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).

Ferrous iron transport protein B; Probable transporter for a GTP-driven Fe(2+) uptake system. Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like GTPase superfamily. FeoB GTPase (TC 9.A.8) family.

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.

Ferrous iron transport protein B; Probable transporter for a GTP-driven Fe(2+) uptake system. Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like GTPase superfamily. FeoB GTPase (TC 9.A.8) family.

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 [...]

Ferrous iron transport protein B; Probable transporter for a GTP-driven Fe(2+) uptake system. Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like GTPase superfamily. FeoB GTPase (TC 9.A.8) family.

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).

Ferrous iron transport protein B; Probable transporter for a GTP-driven Fe(2+) uptake system. Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like GTPase superfamily. FeoB GTPase (TC 9.A.8) family.

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.

Ferrous iron transport protein B; Probable transporter for a GTP-driven Fe(2+) uptake system. Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like GTPase superfamily. FeoB GTPase (TC 9.A.8) 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 [...]

Glyceraldehyde-3-phosphate dehydrogenase A; Catalyzes the oxidative phosphorylation of glyceraldehyde 3- phosphate (G3P) to 1,3-bisphosphoglycerate (BPG) using the cofactor NAD. The first reaction step involves the formation of a hemiacetal intermediate between G3P and a cysteine residue, and this hemiacetal intermediate is then oxidized to a thioester, with concomitant reduction of NAD to NADH. The reduced NADH is then exchanged with the second NAD, and the thioester is attacked by a nucleophilic inorganic phosphate to produce BPG.

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 [...]

Invasion protein; Involved in the invasion of the cells of the intestinal epithelium. Could be involved in the translocation of the InvE protein; Belongs to the FHIPEP (flagella/HR/invasion proteins export pore) family.

Putative glycosyl transferase; Related to UDP-glucuronosyltransferase.

Invasion protein; Involved in the invasion of the cells of the intestinal epithelium. Could be involved in the translocation of the InvE protein; Belongs to the FHIPEP (flagella/HR/invasion proteins export pore) family.

Nonspecific acid phosphatase precursor. (SW:PHON_SALTY).

Putative glycosyl transferase; Related to UDP-glucuronosyltransferase.

Invasion protein; Involved in the invasion of the cells of the intestinal epithelium. Could be involved in the translocation of the InvE protein; Belongs to the FHIPEP (flagella/HR/invasion proteins export pore) family.

Putative glycosyl transferase; Related to UDP-glucuronosyltransferase.

Putative ATP binding cassette (ABC) transporter; Similar to E. coli ATP-binding transport protein; multicopy suppressor of htrB (AAC74000.1); Blastp hit to AAC74000.1 (582 aa), 26% identity in aa 14 - 582, 29% identity in aa 34 - 565.

Putative ATP binding cassette (ABC) transporter; Similar to E. coli ATP-binding transport protein; multicopy suppressor of htrB (AAC74000.1); Blastp hit to AAC74000.1 (582 aa), 26% identity in aa 14 - 582, 29% identity in aa 34 - 565.

Putative glycosyl transferase; Related to UDP-glucuronosyltransferase.

Nonspecific acid phosphatase precursor. (SW:PHON_SALTY).

Invasion protein; Involved in the invasion of the cells of the intestinal epithelium. Could be involved in the translocation of the InvE protein; Belongs to the FHIPEP (flagella/HR/invasion proteins export pore) 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 [...]

Ferrous iron transport protein B; Probable transporter for a GTP-driven Fe(2+) uptake system. Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like GTPase superfamily. FeoB GTPase (TC 9.A.8) 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 [...]

Glyceraldehyde-3-phosphate dehydrogenase A; Catalyzes the oxidative phosphorylation of glyceraldehyde 3- phosphate (G3P) to 1,3-bisphosphoglycerate (BPG) using the cofactor NAD. The first reaction step involves the formation of a hemiacetal intermediate between G3P and a cysteine residue, and this hemiacetal intermediate is then oxidized to a thioester, with concomitant reduction of NAD to NADH. The reduced NADH is then exchanged with the second NAD, and the thioester is attacked by a nucleophilic inorganic phosphate to produce BPG.