Difference between revisions of "Part:BBa K3610005"
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− | + | This part entails the sequence of the plant PRR EFR from A. thaliana. | |
− | + | ===Usage and Biology=== | |
+ | Elongation factor-thermo unstable receptor (EFR) from A. thaliana is a plant pattern-recognition receptor (PRR). It is a cell surface receptor and part of the plants firts defence mechanism against potential pathogens. | ||
+ | The EFR receptor is also a leucin-rich-repeats (LRR) receptor-like serine/threonine-protein kinase. The protein consists of an extracellular domain with leucin-rich repeats, a ligand binding domain found in many receptors, a single-pass transmembrane domain and finally an intracellular kinase domain. | ||
+ | The ligand binding domain from EFR has high specificity to a bacterial pathogen-associated moleculat pattern (PAMP), namely the epitope elf18 of the abundant protein Elongation Factor Tu (EF-Tu), which is catalyzes the binding of aminoacyl-tRNA (aa-tRNA) to the ribosome in most prokaryotes and therefore is evolutionarily highly conserved. This makes the EFR a receptor that can be activated by the presence of a huge variety of bacteria. | ||
+ | Upon binding of the ligand to the extracellular domain, the receptor dimerizes with its coreceptor BRI1-associated receptor kinase (BAK1). This interaction triggers the activation of the intracellular kinase domain of EFR and BAK1, initiating a signal cascade leading to an upregulation of immune response mechanisms. | ||
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− | + | <span class='h3bb'>Sequence and Features</span> | |
+ | <partinfo>BBa_K3610005 SequenceAndFeatures</partinfo> |
Latest revision as of 20:20, 27 October 2020
EFR from A. thaliana
This part entails the sequence of the plant PRR EFR from A. thaliana.
Usage and Biology
Elongation factor-thermo unstable receptor (EFR) from A. thaliana is a plant pattern-recognition receptor (PRR). It is a cell surface receptor and part of the plants firts defence mechanism against potential pathogens. The EFR receptor is also a leucin-rich-repeats (LRR) receptor-like serine/threonine-protein kinase. The protein consists of an extracellular domain with leucin-rich repeats, a ligand binding domain found in many receptors, a single-pass transmembrane domain and finally an intracellular kinase domain. The ligand binding domain from EFR has high specificity to a bacterial pathogen-associated moleculat pattern (PAMP), namely the epitope elf18 of the abundant protein Elongation Factor Tu (EF-Tu), which is catalyzes the binding of aminoacyl-tRNA (aa-tRNA) to the ribosome in most prokaryotes and therefore is evolutionarily highly conserved. This makes the EFR a receptor that can be activated by the presence of a huge variety of bacteria. Upon binding of the ligand to the extracellular domain, the receptor dimerizes with its coreceptor BRI1-associated receptor kinase (BAK1). This interaction triggers the activation of the intracellular kinase domain of EFR and BAK1, initiating a signal cascade leading to an upregulation of immune response mechanisms.
Sequence and Features
- 10INCOMPATIBLE WITH RFC[10]Illegal EcoRI site found at 2753
Illegal XbaI site found at 433
Illegal XbaI site found at 2568
Illegal SpeI site found at 1114
Illegal PstI site found at 2407 - 12INCOMPATIBLE WITH RFC[12]Illegal EcoRI site found at 2753
Illegal SpeI site found at 1114
Illegal PstI site found at 2407 - 21INCOMPATIBLE WITH RFC[21]Illegal EcoRI site found at 2753
Illegal BglII site found at 2418
Illegal BglII site found at 2446
Illegal BglII site found at 2989
Illegal XhoI site found at 2442
Illegal XhoI site found at 3032 - 23INCOMPATIBLE WITH RFC[23]Illegal EcoRI site found at 2753
Illegal XbaI site found at 433
Illegal XbaI site found at 2568
Illegal SpeI site found at 1114
Illegal PstI site found at 2407 - 25INCOMPATIBLE WITH RFC[25]Illegal EcoRI site found at 2753
Illegal XbaI site found at 433
Illegal XbaI site found at 2568
Illegal SpeI site found at 1114
Illegal PstI site found at 2407
Illegal AgeI site found at 256 - 1000COMPATIBLE WITH RFC[1000]