| IED ID | IndEnz0002010137 |
| Enzyme Type ID | protease010137 |
| Protein Name |
Subtilisin-like protease SBT3 EC 3.4.21.- LeSBT3 SlSBT3 Subtilase 3 |
| Gene Name | sbt3 Solyc01g087850 |
| Organism | Solanum lycopersicum (Tomato) (Lycopersicon esculentum) |
| Taxonomic Lineage | cellular organisms Eukaryota Viridiplantae Streptophyta Streptophytina Embryophyta Tracheophyta Euphyllophyta Spermatophyta Magnoliopsida Mesangiospermae eudicotyledons Gunneridae Pentapetalae asterids lamiids Solanales Solanaceae Solanoideae Solaneae Solanum Solanum subgen. Lycopersicon Solanum lycopersicum (Tomato) (Lycopersicon esculentum) |
| Enzyme Sequence | MELLHLLLFSWALSAHLFLALAQRSTYIVHLDKSLMPNVFTDHHHWHSSTIDSIKASVPSSVDRFHSAPKLVYSYDNVLHGFSAVLSKDELAALKKLPGFISAYKDRTVEPHTTHTSDFLKLNPSSGLWPASGLGQDVIVAVLDSGIWPESASFQDDGMPEIPKRWKGICKPGTQFNASMCNRKLIGANYFNKGILANDPTVNITMNSARDTDGHGTHCASITAGNFAKGVSHFGYAPGTARGVAPRARLAVYKFSFNEGTFTSDLIAAMDQAVADGVDMISISYGYRFIPLYEDAISIASFGAMMKGVLVSASAGNRGPGIGSLNNGSPWILCVASGHTDRTFAGTLTLGNGLKIRGWSLFPARAFVRDSPVIYNKTLSDCSSEELLSQVENPENTIVICDDNGDFSDQMRIITRARLKAAIFISEDPGVFRSATFPNPGVVVNKKEGKQVINYVKNSVTPTATITFQETYLDTKPAPVVAASSARGPSRSYLGISKPDILAPGVLILAAYPPNVFATSIGTNILLSTDYILESGTSMAAPHAAGIAAMLKAAHPEWSPSAIRSAMMTTADPLDNTRKPIKDSDNNKAATPLDMGAGHVDPNRALDPGLVYDATPQDYVNLLCSLNFTEEQFKTIARSSASHNCSNPSADLNYPSFIALYSIEGNFTLLEQKFKRTVTNVGKGAATYKAKLKAPKNSTISVSPQILVFKNKNEKQSYTLTIRYIGDEGQSRNVGSITWVEQNGNHSVRSPIVTSPIIEVW |
| Enzyme Length | 761 |
| Uniprot Accession Number | O82777 |
| Absorption | |
| Active Site | ACT_SITE 144; /note="Charge relay system"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"; ACT_SITE 215; /note="Charge relay system"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01240, ECO:0000269|PubMed:19805099"; ACT_SITE 538; /note="Charge relay system"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01240, ECO:0000269|PubMed:19332543, ECO:0000269|PubMed:19805099" |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by 1 mM 4-(2-aminoethyl)-benzenesulfonyl fluoride (AEBSF), a general inhibitor of serine proteinases, but not by the more selective serine protease inhibitors N-alpha-tosyl-L-lysinyl-chloromethylketone (TLCK), N-tosyl-L-phenylalaninyl-chloromethylketone (TPCK), leupeptin, aprotinin or benzamidine (PubMed:19332543). Its proteolytic activity is autoinhibited by the non-covalent binding of the propeptide to the catalytic domain (PubMed:27451395). No effect on activity by the addition of CaCl(2) or calcium chelators (PubMed:19805099). {ECO:0000269|PubMed:19332543, ECO:0000269|PubMed:19805099, ECO:0000269|PubMed:27451395}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.21.- |
| Enzyme Function | FUNCTION: Serine protease (PubMed:19332543, PubMed:19407393, PubMed:19805099, PubMed:27451395, PubMed:27259555). Has preference for Gln in the P1 position and Lys in the P2 position of oligopeptide substrates. Active also with His in the P1 position (PubMed:19332543). Involved in resistance against insects partly by regulating expression of systemic wound response genes and possibly by its post-ingestive activity in the insect gut. Apart from the role in defense, may be involved in regulation of pectin methylesterases (PMEs) activity and pectin methylesterification of the cell wall (PubMed:27259555). {ECO:0000269|PubMed:19332543, ECO:0000269|PubMed:19407393, ECO:0000269|PubMed:19805099, ECO:0000269|PubMed:27259555, ECO:0000269|PubMed:27451395}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Thermostable (PubMed:19332543, PubMed:27451395, PubMed:19805099). Activity is unaffected by heating to 60 degrees Celsius and only partially reduced after incubation at 70 degrees Celsius (PubMed:19332543). {ECO:0000269|PubMed:19332543, ECO:0000269|PubMed:19805099, ECO:0000269|PubMed:27451395}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.5-8.0. 60% of the activity is retained at pH 11.0 (PubMed:19332543). No autolysis at pH 4.0-9.0 in the presence of 5 mM EDTA or 5 mM CaCl(2) (PubMed:19805099). {ECO:0000269|PubMed:19332543, ECO:0000269|PubMed:19805099}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Beta strand (34); Chain (1); Disulfide bond (3); Domain (2); Glycosylation (9); Helix (20); Mutagenesis (8); Propeptide (1); Region (2); Signal peptide (1); Site (2); Turn (4) |
| Keywords | 3D-structure;Autocatalytic cleavage;Cleavage on pair of basic residues;Direct protein sequencing;Disulfide bond;Glycoprotein;Hydrolase;Plant defense;Protease;Reference proteome;Secreted;Serine protease;Signal;Zymogen |
| Interact With | Itself |
| Induction | INDUCTION: Expressed in response to mechanical wounding and insect herbivory in leaves. Not expressed in uninjured leaves. {ECO:0000269|PubMed:27259555}. |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:19332543, ECO:0000269|PubMed:19407393, ECO:0000269|PubMed:19805099, ECO:0000269|PubMed:27451395}. Note=Autocatalytic cleavage is required for the secretion of the mature protein. {ECO:0000269|PubMed:19332543}. |
| Modified Residue | |
| Post Translational Modification | PTM: Propeptide is internally cleaved at Asn-38 and Asp-52 in a pH-dependent manner leading to the dissociation of the propeptide from the catalytic domain and resulting in the release of the active subtilase. Cleavage occurs at pH 5.7 and to a stronger extent at pH 5.2. {ECO:0000269|PubMed:27451395}. |
| Signal Peptide | SIGNAL 1..22; /evidence=ECO:0000255 |
| Structure 3D | X-ray crystallography (2) |
| Cross Reference PDB | 3I6S; 3I74; |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 82,226 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=32.8 uM for aminobenzoyl-SKRDPPKMQTDLY(NO2) derived from the plant peptide hormone systemin (at pH 8.0 and 25 degrees Celsius) {ECO:0000269|PubMed:19332543}; Vmax=0.151 nmol/min/mg enzyme with aminobenzoyl-SKRDPPKMQTDLY(NO2) derived from the plant peptide hormone systemin as substrate (at pH 8.0 and 25 degrees Celsius) {ECO:0000269|PubMed:19332543}; |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |