G_BPPHS
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 23-FEB-2022, entry version 132.
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; Monodnaviria; Sangervirae; Phixviricota; Malgrandaviricetes;
OC Petitvirales; Microviridae; Bullavirinae; Sinsheimervirus.
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 PDBsum; 1AL0; -.
DR PDBsum; 1CD3; -.
DR PDBsum; 2BPA; -.
DR SMR; P03643; -.
DR DIP; DIP-6199N; -.
DR IntAct; P03643; 1.
DR EvolutionaryTrace; P03643; -.
DR Proteomes; UP000005893; Genome.
DR GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
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; 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 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
