| IED ID | IndEnz0002001001 |
| Enzyme Type ID | protease001001 |
| Protein Name |
Internal scaffolding protein B EC 3.4.-.- Scaffolding protein B GPB |
| Gene Name | B |
| Organism | Enterobacteria phage phiX174 (Isolate Sanger) (Bacteriophage phi-X174) |
| Taxonomic Lineage | Viruses Monodnaviria (single-stranded DNA viruses) Sangervirae Phixviricota Malgrandaviricetes Petitvirales Microviridae (isometric ssDNA phages) Bullavirinae Sinsheimervirus Escherichia phage phiX174 (Bacteriophage phi-X174) Enterobacteria phage phiX174 (Isolate Sanger) (Bacteriophage phi-X174) |
| Enzyme Sequence | MEQLTKNQAVATSQEAVQNQNEPQLRDENAHNDKSVHGVLNPTYQAGLRRDAVQPDIEAERKKRDEIEAGKSYCSRRFGGATCDDKSAQIYARFDKNDWRIQPAEFYRFHDAEVNTFGYF |
| Enzyme Length | 120 |
| Uniprot Accession Number | P03633 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.-.- |
| Enzyme Function | FUNCTION: Participates in the assembly of the viral procapsid in the cytoplasm. Forms first a 12S pre-assembly complex with protein H, and F and G pentamers, then twelve 12S complexes are joined by the D protein to form the procapsid. Internal scaffold protein B is released from the procapsid upon genome packaging (PubMed:159449). Autoproteolytic activity cleaves protein B and probably facilitates its removal through the pores of the procapsid (PubMed:12473449). {ECO:0000269|PubMed:12473449, ECO:0000269|PubMed:159449}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Chain (1); Compositional bias (1); Helix (3); Region (1); Site (3) |
| Keywords | 3D-structure;Autocatalytic cleavage;Direct protein sequencing;Host cytoplasm;Hydrolase;Protease;Reference proteome;Viral capsid assembly;Viral release from host cell |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Host cytoplasm. |
| Modified Residue | |
| Post Translational Modification | PTM: The proteolytic cleavage of the internal scaffolding protein B releases the scaffold protein in order to continue virion assembly. {ECO:0000269|PubMed:12473449}. |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (2) |
| Cross Reference PDB | 1AL0; 1CD3; |
| Mapped Pubmed ID | 10329166; 1370343; 7613866; 8158636; |
| Motif | |
| Gene Encoded By | |
| Mass | 13,843 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |