IED ID | IndEnz0002008199 |
Enzyme Type ID | protease008199 |
Protein Name |
Presequence protease 1, chloroplastic/mitochondrial AtPreP1 PreP 1 EC 3.4.24.- Zinc metalloprotease 1 AtZnMP1 |
Gene Name | PREP1 ZNMP1 At3g19170 MVI11.6 MVI11.7 MVI11_8 |
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 | MLRTVSCLASRSSSSLFFRFFRQFPRSYMSLTSSTAALRVPSRNLRRISSPSVAGRRLLLRRGLRIPSAAVRSVNGQFSRLSVRAVATQPAPLYPDVGQDEAEKLGFEKVSEEFISECKSKAILFKHKKTGCEVMSVSNEDENKVFGVVFRTPPKDSTGIPHILEHSVLCGSRKYPVKEPFVELLKGSLHTFLNAFTYPDRTCYPVASTNTKDFYNLVDVYLDAVFFPKCVDDAHTFQQEGWHYELNDPSEDISYKGVVFNEMKGVYSQPDNILGRIAQQALSPENTYGVDSGGDPKDIPNLTFEEFKEFHRQYYHPSNARIWFYGDDDPVHRLRVLSEYLDMFEASPSPNSSKIKFQKLFSEPVRLVEKYPAGRDGDLKKKHMLCVNWLLSEKPLDLQTQLALGFLDHLMLGTPASPLRKILLESGLGEALVSSGLSDELLQPQFGIGLKGVSEENVQKVEELIMDTLKKLAEEGFDNDAVEASMNTIEFSLRENNTGSFPRGLSLMLQSISKWIYDMDPFEPLKYTEPLKALKTRIAEEGSKAVFSPLIEKLILNNSHRVTIEMQPDPEKATQEEVEEKNILEKVKAAMTEEDLAELARATEELKLKQETPDPPEALRCVPSLNLGDIPKEPTYVPTEVGDINGVKVLRHDLFTNDIIYTEVVFDIGSLKHELLPLVPLFCQSLLEMGTKDLTFVQLNQLIGRKTGGISVYPLTSSVRGKDEPCSKIIVRGKSMAGRADDLFNLMNCLLQEVQFTDQQRFKQFVSQSRARMENRLRGSGHGIAAARMDAMLNIAGWMSEQMGGLSYLEFLHTLEKKVDEDWEGISSSLEEIRRSLLARNGCIVNMTADGKSLTNVEKSVAKFLDLLPENPSGGLVTWDGRLPLRNEAIVIPTQVNYVGKAGNIYSTGYELDGSAYVISKHISNTWLWDRVRVSGGAYGGFCDFDSHSGVFSYLSYRDPNLLKTLDIYDGTGDFLRGLDVDQETLTKAIIGTIGDVDSYQLPDAKGYSSLLRHLLGVTDEERQRKREEILTTSLKDFKDFAQAIDVVRDKGVAVAVASAEDIDAANNERSNFFEVKKAL |
Enzyme Length | 1080 |
Uniprot Accession Number | Q9LJL3 |
Absorption | |
Active Site | ACT_SITE 165; /note=Proton acceptor; /evidence=ECO:0000269|PubMed:16601675; ACT_SITE 240; /evidence=ECO:0000305 |
Activity Regulation | ACTIVITY REGULATION: Inactive in the absence of MgCl(2) and CaCl(2) and full activation at 10 mM concentrations of either ion. Completely inhibited by the metal chelator orthophenanthroline, but not affected by phenylmethylsulfonyl fluoride (PMSF) or N-ethylmaleimide (NEM). |
Binding Site | |
Calcium Binding | |
catalytic Activity | |
DNA Binding | |
EC Number | 3.4.24.- |
Enzyme Function | FUNCTION: ATP-independent protease that degrades both mitochondrial and chloroplastic transit peptides after their cleavage. Also degrades other unstructured peptides. Specific for peptides in the range of 10 to 65 residues. Shows a preference for cleavage after small polar residues and before basic residues, with a bias for positively charged amino acid residues. {ECO:0000269|PubMed:12138166}. |
Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 28 degrees Celsius. Active from 4 to 40 degrees Celsius.; |
PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Active from pH 4 to 10.; |
Pathway | |
nucleotide Binding | |
Features | Active site (2); Beta strand (30); Chain (1); Coiled coil (1); Erroneous initiation (1); Helix (49); Metal binding (3); Modified residue (1); Mutagenesis (18); Transit peptide (1); Turn (9) |
Keywords | 3D-structure;Acetylation;Alternative splicing;Chloroplast;Coiled coil;Hydrolase;Magnesium;Metal-binding;Metalloprotease;Mitochondrion;Plastid;Protease;Reference proteome;Transit peptide;Zinc |
Interact With | P17614 |
Induction | |
Subcellular Location | SUBCELLULAR LOCATION: Plastid, chloroplast stroma. Mitochondrion matrix. |
Modified Residue | MOD_RES 86; /note=N-acetylvaline; /evidence=ECO:0007744|PubMed:22223895 |
Post Translational Modification | |
Signal Peptide | |
Structure 3D | X-ray crystallography (1) |
Cross Reference PDB | 2FGE; |
Mapped Pubmed ID | 12938931; 14576160; 14730085; 15028209; 15047901; 15276459; 16207701; 16502469; 16766689; 17081117; 18230142; 18431481; 18538804; 18633119; 18650403; 19423572; 19646442; 19701724; 21333657; 21621546; 21798377; 21995547; 22995300; 24373893; 28627464; 30242930; 32663165; 33229537; |
Motif | |
Gene Encoded By | |
Mass | 121,015 |
Kinetics | |
Metal Binding | METAL 162; /note=Zinc; catalytic; /evidence=ECO:0000269|PubMed:16601675; METAL 166; /note=Zinc; catalytic; /evidence=ECO:0000269|PubMed:16601675; METAL 262; /note=Zinc; catalytic; /evidence=ECO:0000269|PubMed:16601675 |
Rhea ID | |
Cross Reference Brenda |