ID   G_BPPHS                 Reviewed;         175 AA.
AC   P03643;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   02-SEP-2026, entry version 141.
DE   RecName: Full=Major spike protein G;
DE   AltName: Full=G protein;
DE   AltName: Full=GPG;
GN   Name=G;
OS   Enterobacteria phage phiX174 (Isolate Sanger) (Bacteriophage phi-X174).
OC   Viruses; Floreoviria; Sangervirae; Phixviricota; Microviricetes;
OC   Bullavirales; Sinsheimervirus; Escherichia phage phiX174.
OX   NCBI_TaxID=1217068;
OH   NCBI_TaxID=498388; Escherichia coli C.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=870828; DOI=10.1038/265687a0;
RA   Sanger F., Air G.M., Barrell B.G., Brown N.L., Coulson A.R., Fiddes J.C.,
RA   Hutchison C.A. III, Slocombe P.M., Smith M.;
RT   "Nucleotide sequence of bacteriophage phi X174 DNA.";
RL   Nature 265:687-695(1977).
RN   [2]
RP   SEQUENCE REVISION.
RX   PubMed=731693; DOI=10.1016/0022-2836(78)90346-7;
RA   Sanger F., Coulson A.R., Friedmann T., Air G.M., Barrell B.G., Brown N.L.,
RA   Fiddes J.C., Hutchison C.A. III, Slocombe P.M., Smith M.;
RT   "The nucleotide sequence of bacteriophage phiX174.";
RL   J. Mol. Biol. 125:225-246(1978).
RN   [3]
RP   PROTEIN SEQUENCE OF 1-67, AND NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1081600; DOI=10.1016/0022-2836(75)90147-3;
RA   Air G.M., Blackburn E.H., Sanger F., Coulson A.R.;
RT   "The nucleotide and amino acid sequences of the N (5') terminal region of
RT   gene G of bacteriophage phiphiX 174.";
RL   J. Mol. Biol. 96:703-719(1975).
RN   [4]
RP   PROTEIN SEQUENCE OF 63-175, AND NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1088827; DOI=10.1016/s0022-2836(76)80134-9;
RA   Air G.M., Sanger F., Coulson A.R.;
RT   "Nucleotide and amino acid sequences of gene G of omegaX174.";
RL   J. Mol. Biol. 108:519-533(1976).
RN   [5]
RP   FUNCTION.
RX   PubMed=10739948; DOI=10.1093/oxfordjournals.jbchem.a022643;
RA   Inagaki M., Tanaka A., Suzuki R., Wakashima H., Kawaura T., Karita S.,
RA   Nishikawa S., Kashimura N.;
RT   "Characterization of the binding of spike H protein of bacteriophage
RT   phiX174 with receptor lipopolysaccharides.";
RL   J. Biochem. 127:577-583(2000).
RN   [6]
RP   FUNCTION.
RX   PubMed=14553915; DOI=10.1016/s0378-1097(03)00601-3;
RA   Inagaki M., Kawaura T., Wakashima H., Kato M., Nishikawa S., Kashimura N.;
RT   "Different contributions of the outer and inner R-core residues of
RT   lipopolysaccharide to the recognition by spike H and G proteins of
RT   bacteriophage phiX174.";
RL   FEMS Microbiol. Lett. 226:221-227(2003).
RN   [7]
RP   CRYSTALLIZATION.
RX   PubMed=1370343; DOI=10.1038/355137a0;
RA   McKenna R., Xia D., Williangmann P., Ilag L.L., Krishnaswamy S.,
RA   Rossmann M.G., Olson N.H., Baker T.S., Incardona N.L.;
RT   "Atomic structure of single-stranded DNA bacteriophage phi X174 and its
RT   functional implications.";
RL   Nature 355:137-143(1992).
RN   [8]
RP   X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
RX   PubMed=8158636; DOI=10.1006/jmbi.1994.1253;
RA   McKenna R., Ilag L.L., Rossmann M.G.;
RT   "Analysis of the single-stranded DNA bacteriophage phi X174, refined at a
RT   resolution of 3.0 A.";
RL   J. Mol. Biol. 237:517-543(1994).
