| IED ID | IndEnz0002016193 |
| Enzyme Type ID | protease016193 |
| Protein Name |
Magnetosome formation protease MamE EC 3.4.21.- Magnetochrome MamE Magnetosome serine protease MamE |
| Gene Name | mamE amb0963 |
| Organism | Magnetospirillum magneticum (strain AMB-1 / ATCC 700264) |
| Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Alphaproteobacteria Rhodospirillales Rhodospirillaceae (purple nonsulfur bacteria) Magnetospirillum Magnetospirillum magneticum Magnetospirillum magneticum (strain AMB-1 / ATCC 700264) |
| Enzyme Sequence | MAMFNGDVEDGGRGDASCGKDLKRYLMLMGVVALVVLFGAFIYRQSSGGLRLGAMLEQMGRGTGPAVNVPVQQGGPSAAVNPAMSVPAGARVAPPSAAGAIATMPPMVDFGPAPIGAGGPFSSVVTLLRNSVVAVTASSANGQAMPDPLGLANPDGLPHFANPATRSVENIGTGVIVRNDGFIVTNYHVVRGANSVFVTVQDDVGSTRYSAEIIKMDEALDLALLKVAPKTPLTAAVLGDSDGVQVADEVIAIGTPFGLDMTVSRGIISAKRKSMVIEGVTHSNLLQTDAAINQGNSGGPLVISNGTVVGINTAIYTPNGAFAGIGFAVPSNQARLFILDEVGWLPTSTAEGASMGLVAMQRPMGGGVGAAGPAIFAGTRAPHTDGRQNMDCTTCHDLIPAGNGRPAPMMPIAAPIPPPPIPMGAVSPHTDGRQNMNCANCHQMLGGAAPIAAPGLGGGAYRFAQPPGSLAINIQGPRGGQSTAAGTGRVTLLGAALTPMSQRLGAQTGVPVGRGVFISGVTPNTPAATAGLRPGDVLLKVDGRPVRLPEEVSAIMVEMHAGRSVRLGVLRDGDVRNMTLVAGPAGLAAAAVQAPAIADMAQPPMGGMAPTAPGMVAVPGGPAVMPKPPTEFNWLGMEIETFQAPRPITGVPGAVPVPGAKGAQVAEVLVGSRAAVAGLQANDLILEVNNRPVAGPARLDAAIKGATNAGQQILLKVNRNGQEFWIVL |
| Enzyme Length | 728 |
| Uniprot Accession Number | Q2W8Q8 |
| Absorption | |
| Active Site | ACT_SITE 188; /note="Charge relay system"; /evidence="ECO:0000250|UniProtKB:P0C0V0, ECO:0000269|PubMed:26981620, ECO:0000305|PubMed:21414040"; ACT_SITE 221; /note="Charge relay system"; /evidence="ECO:0000250|UniProtKB:P0C0V0, ECO:0000269|PubMed:26981620, ECO:0000305|PubMed:21414040"; ACT_SITE 297; /note="Charge relay system"; /evidence="ECO:0000250|UniProtKB:P0C0V0, ECO:0000269|PubMed:26981620, ECO:0000305|PubMed:21414040" |
| Activity Regulation | ACTIVITY REGULATION: Autoproteolysis is stimulated by exogenous substrates or peptides that bind to its PDZ domains; may be stimulated by an environmental cue in vivo. Protease activity is tightly regulated; increasing its activity decreases substrate levels and disturbs biomineralization. {ECO:0000269|PubMed:27302060}. |
| Binding Site | BINDING 392; /note="Heme 1; covalent"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00433, ECO:0000305|PubMed:21414040, ECO:0000305|PubMed:23176475"; BINDING 395; /note="Heme 1; covalent"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00433, ECO:0000305|PubMed:21414040, ECO:0000305|PubMed:23176475"; BINDING 438; /note="Heme 2; covalent"; /evidence="ECO:0000305|PubMed:21414040, ECO:0000305|PubMed:23176475"; BINDING 441; /note="Heme 2; covalent"; /evidence="ECO:0000305|PubMed:21414040, ECO:0000305|PubMed:23176475" |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.21.- |
| Enzyme Function | FUNCTION: Acts at 2 distinct steps of magnetosome formation; required for correct localization of proteins to the magnetosome while the protease activity is required for maturation of small magnetite crystals into larger, functional ones. The 2 functions are separable by mutation (PubMed:21414040). Probably cleaves at least itself, MamO and MamP; cleavage requires the putative transport domain of MamO (Probable) (PubMed:26981620). Involved in localization of some proteins (at least MamA, MamC, MamF, MamI and MamJ) to the magnetosome (PubMed:20212111, PubMed:21414040). {ECO:0000269|PubMed:20212111, ECO:0000269|PubMed:21414040, ECO:0000269|PubMed:26981620, ECO:0000305|PubMed:21414040}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Binding site (4); Chain (1); Domain (2); Metal binding (2); Motif (2); Mutagenesis (5); Topological domain (2); Transmembrane (1) |
| Keywords | Autocatalytic cleavage;Biomineralization;Heme;Hydrolase;Iron;Magnetosome;Membrane;Metal-binding;Protease;Reference proteome;Repeat;Transmembrane;Transmembrane helix |
| Interact With | |
| Induction | INDUCTION: Expressed during exponential phase in static growth conditions (PubMed:20161777). Part of the probable 18 gene mamAB operon (Probable). {ECO:0000269|PubMed:20161777, ECO:0000305|PubMed:20212111}. |
| Subcellular Location | SUBCELLULAR LOCATION: Magnetosome membrane {ECO:0000269|PubMed:20161777, ECO:0000305|PubMed:21414040}; Single-pass membrane protein {ECO:0000255}. |
| Modified Residue | |
| Post Translational Modification | PTM: Subject to autocatalytic cleavage; cleavage also requires MamO. {ECO:0000269|PubMed:26981620}. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | MOTIF 375..398; /note=MCR (magnetochrome) 1; /evidence=ECO:0000305|PubMed:23176475; MOTIF 421..444; /note=MCR 2; /evidence=ECO:0000305|PubMed:23176475 |
| Gene Encoded By | |
| Mass | 73,478 |
| Kinetics | |
| Metal Binding | METAL 396; /note="Iron 1 (heme axial ligand)"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00433, ECO:0000305|PubMed:21414040, ECO:0000305|PubMed:23176475"; METAL 442; /note="Iron 2 (heme axial ligand)"; /evidence="ECO:0000305|PubMed:21414040, ECO:0000305|PubMed:23176475" |
| Rhea ID | |
| Cross Reference Brenda |