| IED ID | IndEnz0002016238 |
| Enzyme Type ID | protease016238 |
| Protein Name |
Peptidyl-Asp metalloendopeptidase EC 3.4.24.33 Biofilm-associated metzincin protease Metalloendopeptidase Mep72 |
| Gene Name | mep72 PA2783 |
| Organism | Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1) |
| Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Gammaproteobacteria Pseudomonadales Pseudomonadaceae Pseudomonas Pseudomonas aeruginosa group Pseudomonas aeruginosa Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1) |
| Enzyme Sequence | MKKSLLCSTLALAVASAAQAAPKTVDIMVLYTPAATQTANGRDIDARIASYIEFANTAYEKSGVNLRLRLVHKQRLDWADYPTVTGANLDRFMRDPQVQRLREQYGADLVSLVNRSQNSGNGYITCGIGYMGSGDKNSGRFHGNAKDIAYNLTGVDCGLNTFAHEAGHNMGLRHSYEQDLESSYYDPRYAHSGTYEWSRGYGVQGRFATVMAYPHAFGTNKQAPFFANPRLVNAECANQPCGREEHADAVRALNSMATQIADFRPTKVPGTVNPGSGGDTPTPPDLPWCTKAKLGGLLGDGEFASMEGWRAWSGNAQLSLVNVAKGCRDNALLVDVRGFDLLVRPIAPLRAGSGYRLSGKVMLKAANTRETVRMALLSERADGALAYNPAQSVELSVSGNEFSRLEKTFDYRPAADQRNLYVAVWSDSGASLLVDEMNLQEAQAAPPSVPPAPKRIAYDFESGIGGWSGVHASARATRVASAGRLALEAYQRRYAGTGASTSLLGNLEAGRTYAFSADVRVGDGRGSQAMTYAYLYLESQGRPGEYLPLGYKVVENGRWASLRGQVQLPKGPIKRAELMILSGNQQESMFIDNVQLLQK |
| Enzyme Length | 599 |
| Uniprot Accession Number | Q9I060 |
| Absorption | |
| Active Site | ACT_SITE 165; /evidence=ECO:0000305|PubMed:24279383 |
| Activity Regulation | ACTIVITY REGULATION: Is inhibited by BamI, the product of its coregulated adjacent gene. {ECO:0000269|PubMed:25488299}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Cleavage of Xaa-|-Asp, Xaa-|-Glu and Xaa-|-cysteic acid bonds.; EC=3.4.24.33; Evidence={ECO:0000250|UniProtKB:Q9R4J4}; |
| DNA Binding | |
| EC Number | 3.4.24.33 |
| Enzyme Function | FUNCTION: Metalloprotease with endopeptidase activity (PubMed:24279383). Specifically cleaves on the N-terminal side of aspartyl, glutamyl and cysteic acid residues (By similarity). Mep72 appears to be a secreted biofilm-specific regulator that affects the processing of a very specific subset of virulence factors exported by the type III secretion machinery as well as flagellar proteins. Binds directly to ExoS and PcrV and affects the processing of these proteins in the biofilm secretome, but contrary to expectation, Mep72 seems to protect these targets against proteolytic processing/degradation (PubMed:25488299). {ECO:0000250|UniProtKB:Q9R4J4, ECO:0000269|PubMed:24279383, ECO:0000269|PubMed:25488299}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (1); Domain (1); Metal binding (3); Propeptide (1); Region (1); Signal peptide (1) |
| Keywords | Autocatalytic cleavage;Hydrolase;Metal-binding;Metalloprotease;Protease;Reference proteome;Secreted;Signal;Zinc;Zymogen |
| Interact With | |
| Induction | INDUCTION: Its transcription is positively regulated by Vfr, the virulence factor regulator, in a cAMP-dependent manner (PubMed:24279383). Constitutes an operon together with PA2782 (PubMed:24279383, PubMed:25488299). Is expressed only during biofilm growth (PubMed:25488299). {ECO:0000269|PubMed:24279383, ECO:0000269|PubMed:25488299}. |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:24279383, ECO:0000269|PubMed:25488299}. Note=Is secreted through the type II general secretory pathway (Xcp system) and undergoes processing during export. {ECO:0000269|PubMed:25488299}. |
| Modified Residue | |
| Post Translational Modification | PTM: Made as a membrane-associated pre-pro-protein, which is exported to the periplasm with removal of the signal peptide, leading to a protein with a molecular mass of 65 kDa, that likely contains the metzincin domain plus tandem carbohydrate-binding domains. Undergoes processing during export to the extracellular milieu, probably by autocatalysis, yielding a (mature length) 25 kDa protein that most likely corresponds to the metzincin domain only. {ECO:0000269|PubMed:25488299}. |
| Signal Peptide | SIGNAL 1..20; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 64,960 |
| Kinetics | |
| Metal Binding | METAL 164; /note=Zinc; catalytic; /evidence=ECO:0000305|PubMed:24279383; METAL 168; /note=Zinc; catalytic; /evidence=ECO:0000305|PubMed:24279383; METAL 174; /note=Zinc; catalytic; /evidence=ECO:0000305|PubMed:24279383 |
| Rhea ID | |
| Cross Reference Brenda |