RN   [9]
RP   X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS).
RX   PubMed=9305849; DOI=10.1038/38537;
RA   Dokland T., McKenna R., Ilag L.L., Bowman B.R., Incardona N.L., Fane B.A.,
RA   Rossmann M.G.;
RT   "Structure of a viral procapsid with molecular scaffolding.";
RL   Nature 389:308-313(1997).
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.
CC       {ECO:0000269|PubMed:10739948, ECO:0000269|PubMed:14553915}.
CC   -!- SUBUNIT: Pentamerizes and interacts with H protein, F and B pentamers
CC       to form 12S pre-assembly complex. Joining of twelve 12S complex form
CC       the procapsid.
CC   -!- SUBCELLULAR LOCATION: Virion. Host cytoplasm.
CC   -!- SIMILARITY: Belongs to the microvirus G protein family. {ECO:0000305}.
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DR   EMBL; J02482; AAA32579.1; -; Genomic_DNA.
DR   PIR; C93185; ZGBPF4.
DR   PDB; 1AL0; X-ray; 3.50 A; G=1-175.
DR   PDB; 1CD3; X-ray; 3.50 A; G=1-175.
DR   PDB; 2BPA; X-ray; 3.00 A; 2=1-175.
DR   SMR; P03643; -.
DR   DIP; DIP-6199N; -.
DR   IntAct; P03643; 1.
DR   KEGG; vg:2546401; -.
DR   EvolutionaryTrace; P03643; -.
DR   Proteomes; UP000005893; Segment.
DR   GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0019028; C:viral capsid; IEA:UniProtKB-KW.
DR   GO; GO:0046718; P:symbiont entry into host cell; IEA:UniProtKB-KW.
DR   GO; GO:0044003; P:symbiont-mediated perturbation of host process; IEA:InterPro.
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; ssDNA viruses; 1.
DR   PDBsum; 1AL0; -.
DR   PDBsum; 1CD3; -.
DR   PDBsum; 2BPA; -.
PE   1: Evidence at protein level;
KW   3D-structure; Capsid protein; Direct protein sequencing; Host cytoplasm;
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..175
FT                   /note="Major spike protein G"
FT                   /id="PRO_0000164895"
FT   HELIX           2..4
FT                   /evidence="ECO:0007829|PDB:2BPA"
FT   STRAND          13..17
FT                   /evidence="ECO:0007829|PDB:1AL0"
FT   STRAND          26..28
FT                   /evidence="ECO:0007829|PDB:2BPA"
FT   STRAND          30..33
FT                   /evidence="ECO:0007829|PDB:2BPA"
FT   STRAND          36..49
FT                   /evidence="ECO:0007829|PDB:2BPA"
FT   STRAND          51..61
FT                   /evidence="ECO:0007829|PDB:2BPA"
FT   STRAND          69..83
FT                   /evidence="ECO:0007829|PDB:2BPA"
FT   STRAND          88..98
FT                   /evidence="ECO:0007829|PDB:2BPA"
FT   STRAND          108..110
FT                   /evidence="ECO:0007829|PDB:2BPA"
FT   STRAND          115..117
FT                   /evidence="ECO:0007829|PDB:2BPA"
FT   STRAND          120..130
FT                   /evidence="ECO:0007829|PDB:2BPA"
FT   STRAND          134..137
FT                   /evidence="ECO:0007829|PDB:1CD3"
FT   STRAND          139..150
FT                   /evidence="ECO:0007829|PDB:2BPA"
FT   STRAND          152..163
FT                   /evidence="ECO:0007829|PDB:2BPA"
SQ   SEQUENCE   175 AA;  19047 MW;  AA2418CD82666A7C CRC64;
     MFQTFISRHN SNFFSDKLVL TSVTPASSAP VLQTPKATSS TLYFDSLTVN AGNGGFLHCI
     QMDTSVNAAN QVVSVGADIA FDADPKFFAC LVRFESSSVP TTLPTAYDVY PLNGRHDGGY
     YTVKDCVTID VLPRTPGNNV YVGFMVWSNF TATKCRGLVS LNQVIKEIIC LQPLK
//