| IED ID | IndEnz0002008729 |
| Enzyme Type ID | protease008729 |
| Protein Name |
Neutral metalloprotease ShpI EC 3.4.24.- |
| Gene Name | shpI |
| Organism | Staphylococcus hyicus |
| Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Firmicutes Bacilli Bacillales Staphylococcaceae Staphylococcus Staphylococcus hyicus |
| Enzyme Sequence | MINKKKLVTSLVTSSLLATFTLGSFADAHTYIINNEDINKNAQESSIGTLKQNNFKQSTIDSMKPRNLQSFQEDKVFKAPKEKTPITERARKSENALSNSKLNDVRSFTTVNMRTNENERTAAKLKYNGKNTNVWVADNYITDKQAKNIGEEFDNKIDPLVKEKFGEPSDVDHDGKVNILVYDIKDDFETTGSYTGGYFHPRDLYDVPHSNKAEVFYMDTYPSMGTDKNNLNEKKVYSTLAHEYQHMVNANQKLLKEQKEDGMDVWLDEAFAMASEHMYLQKPLDHRIEYYNNSTSIANGHSLIKWNHRGDVLSNYALSYLFSQYLSAQSDNGDKIFKEILQDPANTSEALENAIHKHVDPKMSLGEFMTNFRVALEKKEATGLHGFNGAPGLNSISPKPVRELPQTLAPQGSVMFETTSPIKVPKDKDEKVNYVKVK |
| Enzyme Length | 438 |
| Uniprot Accession Number | Q08002 |
| Absorption | |
| Active Site | ACT_SITE 243; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095 |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by metal- and zinc-specific inhibitors, such as EDTA and 1,10-phenanthroline in vitro. Is resistant to all inhibitors of serine, cysteine and aspartic proteases. {ECO:0000269|PubMed:8121397}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.24.- |
| Enzyme Function | FUNCTION: Protease that has a low substrate specificity. Catalyzes the hydrolysis of glucagon, melittin and oxidized beta-insulin at various positions in vitro. Is not able to cleave elastin or the synthetic substrates FAGLA (a substrate for neutral proteinases) and FALGPA (a substrate for collagenase). {ECO:0000269|PubMed:8121397}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 55 degrees Celsius. Unstable at temperatures above 45 degrees Celsius. {ECO:0000269|PubMed:8121397}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.4-8.5. {ECO:0000269|PubMed:8121397}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (1); Metal binding (3); Propeptide (1); Signal peptide (1) |
| Keywords | Direct protein sequencing;Hydrolase;Metal-binding;Metalloprotease;Protease;Secreted;Signal;Zinc;Zymogen |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:8121397}. |
| Modified Residue | |
| Post Translational Modification | PTM: Several different N-terminal ends may be produced, the favored N-terminus is position 102. |
| Signal Peptide | SIGNAL 1..26; /evidence=ECO:0000305|PubMed:8121397 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 49,693 |
| Kinetics | |
| Metal Binding | METAL 242; /note="Zinc; catalytic"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10095, ECO:0000305|PubMed:8121397"; METAL 246; /note="Zinc; catalytic"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10095, ECO:0000305|PubMed:8121397"; METAL 269; /note="Zinc; catalytic"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10095, ECO:0000305|PubMed:8121397" |
| Rhea ID | |
| Cross Reference Brenda |