| IED ID | IndEnz0002007676 |
| Enzyme Type ID | protease007676 |
| Protein Name |
Multi-heme protein MamP EC 1.-.-.- Magnetochrome MamP Magnetosome-associated protein MamP |
| Gene Name | mamP amb0970 |
| 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 | MNSKVALLVVGLAVVLALVIGRQGPVAPQATNTQSQAVAAGPVAAPVAFPQPLYPQAANVAMPVEPDPAAGGGTAPATESPLPNFVPRKLKVFEGHWQGMDGRLMTEELARKLNYPRGLQGVLLGEVTLNAAFSGLLAGDLIVRIDDTPVTDMESFKAASRTVANRSDARISVLRKDNRPGAPVVRKLTVVLREAEGGLGFAQLEGAPMILAGDPRPHGYRGACTDCHPIGQGFELTPDPDLISLPPPTITRDMVARSVNPHEVRGPCEACHVIK |
| Enzyme Length | 275 |
| Uniprot Accession Number | Q2W8Q1 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | BINDING 224; /note="Heme 1; covalent"; /evidence="ECO:0000250|UniProtKB:A0A1S7LCW6, ECO:0000305|PubMed:23176475"; BINDING 227; /note="Heme 1; covalent"; /evidence="ECO:0000250|UniProtKB:A0A1S7LCW6, ECO:0000305|PubMed:23176475"; BINDING 268; /note="Heme 2; covalent"; /evidence="ECO:0000250|UniProtKB:A0A1S7LCW6, ECO:0000305|PubMed:23176475"; BINDING 271; /note="Heme 2; covalent"; /evidence="ECO:0000250|UniProtKB:A0A1S7LCW6, ECO:0000305|PubMed:23176475" |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 1.-.-.- |
| Enzyme Function | FUNCTION: Involved in redox-control of magnetite formation; oxidizes Fe(2+) to Fe(3+) or to mixed-valent Fe(2+)-Fe(3+) oxide minerals (PubMed:25775527). May control magnetite crystal size and number (Probable). Overproduction of MamP leads to more crystals than normal during exponential growth of normal size; in stationary phase crystal numbers become wild-type (PubMed:25048532). {ECO:0000269|PubMed:25048532, ECO:0000269|PubMed:25775527, ECO:0000305|PubMed:20212111}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Binding site (4); Chain (1); Metal binding (2); Motif (2); Mutagenesis (4); Region (1); Topological domain (2); Transmembrane (1) |
| Keywords | Biomineralization;Cell inner membrane;Cell membrane;Heme;Iron;Membrane;Metal-binding;Oxidoreductase;Reference proteome;Transmembrane;Transmembrane helix |
| Interact With | |
| Induction | INDUCTION: Constitutively expressed, levels are high for 24 hours after innoculation then decrease in stationary phase (up to 144 hours) (at protein level) (PubMed:25048532). Part of the probable 18 gene mamAB operon (Probable). {ECO:0000269|PubMed:25048532, ECO:0000305|PubMed:20212111}. |
| Subcellular Location | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305|PubMed:25048532}; Single-pass membrane protein {ECO:0000305|PubMed:25048532}. Note=Not seen in magnetosome membranes. {ECO:0000269|PubMed:25048532}. |
| Modified Residue | |
| Post Translational Modification | PTM: Subject to proteolytic cleavage which requires both MamE and MamO. {ECO:0000269|PubMed:26981620, ECO:0000269|PubMed:27302060}. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | MOTIF 210..230; /note=MCR (magnetochrome) 1; /evidence=ECO:0000305|PubMed:24097349; MOTIF 250..274; /note=MCR 2; /evidence=ECO:0000305|PubMed:24097349 |
| Gene Encoded By | |
| Mass | 28,912 |
| Kinetics | |
| Metal Binding | METAL 228; /note="Iron 1 (heme axial ligand)"; /evidence="ECO:0000250|UniProtKB:A0A1S7LCW6, ECO:0000305|PubMed:23176475"; METAL 272; /note="Iron 2 (heme axial ligand)"; /evidence="ECO:0000250|UniProtKB:A0A1S7LCW6, ECO:0000305|PubMed:23176475" |
| Rhea ID | |
| Cross Reference Brenda |