| IED ID | IndEnz0002008174 |
| Enzyme Type ID | protease008174 |
| Protein Name |
Serine/threonine-protein kinase PBS1 EC 2.7.11.1 AvrPphB susceptible protein 1 |
| Gene Name | PBS1 At5g13160 T19L5.120 |
| Organism | Arabidopsis thaliana (Mouse-ear cress) |
| Taxonomic Lineage | cellular organisms Eukaryota Viridiplantae Streptophyta Streptophytina Embryophyta Tracheophyta Euphyllophyta Spermatophyta Magnoliopsida Mesangiospermae eudicotyledons Gunneridae Pentapetalae rosids malvids Brassicales Brassicaceae Camelineae Arabidopsis Arabidopsis thaliana (Mouse-ear cress) |
| Enzyme Sequence | MGCFSCFDSSDDEKLNPVDESNHGQKKQSQPTVSNNISGLPSGGEKLSSKTNGGSKRELLLPRDGLGQIAAHTFAFRELAAATMNFHPDTFLGEGGFGRVYKGRLDSTGQVVAVKQLDRNGLQGNREFLVEVLMLSLLHHPNLVNLIGYCADGDQRLLVYEFMPLGSLEDHLHDLPPDKEALDWNMRMKIAAGAAKGLEFLHDKANPPVIYRDFKSSNILLDEGFHPKLSDFGLAKLGPTGDKSHVSTRVMGTYGYCAPEYAMTGQLTVKSDVYSFGVVFLELITGRKAIDSEMPHGEQNLVAWARPLFNDRRKFIKLADPRLKGRFPTRALYQALAVASMCIQEQAATRPLIADVVTALSYLANQAYDPSKDDSRRNRDERGARLITRNDDGGGSGSKFDLEGSEKEDSPRETARILNRDINRERAVAEAKMWGESLREKRRQSEQGTSESNSTG |
| Enzyme Length | 456 |
| Uniprot Accession Number | Q9FE20 |
| Absorption | |
| Active Site | ACT_SITE 213; /note=Proton acceptor; /evidence=ECO:0000255|PROSITE-ProRule:PRU00159 |
| Activity Regulation | |
| Binding Site | BINDING 115; /note=ATP; /evidence=ECO:0000255|PROSITE-ProRule:PRU00159 |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000269|PubMed:11359614}; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000269|PubMed:11359614}; |
| DNA Binding | |
| EC Number | 2.7.11.1 |
| Enzyme Function | FUNCTION: Protein kinase required for plant defense mechanism mediated by the disease resistance (R) protein RPS5. In case of infection by Pseudomonas syringae, AvrPphB triggers RPS5-mediated defense mechanism via the cleavage of PBS1. Both kinase activity and cleavage by avrPphB are independently required to trigger the RPS5-mediated resistance. Contributes to PAMP-triggered immunity (PTI) signaling and defense responses downstream of FLS2. {ECO:0000269|PubMed:11359614, ECO:0000269|PubMed:12947197, ECO:0000269|PubMed:17277084, ECO:0000269|PubMed:20413097, ECO:0000269|PubMed:22372664}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | NP_BIND 92..100; /note=ATP; /evidence=ECO:0000255|PROSITE-ProRule:PRU00159 |
| Features | Active site (1); Binding site (1); Chain (1); Compositional bias (3); Domain (1); Initiator methionine (1); Lipidation (3); Modified residue (7); Motif (1); Mutagenesis (13); Nucleotide binding (1); Region (2); Site (1) |
| Keywords | ATP-binding;Cell membrane;Direct protein sequencing;Kinase;Lipoprotein;Membrane;Myristate;Nucleotide-binding;Palmitate;Phosphoprotein;Plant defense;Reference proteome;Serine/threonine-protein kinase;Transferase |
| Interact With | O64973 |
| Induction | INDUCTION: Induced by flagellin (flg22). {ECO:0000269|PubMed:20413097}. |
| Subcellular Location | SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor {ECO:0000269|PubMed:22046960, ECO:0000269|PubMed:24225654}. |
| Modified Residue | MOD_RES 21; /note=Phosphoserine; /evidence=ECO:0007744|PubMed:19376835; MOD_RES 160; /note=Phosphotyrosine; /evidence=ECO:0000250|UniProtKB:O48814; MOD_RES 217; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:O48814; MOD_RES 247; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:O48814; MOD_RES 248; /note=Phosphothreonine; /evidence=ECO:0000250|UniProtKB:O48814; MOD_RES 253; /note=Phosphothreonine; /evidence=ECO:0000250|UniProtKB:O48814; MOD_RES 261; /note=Phosphotyrosine; /evidence=ECO:0000250|UniProtKB:O48814 |
| Post Translational Modification | PTM: Cleaved by avrPphB in infected plant cells. Its cleavage serves as a signal that triggers the RPS5-mediated defense system. {ECO:0000269|PubMed:12947197, ECO:0000269|PubMed:17277084}.; PTM: Autophosphorylates (Probable). Autophosphorylation may be required to trigger the RPS5-mediated plant defense system. {ECO:0000305}.; PTM: Palmitoylation at Cys-3 and Cys-6 are required for plasma membrane location that is essential for the RPS5-mediated plant defense response. {ECO:0000269|PubMed:24225654}. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 10224270; 12912986; 14694194; 18775970; 19064707; 19452453; 21477822; 21798944; 25522736; 26912853; 28710392; 29104883; 29907700; 32267815; 32284014; |
| Motif | MOTIF 292..296; /note=Recognition motif required for RPS5-mediated plant resistance to P.syringae; /evidence=ECO:0000269|PubMed:24225654 |
| Gene Encoded By | |
| Mass | 50,384 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | RHEA:17989; RHEA:46608 |
| Cross Reference Brenda |