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P03643 (G_BPPHS) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 100. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Major spike protein G
Alternative name(s):
G protein
GPG
Gene names
Name:G
OrganismEnterobacteria phage phiX174 (Isolate Sanger) (Bacteriophage phi-X174) [Reference proteome]
Taxonomic identifier1217068 [NCBI]
Taxonomic lineageVirusesssDNA virusesMicroviridaeMicrovirus
Virus hostEscherichia coli C [TaxID: 498388]

Protein attributes

Sequence length175 AA.
Sequence statusComplete.
Protein existenceEvidence 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

Pentamerizes 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

Virion. Host cytoplasm.

Sequence similarities

Belongs to the microvirus G protein family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 175175Major spike protein G
PRO_0000164895

Secondary structure

........................... 175
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P03643 [UniParc].

Last modified July 21, 1986. Version 1.
Checksum: AA2418CD82666A7C

FASTA17519,047
        10         20         30         40         50         60 
MFQTFISRHN SNFFSDKLVL TSVTPASSAP VLQTPKATSS TLYFDSLTVN AGNGGFLHCI 

        70         80         90        100        110        120 
QMDTSVNAAN QVVSVGADIA FDADPKFFAC LVRFESSSVP TTLPTAYDVY PLNGRHDGGY 

       130        140        150        160        170 
YTVKDCVTID VLPRTPGNNV YVGFMVWSNF TATKCRGLVS LNQVIKEIIC LQPLK 

« 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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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.
PIRZGBPF4. C93185.
RefSeqNP_040712.1. NC_001422.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1AL0X-ray3.50G1-175[»]
1CD3X-ray3.50G1-175[»]
1PHXmodel-21-175[»]
2BPAX-ray3.0021-175[»]
ProteinModelPortalP03643.
SMRP03643. Positions 1-175.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-6199N.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID2546401.

Phylogenomic databases

ProtClustDBPHA0010.

Family and domain databases

InterProIPR016184. Capsid/spike_ssDNA_virus.
IPR003515. Spike_G.
[Graphical view]
PfamPF02306. Phage_G. 1 hit.
[Graphical view]
PIRSFPIRSF004159. Spike_G. 1 hit.
ProDomPD013365. Spike_G. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMSSF88645. SSF88645. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP03643.

Entry information

Entry nameG_BPPHS
AccessionPrimary (citable) accession number: P03643
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: February 19, 2014
This is version 100 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references