| IED ID | IndEnz0002010798 |
| Enzyme Type ID | protease010798 |
| Protein Name |
Internal scaffolding protein B EC 3.4.-.- Scaffolding protein B GPB |
| Gene Name | B |
| Organism | Escherichia phage alpha3 (Bacteriophage alpha-3) |
| Taxonomic Lineage | Viruses Monodnaviria (single-stranded DNA viruses) Sangervirae Phixviricota Malgrandaviricetes Petitvirales Microviridae (isometric ssDNA phages) Bullavirinae Alphatrevirus Escherichia virus alpha3 Escherichia phage alpha3 (Bacteriophage alpha-3) |
| Enzyme Sequence | MQESINGNLSEERISGTQQSETRNGAPVNGSSEQQGTSGTEPNQLRFQSSVSDSERERQKAIDLEHRRAAFARHFGCAPGSEKHVENYSSFDEKDTRVQLAEFYRFNDGHFKKWGYF |
| Enzyme Length | 117 |
| Uniprot Accession Number | P31278 |
| 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. Autoproteolytic activity cleaves protein B and probably facilitates its removal through the pores of the procapsid. {ECO:0000250|UniProtKB:P03633}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Chain (1); Compositional bias (1); Region (1); Site (3) |
| Keywords | Autocatalytic cleavage;Host cytoplasm;Hydrolase;Protease;Reference proteome;Viral capsid assembly;Viral release from host cell |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Host cytoplasm {ECO:0000250|UniProtKB:P03633}. |
| 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:0000250|UniProtKB:P03633}. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 13,335 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |