Uptake of enterochelin; Involved in the TonB-dependent energy-dependent transport of various receptor-bound substrates. Protects ExbD from proteolytic degradation and functionally stabilizes TonB (By similarity).

tonB-dependent uptake of B colicins; similar to E. coli uptake of enterochelin; tonB-dependent uptake of B colicins (AAC76041.1); Blastp hit to AAC76041.1 (141 aa), 93% identity in aa 1 - 141.

Uptake of enterochelin; Involved in the TonB-dependent energy-dependent transport of various receptor-bound substrates. Protects ExbD from proteolytic degradation and functionally stabilizes TonB (By similarity).

TonB; Interacts with outer membrane receptor proteins that carry out high-affinity binding and energy dependent uptake into the periplasmic space of specific substrates such as cobalamin, and various iron compounds (such as iron dicitrate, enterochelin, aerobactin, etc.). In the absence of TonB these receptors bind their substrates but do not carry out active transport. TonB also interacts with some colicins and is involved in the energy-dependent, irreversible steps of bacteriophages phi 80 and T1 infection. It could act to transduce energy from the cytoplasmic membrane to specific en [...]

tonB-dependent uptake of B colicins; similar to E. coli uptake of enterochelin; tonB-dependent uptake of B colicins (AAC76041.1); Blastp hit to AAC76041.1 (141 aa), 93% identity in aa 1 - 141.

Uptake of enterochelin; Involved in the TonB-dependent energy-dependent transport of various receptor-bound substrates. Protects ExbD from proteolytic degradation and functionally stabilizes TonB (By similarity).

tonB-dependent uptake of B colicins; similar to E. coli uptake of enterochelin; tonB-dependent uptake of B colicins (AAC76041.1); Blastp hit to AAC76041.1 (141 aa), 93% identity in aa 1 - 141.

Putative membrane component hydrogenase; With TolR probably plays a role in maintaining the position of the peptidoglycan cell wall in the periplasm. Acts as a porin with low permeability that allows slow penetration of small solutes; an internal gate slows down solute passage.

tonB-dependent uptake of B colicins; similar to E. coli uptake of enterochelin; tonB-dependent uptake of B colicins (AAC76041.1); Blastp hit to AAC76041.1 (141 aa), 93% identity in aa 1 - 141.

TonB; Interacts with outer membrane receptor proteins that carry out high-affinity binding and energy dependent uptake into the periplasmic space of specific substrates such as cobalamin, and various iron compounds (such as iron dicitrate, enterochelin, aerobactin, etc.). In the absence of TonB these receptors bind their substrates but do not carry out active transport. TonB also interacts with some colicins and is involved in the energy-dependent, irreversible steps of bacteriophages phi 80 and T1 infection. It could act to transduce energy from the cytoplasmic membrane to specific en [...]

Major type 1 subunit fimbrin (pilin); Fimbriae (also called pili), polar filaments radiating from the surface of the bacterium to a length of 0.5-1.5 micrometers and numbering 100-300 per cell, enable bacteria to colonize the epithelium of specific host organs; Belongs to the fimbrial protein family.

Putative membrane component hydrogenase; With TolR probably plays a role in maintaining the position of the peptidoglycan cell wall in the periplasm. Acts as a porin with low permeability that allows slow penetration of small solutes; an internal gate slows down solute passage.

Histone-like protein, located in outer membrane; Molecular chaperone that interacts specifically with outer membrane proteins, thus maintaining the solubility of early folding intermediates during passage through the periplasm.

Putative membrane component hydrogenase; With TolR probably plays a role in maintaining the position of the peptidoglycan cell wall in the periplasm. Acts as a porin with low permeability that allows slow penetration of small solutes; an internal gate slows down solute passage.

Putative membrane component hydrogenase; With TolR probably plays a role in maintaining the position of the peptidoglycan cell wall in the periplasm. Acts as a porin with low permeability that allows slow penetration of small solutes; an internal gate slows down solute passage.

tonB-dependent uptake of B colicins; similar to E. coli uptake of enterochelin; tonB-dependent uptake of B colicins (AAC76041.1); Blastp hit to AAC76041.1 (141 aa), 93% identity in aa 1 - 141.

Putative membrane component hydrogenase; With TolR probably plays a role in maintaining the position of the peptidoglycan cell wall in the periplasm. Acts as a porin with low permeability that allows slow penetration of small solutes; an internal gate slows down solute passage.

Major type 1 subunit fimbrin (pilin); Fimbriae (also called pili), polar filaments radiating from the surface of the bacterium to a length of 0.5-1.5 micrometers and numbering 100-300 per cell, enable bacteria to colonize the epithelium of specific host organs; Belongs to the fimbrial protein family.

Putative membrane component hydrogenase; With TolR probably plays a role in maintaining the position of the peptidoglycan cell wall in the periplasm. Acts as a porin with low permeability that allows slow penetration of small solutes; an internal gate slows down solute passage.

Histone-like protein, located in outer membrane; Molecular chaperone that interacts specifically with outer membrane proteins, thus maintaining the solubility of early folding intermediates during passage through the periplasm.

