| IED ID | IndEnz0002016192 |
| Enzyme Type ID | protease016192 |
| Protein Name |
Magnetosome formation protease MamE EC 3.4.21.- MM36.3 Magnetochrome MamE Magnetosome serine protease MamE |
| Gene Name | mamE MGMSRv2__2379 mgI487 MGR_4091 |
| Organism | Magnetospirillum gryphiswaldense (strain DSM 6361 / JCM 21280 / NBRC 15271 / MSR-1) |
| Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Alphaproteobacteria Rhodospirillales Rhodospirillaceae (purple nonsulfur bacteria) Magnetospirillum Magnetospirillum gryphiswaldense Magnetospirillum gryphiswaldense (strain DSM 6361 / JCM 21280 / NBRC 15271 / MSR-1) |
| Enzyme Sequence | MTMFNGDVEDGGRSNVSCGKDLKRYLMLMGVVALVVLFGAFIYRQSSGGLRLGAMMEQMTGARGAVNVPAQHGAPSAVVDPAMSVPARARVAPPSAAGAIATFPPVVDFGPAPVVSGGPFTGVVTLLRNSVVSVTASSSGGQVMPDPLGLVNPDGLPRFANPTTRSVENIGTGVIVRNDGFIVTNYHVVRGANSVYVTVKDDVGSIRYSGEIVKMDEALDLALLKITPKVQLTAAVLGDSDAVNVADEVIAIGTPFGLDMTVSRGIISAKRKTMVIEGMTHSNLLQTDAAINQGNSGGPLVAANGTVVGINTAIYTPNGAFAGIGFAVPSNQARLFALDEVGWLPTSTAEGPAMGLVAMQRPMGVGVGAAGPVIAAGTPSPHVDGRQNMDCSNCHDIIPAGNGFQAPMMPVAAPVPPPPIPANAVSPHTDGRQNMTCNTCHQFVGGAAAGPIAFGQPMMPIAAPQQPAPAIRANAANPHTDGRQNMNCASCHQIIGSVGAAPIAAPGAGGAYRFSQPPGSLAINIQGPRGGQGAVAGSGGSRASLLGAALTPLTQRLGLQANLPAGRGVFVNGVTPNTPAASAGLRPGDVILKVDGRPVHQPEEVAAIMAEMPNGRSVRIGVLRAGDVSNMSLVTGPSGLAAAVVQAPTAPVVMAGGAPTVPGVQPVIPKVPTEFNWLGMEIETFMAPQPVVGMPGATPVAGGGKGAQVAEVLAGSRAAVAGLQANDLIIEVNNRPVTSPARLDAAIKAATAAGQQILLKVHRNGQEFWIVL |
| Enzyme Length | 772 |
| Uniprot Accession Number | V6F2B6 |
| Absorption | |
| Active Site | ACT_SITE 187; /note=Charge relay system; /evidence=ECO:0000250|UniProtKB:P0C0V0; ACT_SITE 220; /note=Charge relay system; /evidence=ECO:0000250|UniProtKB:P0C0V0; ACT_SITE 296; /note=Charge relay system; /evidence=ECO:0000250|UniProtKB:P0C0V0 |
| Activity Regulation | |
| Binding Site | BINDING 391; /note="Heme 1; covalent"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00433, ECO:0000305|PubMed:23176475"; BINDING 394; /note="Heme 1; covalent"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00433, ECO:0000305|PubMed:23176475"; BINDING 437; /note="Heme 2; covalent"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00433, ECO:0000305"; BINDING 440; /note="Heme 2; covalent"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00433, ECO:0000305"; BINDING 488; /note="Heme 3; covalent"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00433, ECO:0000305|PubMed:23176475"; BINDING 491; /note="Heme 3; covalent"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00433, 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 (By similarity) (PubMed:20674739). Probably cleaves at least itself, MamO and MamP; cleavage requires the putative transprot domain of MamO (By similarity). Involved in localization of some proteins (at least MamA, MamC, MamF, MamI and MamJ) to the magnetosome (By similarity). One of 7 genes (mamLQBIEMO) able to induce magnetosome membrane biogenesis; coexpression of mamLQRBIEMO in a deletion of the 17 gene mamAB operon restores magnetosome vesicle formation but not magnetite biosynthesis (PubMed:27286560). {ECO:0000250|UniProtKB:Q2W8Q8, ECO:0000269|PubMed:20674739, ECO:0000269|PubMed:27286560}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Binding site (6); Chain (1); Domain (3); Metal binding (3); Motif (3); Sequence conflict (1); Topological domain (2); Transmembrane (1) |
| Keywords | Autocatalytic cleavage;Biomineralization;Direct protein sequencing;Heme;Hydrolase;Iron;Magnetosome;Membrane;Metal-binding;Protease;Reference proteome;Repeat;Transmembrane;Transmembrane helix |
| Interact With | |
| Induction | INDUCTION: Part of the probable 17 gene mamAB operon. {ECO:0000305|PubMed:13129949}. |
| Subcellular Location | SUBCELLULAR LOCATION: Magnetosome membrane {ECO:0000269|PubMed:11571158, ECO:0000269|PubMed:14766587}; Single-pass membrane protein {ECO:0000255}. Note=Purified magnetosomes remain attached to each other. {ECO:0000269|PubMed:11571158}. |
| Modified Residue | |
| Post Translational Modification | PTM: The protein isolated from magnetosome membranes has a molecular weight of about 36.3 kDa, probably due to C-terminal cleavage (PubMed:11571158). Subject to autocatalytic cleavage; cleavage also requires MamO; these may be the same event (By similarity). {ECO:0000250|UniProtKB:Q2W8Q8, ECO:0000269|PubMed:11571158}. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | MOTIF 374..397; /note=MCR (magnetochrome) 1; /evidence=ECO:0000305|PubMed:23176475; MOTIF 420..443; /note=MCR 2; /evidence=ECO:0000305; MOTIF 470..494; /note=MCR 3; /evidence=ECO:0000305|PubMed:23176475 |
| Gene Encoded By | |
| Mass | 78,036 |
| Kinetics | |
| Metal Binding | METAL 395; /note="Iron 1 (heme axial ligand)"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00433, ECO:0000305|PubMed:23176475"; METAL 441; /note="Iron 2 (heme axial ligand)"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00433, ECO:0000305"; METAL 492; /note="Iron 3 (heme axial ligand)"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00433, ECO:0000305|PubMed:23176475" |
| Rhea ID | |
| Cross Reference Brenda |