptor proteins that carry out high-affinity binding and energy dependent uptake into the periplasmic space of specific substrates; Although belonging to the TonB family, this protein seems to contain a signal peptide cleaved between the residues 17 and 18, which is unsual for c [...]

TolQ, involved in the tonB-independent uptake of biopolymers, forms a complex with the proteins TolR. This complex energizes TolA from the potential energy of the ion electrochemical gradient. TolA energized, interacts with the outer membrane protein Pal (OprL). The Tol-Pal complex is required for maintaining outer membrane integrity, the transport (uptake) filamentous DNA and is the conduct for bacteriophages; Contains three transmembrane helices; Belongs to the exbB/tolQ family; Localized in the cytoplasmic membrane; High confidence in function and specificity.

TonB-like protein; TonB is an energy-transducer for TonB-dependent receptors of Gram-negative bacteria. Energy flows from the cytoplasmic membrane into the outer membrane via a complex consisting of TonB, ExbB and ExbD proteins which are anchored in the cytoplasmic membrane. TonB interacts with outer membrane receptor proteins that carry out high-affinity binding and energy dependent uptake into the periplasmic space of specific substrates; Although belonging to the TonB family, this protein seems to contain a signal peptide cleaved between the residues 17 and 18, which is unsual for c [...]

TolR, involved in the tonB-independent uptake of biopolymers, forms a complex with the proteins TolQ. This complex energizes TolA from the potential energy of the ion electrochemical gradient. TolA energized, interacts with the outer membrane protein Pal (OprL). The Tol-Pal complex is required for maintaining outer membrane integrity, the transport (uptake) filamentous DNA and is the conduct for bacteriophages; Contains a N-terminal transmembrane helix; Belongs to the exbD/tolR family; Localized in the cytoplasmic membrane; High confidence in function and specificity.

Beta-helix fold protein; This protein likely adopts a right handed parallel beta-helix fold. Displays also a C-terminal PKD domain; Signal peptide cleaved between the residues 28 and 29; Localized in the periplasmic space; Function unclear.

TonB-like protein; TonB is an energy-transducer for TonB-dependent receptors of Gram-negative bacteria. Energy flows from the cytoplasmic membrane into the outer membrane via a complex consisting of TonB, ExbB and ExbD proteins which are anchored in the cytoplasmic membrane. TonB interacts with outer membrane receptor proteins that carry out high-affinity binding and energy dependent uptake into the periplasmic space of specific substrates; Although belonging to the TonB family, this protein seems to contain a signal peptide cleaved between the residues 17 and 18, which is unsual for c [...]

Beta-helix fold protein; This protein likely adopts a right handed parallel beta-helix fold. Displays also a C-terminal PKD domain; Signal peptide cleaved between the residues 28 and 29; Localized in the periplasmic space; Function unclear.

Modular protein containing a N-terminal domain adopting a parallel beta-helix fold and a C-terminal carbohydrate binding module of the family 13 (CBM13). The N-terminal domain is distantly related to the polysaccharide lyases of the family 9 (PL9). Features a signal peptide cleaved between residues 26 and 27. Localized in the periplasm; Specificity unclear.

Modular protein containing a N-terminal domain adopting a parallel beta-helix fold and a C-terminal carbohydrate binding module of the family 13 (CBM13). The N-terminal domain is distantly related to the polysaccharide lyases of the family 9 (PL9). Features a signal peptide cleaved between residues 26 and 27. Localized in the periplasm; Specificity unclear.

TonB-like protein; TonB is an energy-transducer for TonB-dependent receptors of Gram-negative bacteria. Energy flows from the cytoplasmic membrane into the outer membrane via a complex consisting of TonB, ExbB and ExbD proteins which are anchored in the cytoplasmic membrane. TonB interacts with outer membrane receptor proteins that carry out high-affinity binding and energy dependent uptake into the periplasmic space of specific substrates; Although belonging to the TonB family, this protein seems to contain a signal peptide cleaved between the residues 17 and 18, which is unsual for c [...]

Modular protein containing a N-terminal domain adopting a parallel beta-helix fold and a C-terminal carbohydrate binding module of the family 13 (CBM13). The N-terminal domain is distantly related to the polysaccharide lyases of the family 9 (PL9). Features a signal peptide cleaved between residues 26 and 27. Localized in the periplasm; Specificity unclear.

Beta-helix fold protein; This protein likely adopts a right handed parallel beta-helix fold. Displays also a C-terminal PKD domain; Signal peptide cleaved between the residues 28 and 29; Localized in the periplasmic space; Function unclear.

