IED ID | IndEnz0002010517 |
Enzyme Type ID | protease010517 |
Protein Name |
Transglutaminase-activating metalloprotease TAMEP TGase-activating protease EC 3.4.-.- Transglutaminase-activating metalloproteinase |
Gene Name | |
Organism | Streptomyces mobaraensis (Streptoverticillium mobaraense) |
Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Actinobacteria Actinomycetia (high G+C Gram-positive bacteria) Streptomycetales Streptomycetaceae Streptomyces Streptomyces mobaraensis (Streptoverticillium mobaraense) |
Enzyme Sequence | MRPTPQRRAVATGALVAVTAMLAVGVQTTSANAGQDKAAHPAPRQSIHKPDPGAEPVKLTPSQRAELIRDANATKAETAKNLGLGAKEKLVVKDVVKDKNGTLHTRYERTYDGLPVLGGDLVVDATRSGQVKTAAKATKQRIAVASTTPSLAASAAEKDAVKAARAKGSKAGKADKAPRKVVWAAKGTPVLAYETVVGGVQDDGTPSQLHVITDAKTGKKLFEFQGVKQGTGNSQHSGQVQIGTTKSGSSYQMNDTTRGGHKTYNLNHGSSGTGTLFTDSDDVWGNGTNSDPATAGVDAHYGAQLTWDYYKNVHGRNGIRGDGVGAYSRVHYGNNYVNAFWDDSCFCMTYGDGNGIPLTSIDVAAHEMTHGVTSATANLTYSGESGGLNEATSDMMATAVEFWANNPADPGDYLIGEKININGDGTPLRYMDKPSKDGASKDAWYSGLGGIDVHYSSGPANHWFYLASEGSGPKDIGGVHYDSPTSDGLPVTGVGRDNAAKIWFKALTERMQSNTDYKGARDATLWAAGELFGVNSDTYNNVANAWAAINVGPRASSGVSVTSPGDQTSIVNQAVSLQIKATGSTSGALTYSATGLPAGLSINASTGLISGTPTTTGTSNVTVTVKDSAGKTGSTSFKWTVNTTGGGSVFENTTQVAIPDAGAAVTSPIVVTRSGNGPSALKVDVNITHTYRGDLTIDLVAPNGKTWRLKNSDAWDSAADVSETYTVDASSVSANGTWKLKVQDVYSGDSGTIDKWRLTF |
Enzyme Length | 760 |
Uniprot Accession Number | P83543 |
Absorption | |
Active Site | ACT_SITE 367; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095; ACT_SITE 454; /note=Proton donor; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095 |
Activity Regulation | |
Binding Site | |
Calcium Binding | |
catalytic Activity | |
DNA Binding | |
EC Number | 3.4.-.- |
Enzyme Function | FUNCTION: Cleaves the N-terminal propeptide of transglutaminase thus activating it. {ECO:0000269|PubMed:12869197}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Active site (2); Chain (1); Domain (1); Metal binding (3); Propeptide (1); Region (2); Signal peptide (1) |
Keywords | Direct protein sequencing;Hydrolase;Metal-binding;Metalloprotease;Protease;Secreted;Signal;Zinc |
Interact With | |
Induction | |
Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:12869197}. |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | SIGNAL 1..33; /evidence=ECO:0000255 |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | - |
Motif | |
Gene Encoded By | |
Mass | 79,181 |
Kinetics | |
Metal Binding | METAL 366; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095; METAL 370; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095; METAL 390; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095 |
Rhea ID | |
Cross Reference Brenda |