P03643 (G_BPPHX) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 86.
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: Major spike protein G Alternative name(s): G protein GPG | ||
| 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 | 175 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | Attaches the circulating virion to the bacterial lipopolysaccharides which serve as receptor for the virus. Determines the phage host-range. Probably triggers with protein H the injection of the phage DNA into the host cytoplasm upon conformational changes induced by the interaction with host lipopolysaccharides. Ref.5 Ref.6 |
| Subunit structure | Pentamerises and interacts with H protein, F and B pentamers to form 12S pre-assembly complex. Joining of twelve 12S complex form the procapsid. |
| Subcellular location | |
| Sequence similarities | Belongs to the microvirus G protein family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Host-virus interaction Initiation of viral infection Viral attachment to host cell Viral genome injection through bacterial membranes Viral penetration into host cytoplasm |
| Cellular component | Host cytoplasm Virion |
| Molecular function | Capsid protein |
| Technical term | 3D-structure Direct protein sequencing |
| Gene Ontology (GO) | |
| Biological process | virus-host interaction Inferred from electronic annotation. Source: InterPro |
| Cellular component | host cell cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell viral capsidInferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||||||||||||||||||||||
Molecule processing | |||||||||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 175 | 175 | Major spike protein G | PRO_0000164895 | |||||||||||||||||||||||||||
Secondary structure | |||||||||||||||||||||||||||||||
Helix Strand Turn | |||||||||||||||||||||||||||||||
| Beta strand | 26 – 28 | 3 | |||||||||||||||||||||||||||||
| Beta strand | 30 – 33 | 4 | |||||||||||||||||||||||||||||
| Beta strand | 36 – 49 | 14 | |||||||||||||||||||||||||||||
| Beta strand | 51 – 61 | 11 | |||||||||||||||||||||||||||||
| Beta strand | 69 – 83 | 15 | |||||||||||||||||||||||||||||
| Beta strand | 88 – 98 | 11 | |||||||||||||||||||||||||||||
| Beta strand | 108 – 110 | 3 | |||||||||||||||||||||||||||||
| Beta strand | 115 – 117 | 3 | |||||||||||||||||||||||||||||
| Beta strand | 120 – 130 | 11 | |||||||||||||||||||||||||||||
| Beta strand | 139 – 150 | 12 | |||||||||||||||||||||||||||||
| Beta strand | 152 – 163 | 12 | |||||||||||||||||||||||||||||
Sequences
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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] | "The nucleotide sequence of bacteriophage phiX174." Sanger F., Coulson A.R., Friedmann T., Air G.M., Barrell B.G., Brown N.L., Fiddes J.C., Hutchison C.A. III, Slocombe P.M., Smith M. J. Mol. Biol. 125:225-246(1978) [PubMed: 731693] [Abstract] Cited for: SEQUENCE REVISION. |
| [3] | "The nucleotide and amino acid sequences of the N (5') terminal region of gene G of bacteriophage phiphiX 174." Air G.M., Blackburn E.H., Sanger F., Coulson A.R. J. Mol. Biol. 96:703-719(1975) [PubMed: 1081600] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-67, NUCLEOTIDE SEQUENCE [GENOMIC DNA]. |
| [4] | "Nucleotide and amino acid sequences of gene G of omegaX174." Air G.M., Sanger F., Coulson A.R. J. Mol. Biol. 108:519-533(1976) [PubMed: 1088827] [Abstract] Cited for: PROTEIN SEQUENCE OF 63-175, NUCLEOTIDE SEQUENCE [GENOMIC DNA]. |
| [5] | "Characterization of the binding of spike H protein of bacteriophage phiX174 with receptor lipopolysaccharides." Inagaki M., Tanaka A., Suzuki R., Wakashima H., Kawaura T., Karita S., Nishikawa S., Kashimura N. J. Biochem. 127:577-583(2000) [PubMed: 10739948] [Abstract] Cited for: FUNCTION. |
| [6] | "Different contributions of the outer and inner R-core residues of lipopolysaccharide to the recognition by spike H and G proteins of bacteriophage phiX174." Inagaki M., Kawaura T., Wakashima H., Kato M., Nishikawa S., Kashimura N. FEMS Microbiol. Lett. 226:221-227(2003) [PubMed: 14553915] [Abstract] Cited for: FUNCTION. |
| [7] | "Atomic structure of single-stranded DNA bacteriophage phi X174 and its functional implications." McKenna R., Xia D., Williangmann P., Ilag L.L., Krishnaswamy S., Rossmann M.G., Olson N.H., Baker T.S., Incardona N.L. Nature 355:137-143(1992) [PubMed: 1370343] [Abstract] Cited for: CRYSTALLIZATION. |
| [8] | "Analysis of the single-stranded DNA bacteriophage phi X174, refined at a resolution of 3.0 A." McKenna R., Ilag L.L., Rossmann M.G. J. Mol. Biol. 237:517-543(1994) [PubMed: 8158636] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS). |
| [9] | "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: AAA32579.1. | ||||||||||||||||||||||||||||||
| PIR | ZGBPF4. C93185. | ||||||||||||||||||||||||||||||
| RefSeq | NP_040712.1. NC_001422.1. | ||||||||||||||||||||||||||||||
3D structure databases | |||||||||||||||||||||||||||||||
| PDBe RCSB PDB PDBj |
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| ProteinModelPortal | P03643. | ||||||||||||||||||||||||||||||
| SMR | P03643. Positions 1-175. | ||||||||||||||||||||||||||||||
| ModBase | Search... | ||||||||||||||||||||||||||||||
Protein-protein interaction databases | |||||||||||||||||||||||||||||||
| DIP | DIP-6199N. | ||||||||||||||||||||||||||||||
Protocols and materials databases | |||||||||||||||||||||||||||||||
| StructuralBiologyKnowledgebase | Search... | ||||||||||||||||||||||||||||||
Genome annotation databases | |||||||||||||||||||||||||||||||
| GeneID | 2546401. | ||||||||||||||||||||||||||||||
| GenomeReviews | Gene locus G in contig J02482_GR. | ||||||||||||||||||||||||||||||
Phylogenomic databases | |||||||||||||||||||||||||||||||
| ProtClustDB | PHA0010. | ||||||||||||||||||||||||||||||
Family and domain databases | |||||||||||||||||||||||||||||||
| InterPro | IPR016184. Capsid/spike_ssDNA_virus. IPR003515. Spike_G. [Graphical view] | ||||||||||||||||||||||||||||||
| Pfam | PF02306. Phage_G. 1 hit. [Graphical view] | ||||||||||||||||||||||||||||||
| PIRSF | PIRSF004159. Spike_G. 1 hit. | ||||||||||||||||||||||||||||||
| ProDom | PD013365. Spike_G. 1 hit. [Graphical view] [Entries sharing at least one domain] | ||||||||||||||||||||||||||||||
| SUPFAM | SSF88645. Capsid/spike_ssDNA_virus. 1 hit. | ||||||||||||||||||||||||||||||
| ProtoNet | Search... | ||||||||||||||||||||||||||||||
Entry information
| Entry name | G_BPPHX | ||||||||
| Accession | Primary (citable) accession number: P03643 | ||||||||
| 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 |

Clusters with