TonB-dependent Transducer; Protein localized in the outer membrane involved in uptake of macromolecules that are too large to diffuse via the outer membrane porins; The presence of an additional N-terminal extension (Secretin/TonB (STN) domain (50-101)) that probably interacts with an anti-sigma factor, would be responsible of the signal transduction; Contains a carboxypeptidase regulatory domain (106-180) and a Plug module (197-327) acting as the channel gate; The signal peptide is cleaved between the residue 22 and 23; Family membership.

TonB-like protein; TonB is an energy-transducer for TonB-dependent receptors of Gram-negative bacteria. Energy flows from the cytoplasmic membrane into the outer membrane via a complex consisting of TonB, ExbB and ExbD proteins which are anchored in the cytoplasmic membrane. TonB interacts with outer membrane receptor proteins that carry out high-affinity binding and energy dependent uptake into the periplasmic space of specific substrates; Although belonging to the TonB family, this protein seems to contain a signal peptide cleaved between the residues 17 and 18, which is unsual for c [...]

TonB-dependent Receptor; Protein localized in the outer membrane involved in uptake of macromolecules that are too large to diffuse via the outer membrane porins channels or are encountered at very low concentrations; Contains a carboxypeptidase regulatory domain (34-108) and the Plug module (124-231) acting as a channel gate; The signal peptide is cleaved between the residues 30 and 31; Family membership.

TonB-like protein; TonB is an energy-transducer for TonB-dependent receptors of Gram-negative bacteria. Energy flows from the cytoplasmic membrane into the outer membrane via a complex consisting of TonB, ExbB and ExbD proteins which are anchored in the cytoplasmic membrane. TonB interacts with outer membrane receptor proteins that carry out high-affinity binding and energy dependent uptake into the periplasmic space of specific substrates; Although belonging to the TonB family, this protein seems to contain a signal peptide cleaved between the residues 17 and 18, which is unsual for c [...]

TonB-dependent Receptor; Protein localized in the outer membrane involved in uptake of macromolecules that are too large to diffuse via the outer membrane porins channels or are encountered at very low concentrations; Contains a carboxypeptidase regulatory domain (22-108) and the Plug module (122-217) acting as a channel gate; The signal peptide is putatively cleaved between the residues 25 and 26; Family membership.

TonB-like protein; TonB is an energy-transducer for TonB-dependent receptors of Gram-negative bacteria. Energy flows from the cytoplasmic membrane into the outer membrane via a complex consisting of TonB, ExbB and ExbD proteins which are anchored in the cytoplasmic membrane. TonB interacts with outer membrane receptor proteins that carry out high-affinity binding and energy dependent uptake into the periplasmic space of specific substrates; Although belonging to the TonB family, this protein seems to contain a signal peptide cleaved between the residues 17 and 18, which is unsual for c [...]

ExbB is involved in the tonB-dependent energy-dependent transport of various receptor-bound substrates. ExbB protects ExbD from proteolytic degradation and functionally stabilizes tonB. TonB is coupled to the protomotive force by the ExbB/ExbD complex which is required for the energization of TonB; Contains four transmembrane segments; Belongs to the ExbB/TolQ family; Signal peptide cleaved between residues 23 and 24; Localized in the cytoplasmic membrane; High confidence in function and specificity.

TonB-like protein; TonB is an energy-transducer for TonB-dependent receptors of Gram-negative bacteria. Energy flows from the cytoplasmic membrane into the outer membrane via a complex consisting of TonB, ExbB and ExbD proteins which are anchored in the cytoplasmic membrane. TonB interacts with outer membrane receptor proteins that carry out high-affinity binding and energy dependent uptake into the periplasmic space of specific substrates; Although belonging to the TonB family, this protein seems to contain a signal peptide cleaved between the residues 17 and 18, which is unsual for c [...]

ExbB is involved in the tonB-dependent energy-dependent transport of various receptor-bound substrates. ExbB protects ExbD from proteolytic degradation and functionally stabilizes tonB. TonB is coupled to the protomotive force by the ExbB/ExbD complex which is required for the energization of TonB; Contains four transmembrane segments; Belongs to the ExbB/TolQ family; Signal peptide cleaved between residues 23 and 24; Localized in the cytoplasmic membrane; High confidence in function and specificity.

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.

ExbB is involved in the tonB-dependent energy-dependent transport of various receptor-bound substrates. ExbB protects ExbD from proteolytic degradation and functionally stabilizes tonB. TonB is coupled to the protomotive force by the ExbB/ExbD complex which is required for the energization of TonB; Contains four transmembrane segments; Belongs to the ExbB/TolQ family; Signal peptide cleaved between residues 23 and 24; Localized in the cytoplasmic membrane; High confidence in function and specificity.

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.