P03633 (B_BPPHX) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 64.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Internal scaffolding protein B Short name=GPB | ||
| Gene names |
| ||
| Organism | Enterobacteria phage phiX174 (Bacteriophage phi-X174) | ||
| Taxonomic identifier | 10847 [NCBI] | ||
| Taxonomic lineage | Viruses › ssDNA viruses › Microviridae › Microvirus | ||
| Virus host | Escherichia coli [TaxID: 562] |
Protein attributes
| Sequence length | 120 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| 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, possibly through affinity displacement by the protein J, or by proteolysis. Ref.2 |
| Subunit structure | Component of the procapsid complex composed of 60 copies of the internally located B, 240 copies of the external scaffolding protein D, 60 copies of each of the viral structural proteins F and G proteins, and 12 copies of H. |
| Subcellular location | |
| Post-translational modification | The proteolytic cleavage of the protein B by the host may occur directly inside the procapsid, thus releasing the scaffold protein in order to continue virion assembly. The B protein would be completely processed into small fragments by proteolytic digestion. |
| Sequence similarities | Belongs to the microviridae B protein family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Capsid assembly |
| Cellular component | Host cytoplasm |
| Technical term | 3D-structure |
| Gene Ontology (GO) | |
| Biological process | viral capsid assembly Inferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | host cell cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell viral procapsidInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
Sequences
References
| [1] | "Nucleotide sequence of bacteriophage phi X174 DNA." Sanger F., Air G.M., Barrell B.G., Brown N.L., Coulson A.R., Fiddes J.C., Hutchison C.A. III, Slocombe P.M., Smith M. Nature 265:687-695(1977) [PubMed: 870828] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. |
| [2] | "Isolation and identification of bacteriophage phi X174 prohead." Mukai R., Hamatake R.K., Hayashi M. Proc. Natl. Acad. Sci. U.S.A. 76:4877-4881(1979) [PubMed: 159449] [Abstract] Cited for: FUNCTION AND PROCAPSID STRUCTURE. |
| [3] | "Proteolysis of bacteriophage phi X174 prohead protein gpB by a protease located in the Escherichia coli outer membrane." Richardson D.L. Jr., Aoyama A., Hayashi M. J. Bacteriol. 170:5564-5571(1988) [PubMed: 2973457] [Abstract] Cited for: CLEAVAGE SITE, PROTEIN SEQUENCING 1-5. |
| [4] | "Structure of a viral procapsid with molecular scaffolding." Dokland T., McKenna R., Ilag L.L., Bowman B.R., Incardona N.L., Fane B.A., Rossmann M.G. Nature 389:308-313(1997) [PubMed: 9305849] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS). |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| EMBL GenBank DDBJ | J02482 Genomic DNA. Translation: AAA32572.1. | ||||||||||||||||||
| PIR | ZBBPF4. A04241. | ||||||||||||||||||
| RefSeq | NP_040705.1. NC_001422.1. | ||||||||||||||||||
3D structure databases | |||||||||||||||||||
| PDBe RCSB PDB PDBj |
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| ProteinModelPortal | P03633. | ||||||||||||||||||
| SMR | P03633. Positions 80-120. | ||||||||||||||||||
| ModBase | Search... | ||||||||||||||||||
Protocols and materials databases | |||||||||||||||||||
| StructuralBiologyKnowledgebase | Search... | ||||||||||||||||||
Genome annotation databases | |||||||||||||||||||
| GeneID | 2546405. | ||||||||||||||||||
| GenomeReviews | Gene locus phiX174p04 in contig J02482_GR. | ||||||||||||||||||
Phylogenomic databases | |||||||||||||||||||
| ProtClustDB | PHA0003. | ||||||||||||||||||
Family and domain databases | |||||||||||||||||||
| InterPro | IPR003513. Phage_B. [Graphical view] | ||||||||||||||||||
| Pfam | PF02304. Phage_B. 1 hit. [Graphical view] | ||||||||||||||||||
| ProDom | PD012751. Phage_B. 1 hit. [Graphical view] [Entries sharing at least one domain] | ||||||||||||||||||
| ProtoNet | Search... | ||||||||||||||||||
Entry information
| Entry name | B_BPPHX | ||||||||
| Accession | Primary (citable) accession number: P03633 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Viral Protein Annotation Program | ||||||||
Relevant documents
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |

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