ID   G_BPAL3                 Reviewed;         187 AA.
AC   P31281;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1993, sequence version 1.
DT   03-AUG-2022, entry version 113.
DE   RecName: Full=Major spike protein G;
DE   AltName: Full=G protein;
DE   AltName: Full=GPG;
GN   Name=G;
OS   Escherichia phage alpha3 (Bacteriophage alpha-3).
OC   Viruses; Monodnaviria; Sangervirae; Phixviricota; Malgrandaviricetes;
OC   Petitvirales; Microviridae; Bullavirinae; Alphatrevirus.
OX   NCBI_TaxID=10849;
OH   NCBI_TaxID=562; Escherichia coli.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1532908; DOI=10.1016/0167-4781(92)90440-b;
RA   Kodaira K., Nakano K., Okada S., Taketo A.;
RT   "Nucleotide sequence of the genome of the bacteriophage alpha 3:
RT   interrelationship of the genome structure and the gene products with those
RT   of the phages, phi X174, G4 and phi K.";
RL   Biochim. Biophys. Acta 1130:277-288(1992).
RN   [2]
RP   PARTIAL PROTEIN SEQUENCE.
RX   PubMed=387790; DOI=10.1016/s0021-9258(19)86359-7;
RA   Sims J., Capon D., Dressler D.;
RT   "dnaG (primase)-dependent origins of DNA replication. Nucleotide sequences
RT   of the negative strand initiation sites of bacteriophages St-1, phi K, and
RT   alpha 3.";
RL   J. Biol. Chem. 254:12615-12628(1979).
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS).
RX   PubMed=12473449; DOI=10.1016/s0022-2836(02)01201-9;
RA   Bernal R.A., Hafenstein S., Olson N.H., Bowman V.D., Chipman P.R.,
RA   Baker T.S., Fane B.A., Rossmann M.G.;
RT   "Structural studies of bacteriophage alpha3 assembly.";
RL   J. Mol. Biol. 325:11-24(2003).
CC   -!- FUNCTION: Attaches the circulating virion to the bacterial
CC       lipopolysaccharides which serve as receptor for the virus. Determines
CC       the phage host-range. Probably triggers with protein H the injection of
CC       the phage DNA into the host cytoplasm upon conformational changes
CC       induced by the interaction with host lipopolysaccharides (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBUNIT: The virion is composed of 60 copies each of the F, G, and J
CC       proteins, and 12 copies of the H protein. There are 12 spikes which are
CC       each composed of 5 G and one H proteins.
CC   -!- SUBCELLULAR LOCATION: Virion {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the microvirus G protein family. {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral capsid
CC       structure;
CC       URL="https://viperdb.scripps.edu/Info_Page.php?VDB=1n6g";
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DR   EMBL; X60322; CAA42882.1; -; Genomic_DNA.
DR   PIR; S22331; S22331.
DR   RefSeq; NP_039598.1; NC_001330.1.
DR   PDB; 1M06; X-ray; 3.50 A; G=1-187.
DR   PDB; 1M0F; EM; 16.00 A; G=1-187.
DR   PDB; 1RB8; X-ray; 3.50 A; G=1-187.
DR   PDBsum; 1M06; -.
DR   PDBsum; 1M0F; -.
DR   PDBsum; 1RB8; -.
DR   SMR; P31281; -.
DR   GeneID; 1260698; -.
DR   KEGG; vg:1260698; -.
DR   EvolutionaryTrace; P31281; -.
DR   Proteomes; UP000002137; Genome.
DR   GO; GO:0019028; C:viral capsid; IEA:UniProtKB-KW.
DR   GO; GO:0019048; P:modulation by virus of host process; IEA:InterPro.
DR   GO; GO:0046718; P:viral entry into host cell; IEA:UniProtKB-KW.
DR   GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW.
DR   Gene3D; 2.60.120.20; -; 1.
DR   InterPro; IPR016184; Capsid/spike_ssDNA_virus.
DR   InterPro; IPR003515; Spike_G.
DR   InterPro; IPR029053; Viral_coat.
DR   Pfam; PF02306; Phage_G; 1.
DR   PIRSF; PIRSF004159; Spike_G; 1.
DR   SUPFAM; SSF88645; SSF88645; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Capsid protein; Direct protein sequencing;
KW   Host-virus interaction; Reference proteome; Viral attachment to host cell;
KW   Viral genome ejection through host cell envelope;
KW   Viral penetration into host cytoplasm; Virion; Virus entry into host cell.
FT   CHAIN           1..187
FT                   /note="Major spike protein G"
FT                   /id="PRO_0000164892"
FT   STRAND          16..24
FT                   /evidence="ECO:0007829|PDB:1M06"
FT   STRAND          31..35
FT                   /evidence="ECO:0007829|PDB:1M06"
FT   STRAND          43..54
FT                   /evidence="ECO:0007829|PDB:1M06"
FT   STRAND          60..69
FT                   /evidence="ECO:0007829|PDB:1M06"
FT   STRAND          76..91
FT                   /evidence="ECO:0007829|PDB:1M06"
FT   STRAND          96..108
FT                   /evidence="ECO:0007829|PDB:1M06"
FT   STRAND          110..113
FT                   /evidence="ECO:0007829|PDB:1M06"
FT   HELIX           114..116
FT                   /evidence="ECO:0007829|PDB:1M06"
FT   STRAND          118..120
FT                   /evidence="ECO:0007829|PDB:1M06"
FT   STRAND          125..127
FT                   /evidence="ECO:0007829|PDB:1M06"
FT   STRAND          129..141
FT                   /evidence="ECO:0007829|PDB:1M06"
FT   STRAND          150..161
FT                   /evidence="ECO:0007829|PDB:1M06"
FT   STRAND          164..175
FT                   /evidence="ECO:0007829|PDB:1M06"
SQ   SEQUENCE   187 AA;  19585 MW;  66C4DB964F7758EF CRC64;
     MYQNFVTKHD TAIQTSRFSV TGNVIPAAPT GNIPVINGGS ITAERAVVNL YANMNVSTSS
     DGSFIVAMKV DTSPTDPNCV ISAGVNLSFA GTSYPIVGIV RFESASEQPT SIAGSEVEHY
     PIEMSVGSGG VCSARDCATV DIHPRTSGNN VFVGVICSSA KWTSGRVIGT IATTQVIHEY
     QVLQPLK