| IED ID | IndEnz0002010680 |
| Enzyme Type ID | protease010680 |
| Protein Name |
Protease I Gene product 32 gp32 Gene product I gpI |
| Gene Name | I Z Mup32 Mup33 |
| Organism | Escherichia phage Mu (Bacteriophage Mu) |
| Taxonomic Lineage | Viruses Duplodnaviria Heunggongvirae Uroviricota Caudoviricetes Caudovirales Myoviridae (phages with contractile tails) Muvirus Escherichia phage Mu (Bacteriophage Mu) |
| Enzyme Sequence | MKKHAIGIAALNALSIDDDGWCQLLPAGHFSARDGRPFDVTGGQGWFIDGEIAGRLVEGVRALNQDVLIDYEHNQLRKDKGLPPEQLVAAGWFNADEMQWREGEGLFIHPRWTAAAQQRIDDGEFGYLSAVFPYDTATGAVLQIRLAALTNDPGATGMKKLTALAADLPDILQQENKPMNETLRKLLARLGVTVPENADITDEQATAALTALDTLEINAGKVAALSAELEKAQKAAVDLTKYVPVESYNALRDELAQATAQSATASLSAVLDKAEQEGRIFKSERTYLEQLGGQIGVAALSAQLEKKQPIAALSAMQTTTAKIPSQEKTAVAVLSADEQAAVKALGITEAEYLKMKQEQEK |
| Enzyme Length | 361 |
| Uniprot Accession Number | Q01267 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | |
| Enzyme Function | FUNCTION: Protease I is involved in virion assembly and maturation. Protease I cleaves the portal protein to yield mature procapsids competent for DNA packaging (Probable). Isoform scaffold protein Z probably helps the capsid proteins to assemble into a functional capsid (Probable). {ECO:0000305|PubMed:11922669, ECO:0000305|PubMed:8599204, ECO:0000305|PubMed:9495752}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Alternative sequence (1); Chain (1) |
| Keywords | Acetylation;Alternative initiation;Direct protein sequencing;Host cytoplasm;Hydrolase;Late protein;Protease;Reference proteome;Viral capsid assembly;Viral capsid maturation;Viral release from host cell |
| Interact With | |
| Induction | INDUCTION: Expressed in the late phase of the viral replicative cycle. Expression of late genes is activated by the viral late transcription activator C. {ECO:0000269|PubMed:8293968}. |
| Subcellular Location | SUBCELLULAR LOCATION: Host cytoplasm {ECO:0000305}. |
| Modified Residue | |
| Post Translational Modification | PTM: The N-terminus is acetylated. {ECO:0000305}. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 38,893 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |