IED ID | IndEnz0002004607 |
Enzyme Type ID | protease004607 |
Protein Name |
Probable periplasmic serine endoprotease DegP-like EC 3.4.21.107 Protease Do |
Gene Name | Mmwyl1_1102 |
Organism | Marinomonas sp. (strain MWYL1) |
Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Gammaproteobacteria Oceanospirillales Oceanospirillaceae Marinomonas unclassified Marinomonas Marinomonas sp. (strain MWYL1) |
Enzyme Sequence | MNRLLKQVCMVVVSSFMMASMLTHAASLPDFTELVEKASPAVVNISTEQTVTTKTANEGGQQLGPNSEELNEFFKHFFGQQPFGQQAPPQQGQRSSLGSGFIISHDGYVLTNNHVIDGADVIHVRLNDRREYVAKLVGTDPRTDLALLKIEADDLPIVKMGDSDKLKPGQWVLAIGSPFGFDYTVTAGIVSATGRSLPSDNYVPFIQTDVAINPGNSGGPLFNLDGEVVGINSQIYTRSGGFMGVSFAIPSKVAMSVVDQLKSDGKVSRAWLGVLIQDVNNELAESFGLDRSNGALISRVLPDSPAEKAGLKSGDIILEFNGQSIAHSGELPYIVGQMKADEKVDAKVYRDGKEQTISVTLEARPNDPKVVAQSQQDQNRLGMIVGEVPADMAKKFEIDNGVVIEQVLGGTAARNGLQQGDVITMLNGKRITSVAEFAKIAKDIPSGRSVPMRVIRQGYPMFIPFKIMD |
Enzyme Length | 469 |
Uniprot Accession Number | A6VUA4 |
Absorption | |
Active Site | ACT_SITE 114; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 144; /note=Charge relay system; /evidence=ECO:0000255; ACT_SITE 217; /note=Charge relay system; /evidence=ECO:0000250 |
Activity Regulation | |
Binding Site | |
Calcium Binding | |
catalytic Activity | CATALYTIC ACTIVITY: Reaction=Acts on substrates that are at least partially unfolded. The cleavage site P1 residue is normally between a pair of hydrophobic residues, such as Val-|-Val.; EC=3.4.21.107; |
DNA Binding | |
EC Number | 3.4.21.107 |
Enzyme Function | FUNCTION: Might be efficient in the degradation of transiently denatured and unfolded proteins which accumulate in the periplasm following stress conditions. {ECO:0000250}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Active site (3); Chain (1); Domain (2); Region (2); Signal peptide (1) |
Keywords | Hydrolase;Periplasm;Protease;Repeat;Serine protease;Signal;Stress response |
Interact With | |
Induction | |
Subcellular Location | SUBCELLULAR LOCATION: Periplasm {ECO:0000305}. |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | SIGNAL 1..25; /evidence=ECO:0000255 |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | - |
Motif | |
Gene Encoded By | |
Mass | 50,582 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda |