energy transducer TonB [Burkholderia gladioli]
energy transducer TonB( domain architecture ID 10018802)
energy transducer 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.)
List of domain hits
Name | Accession | Description | Interval | E-value | ||
tonB_Cterm | TIGR01352 | TonB family C-terminal domain; This model represents the C-terminal of TonB and is homologs. ... |
78-132 | 6.67e-08 | ||
TonB family C-terminal domain; This model represents the C-terminal of TonB and is homologs. TonB is an energy-transducer for TonB-dependent receptors of Gram-negative bacteria. Most members are designated as TonB or TonB-related proteins, but a few represent the paralogous TolA protein. Several bacteria have up to four TonB paralogs. In nearly every case, a proline-rich repetive region is found N-terminal to this domain; these low-complexity regions are highly divergent and cannot readily be aligned. The region is suggested to help span the periplasm. [Transport and binding proteins, Cations and iron carrying compounds] : Pssm-ID: 273570 [Multi-domain] Cd Length: 74 Bit Score: 47.30 E-value: 6.67e-08
|
||||||
Name | Accession | Description | Interval | E-value | ||
tonB_Cterm | TIGR01352 | TonB family C-terminal domain; This model represents the C-terminal of TonB and is homologs. ... |
78-132 | 6.67e-08 | ||
TonB family C-terminal domain; This model represents the C-terminal of TonB and is homologs. TonB is an energy-transducer for TonB-dependent receptors of Gram-negative bacteria. Most members are designated as TonB or TonB-related proteins, but a few represent the paralogous TolA protein. Several bacteria have up to four TonB paralogs. In nearly every case, a proline-rich repetive region is found N-terminal to this domain; these low-complexity regions are highly divergent and cannot readily be aligned. The region is suggested to help span the periplasm. [Transport and binding proteins, Cations and iron carrying compounds] Pssm-ID: 273570 [Multi-domain] Cd Length: 74 Bit Score: 47.30 E-value: 6.67e-08
|
||||||
TonB | COG0810 | Periplasmic protein TonB, links inner and outer membranes [Cell wall/membrane/envelope ... |
86-132 | 3.02e-06 | ||
Periplasmic protein TonB, links inner and outer membranes [Cell wall/membrane/envelope biogenesis]; Pssm-ID: 440572 [Multi-domain] Cd Length: 70 Bit Score: 42.96 E-value: 3.02e-06
|
||||||
TonB_2 | pfam13103 | TonB C terminal; This family contains TonB members that are not captured by pfam03544. |
55-132 | 4.96e-06 | ||
TonB C terminal; This family contains TonB members that are not captured by pfam03544. Pssm-ID: 463788 [Multi-domain] Cd Length: 85 Bit Score: 42.70 E-value: 4.96e-06
|
||||||
Name | Accession | Description | Interval | E-value | ||
tonB_Cterm | TIGR01352 | TonB family C-terminal domain; This model represents the C-terminal of TonB and is homologs. ... |
78-132 | 6.67e-08 | ||
TonB family C-terminal domain; This model represents the C-terminal of TonB and is homologs. TonB is an energy-transducer for TonB-dependent receptors of Gram-negative bacteria. Most members are designated as TonB or TonB-related proteins, but a few represent the paralogous TolA protein. Several bacteria have up to four TonB paralogs. In nearly every case, a proline-rich repetive region is found N-terminal to this domain; these low-complexity regions are highly divergent and cannot readily be aligned. The region is suggested to help span the periplasm. [Transport and binding proteins, Cations and iron carrying compounds] Pssm-ID: 273570 [Multi-domain] Cd Length: 74 Bit Score: 47.30 E-value: 6.67e-08
|
||||||
TonB | COG0810 | Periplasmic protein TonB, links inner and outer membranes [Cell wall/membrane/envelope ... |
86-132 | 3.02e-06 | ||
Periplasmic protein TonB, links inner and outer membranes [Cell wall/membrane/envelope biogenesis]; Pssm-ID: 440572 [Multi-domain] Cd Length: 70 Bit Score: 42.96 E-value: 3.02e-06
|
||||||
TonB_2 | pfam13103 | TonB C terminal; This family contains TonB members that are not captured by pfam03544. |
55-132 | 4.96e-06 | ||
TonB C terminal; This family contains TonB members that are not captured by pfam03544. Pssm-ID: 463788 [Multi-domain] Cd Length: 85 Bit Score: 42.70 E-value: 4.96e-06
|
||||||
TonB_C | pfam03544 | Gram-negative bacterial TonB protein C-terminal; The TonB_C domain is the well-characterized ... |
86-137 | 1.04e-04 | ||
Gram-negative bacterial TonB protein C-terminal; The TonB_C domain is the well-characterized C-terminal region of the TonB receptor molecule. This protein is bound to an inner membrane-bound protein ExbB via a globular domain and has a flexible middle region that is likely to help in positioning the C-terminal domain into the iron-transporter barrel in the outer membrane. TonB_C interacts with the N-terminal TonB box of the outer membrane transporter that binds the Fe3+-siderophore complex. The barrel of the transporter, consisting of 22 beta-sheets and an inside plug, binds the iron complex in the barrel entrance. Pssm-ID: 427361 [Multi-domain] Cd Length: 79 Bit Score: 38.80 E-value: 1.04e-04
|
||||||
tolA_full | TIGR02794 | TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
55-130 | 3.41e-03 | ||
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis] Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 36.75 E-value: 3.41e-03
|
||||||
Blast search parameters | ||||
|