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P03633 (B_BPPHX) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 64. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Internal scaffolding protein B

Short name=GPB
Gene names
Name:B
OrganismEnterobacteria phage phiX174 (Bacteriophage phi-X174)
Taxonomic identifier10847 [NCBI]
Taxonomic lineageVirusesssDNA virusesMicroviridaeMicrovirus
Virus hostEscherichia coli [TaxID: 562]

Protein attributes

Sequence length120 AA.
Sequence statusComplete.
Protein existenceEvidence 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

Host cytoplasm.

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 processCapsid assembly
   Cellular componentHost cytoplasm
   Technical term3D-structure
Gene Ontology (GO)
   Biological processviral capsid assembly

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componenthost cell cytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

viral procapsid

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 120120Internal scaffolding protein B
PRO_0000164870

Sites

Site76 – 772Cleavage; by host

Secondary structure

..... 120
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P03633 [UniParc].

Last modified July 21, 1986. Version 1.
Checksum: D8E52894116497ED

FASTA12013,843
        10         20         30         40         50         60 
MEQLTKNQAV ATSQEAVQNQ NEPQLRDENA HNDKSVHGVL NPTYQAGLRR DAVQPDIEAE 

        70         80         90        100        110        120 
RKKRDEIEAG KSYCSRRFGG ATCDDKSAQI YARFDKNDWR IQPAEFYRFH DAEVNTFGYF 

« Hide

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.
PIRZBBPF4. A04241.
RefSeqNP_040705.1. NC_001422.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1AL0X-ray3.50B1-120[»]
1CD3X-ray3.50B1-120[»]
ProteinModelPortalP03633.
SMRP03633. Positions 80-120.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID2546405.
GenomeReviewsGene locus phiX174p04 in contig J02482_GR.

Phylogenomic databases

ProtClustDBPHA0003.

Family and domain databases

InterProIPR003513. Phage_B.
[Graphical view]
PfamPF02304. Phage_B. 1 hit.
[Graphical view]
ProDomPD012751. Phage_B. 1 hit.
[Graphical view] [Entries sharing at least one domain]
ProtoNetSearch...

Entry information

Entry nameB_BPPHX
AccessionPrimary (citable) accession number: P03633
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: January 25, 2012
This is version 64 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families