Putative membrane component hydrogenase; With TolR probably plays a role in maintaining the position of the peptidoglycan cell wall in the periplasm. Acts as a porin with low permeability that allows slow penetration of small solutes; an internal gate slows down solute passage.

Superoxide dismutase; Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems; Belongs to the iron/manganese superoxide dismutase family.

Putative membrane component hydrogenase; With TolR probably plays a role in maintaining the position of the peptidoglycan cell wall in the periplasm. Acts as a porin with low permeability that allows slow penetration of small solutes; an internal gate slows down solute passage.

TonB; Interacts with outer membrane receptor proteins that carry out high-affinity binding and energy dependent uptake into the periplasmic space of specific substrates such as cobalamin, and various iron compounds (such as iron dicitrate, enterochelin, aerobactin, etc.). In the absence of TonB these receptors bind their substrates but do not carry out active transport. TonB also interacts with some colicins and is involved in the energy-dependent, irreversible steps of bacteriophages phi 80 and T1 infection. It could act to transduce energy from the cytoplasmic membrane to specific en [...]

Superoxide dismutase; Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems; Belongs to the iron/manganese superoxide dismutase family.

Putative membrane component hydrogenase; With TolR probably plays a role in maintaining the position of the peptidoglycan cell wall in the periplasm. Acts as a porin with low permeability that allows slow penetration of small solutes; an internal gate slows down solute passage.

Superoxide dismutase; Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems; Belongs to the iron/manganese superoxide dismutase family.

Copper/zinc superoxide dismutase; Destroys radicals which are normally produced within the cells and which are toxic to biological systems; Belongs to the Cu-Zn superoxide dismutase family.

Superoxide dismutase; Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems; Belongs to the iron/manganese superoxide dismutase family.

TonB; Interacts with outer membrane receptor proteins that carry out high-affinity binding and energy dependent uptake into the periplasmic space of specific substrates such as cobalamin, and various iron compounds (such as iron dicitrate, enterochelin, aerobactin, etc.). In the absence of TonB these receptors bind their substrates but do not carry out active transport. TonB also interacts with some colicins and is involved in the energy-dependent, irreversible steps of bacteriophages phi 80 and T1 infection. It could act to transduce energy from the cytoplasmic membrane to specific en [...]

Copper/zinc superoxide dismutase; Destroys radicals which are normally produced within the cells and which are toxic to biological systems; Belongs to the Cu-Zn superoxide dismutase family.

Superoxide dismutase; Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems; Belongs to the iron/manganese superoxide dismutase family.

TonB; Interacts with outer membrane receptor proteins that carry out high-affinity binding and energy dependent uptake into the periplasmic space of specific substrates such as cobalamin, and various iron compounds (such as iron dicitrate, enterochelin, aerobactin, etc.). In the absence of TonB these receptors bind their substrates but do not carry out active transport. TonB also interacts with some colicins and is involved in the energy-dependent, irreversible steps of bacteriophages phi 80 and T1 infection. It could act to transduce energy from the cytoplasmic membrane to specific en [...]

Uptake of enterochelin; Involved in the TonB-dependent energy-dependent transport of various receptor-bound substrates. Protects ExbD from proteolytic degradation and functionally stabilizes TonB (By similarity).

TonB; Interacts with outer membrane receptor proteins that carry out high-affinity binding and energy dependent uptake into the periplasmic space of specific substrates such as cobalamin, and various iron compounds (such as iron dicitrate, enterochelin, aerobactin, etc.). In the absence of TonB these receptors bind their substrates but do not carry out active transport. TonB also interacts with some colicins and is involved in the energy-dependent, irreversible steps of bacteriophages phi 80 and T1 infection. It could act to transduce energy from the cytoplasmic membrane to specific en [...]

tonB-dependent uptake of B colicins; similar to E. coli uptake of enterochelin; tonB-dependent uptake of B colicins (AAC76041.1); Blastp hit to AAC76041.1 (141 aa), 93% identity in aa 1 - 141.

TonB; Interacts with outer membrane receptor proteins that carry out high-affinity binding and energy dependent uptake into the periplasmic space of specific substrates such as cobalamin, and various iron compounds (such as iron dicitrate, enterochelin, aerobactin, etc.). In the absence of TonB these receptors bind their substrates but do not carry out active transport. TonB also interacts with some colicins and is involved in the energy-dependent, irreversible steps of bacteriophages phi 80 and T1 infection. It could act to transduce energy from the cytoplasmic membrane to specific en [...]

Putative membrane component hydrogenase; With TolR probably plays a role in maintaining the position of the peptidoglycan cell wall in the periplasm. Acts as a porin with low permeability that allows slow penetration of small solutes; an internal gate slows down solute passage.

TonB; Interacts with outer membrane receptor proteins that carry out high-affinity binding and energy dependent uptake into the periplasmic space of specific substrates such as cobalamin, and various iron compounds (such as iron dicitrate, enterochelin, aerobactin, etc.). In the absence of TonB these receptors bind their substrates but do not carry out active transport. TonB also interacts with some colicins and is involved in the energy-dependent, irreversible steps of bacteriophages phi 80 and T1 infection. It could act to transduce energy from the cytoplasmic membrane to specific en [...]

Superoxide dismutase; Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems; Belongs to the iron/manganese superoxide dismutase family.