Major spike protein G - Enterobacteria phage phiX174 (Isolate Sanger)

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P03643 (G_BPPHS) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 94. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Major spike protein G

Alternative name(s):
G protein
GPG

Gene names

Name:

Organism

Enterobacteria phage phiX174 (Isolate Sanger) (Bacteriophage phi-X174) [Complete proteome]

Taxonomic identifier

1217068 [NCBI]

Taxonomic lineage

Viruses › ssDNA viruses › Microviridae › Microvirus ›

Virus host

Escherichia coli C [TaxID: 498388]

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	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.

Ontologies

Keywords
Biological process	Host-virus interaction Viral attachment to host cell Viral genome injection through bacterial membranes Viral penetration into host cytoplasm Virus entry into host cell
Cellular component	Host cytoplasm Virion
Molecular function	Capsid protein
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological_process	viral attachment to host cell Inferred from electronic annotation. Source: UniProtKB-KW viral entry into host cell Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	host cell cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell viral capsid Inferred 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

175

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P03643 [UniParc].

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

FASTA

175

19,047

        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

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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] [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.

PIR

ZGBPF4. C93185.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1AL0	X-ray	3.50	G	1-175	[»]
1CD3	X-ray	3.50	G	1-175	[»]
1PHX	model	-	2	1-175	[»]
2BPA	X-ray	3.00	2	1-175	[»]

ProteinModelPortal

P03643.

SMR

P03643. Positions 1-175.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-6199N.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

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...

Other

EvolutionaryTrace

P03643.

Entry information

Entry name

G_BPPHS

Accession

Primary (citable) accession number: P03643

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	July 21, 1986
Last modified:	May 1, 2013
This is version 94 of the entry and version 1 of the sequence. [Complete history]

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

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protocols and materials databases

Phylogenomic databases

Family and domain databases

Other

Entry information

Relevant documents