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G_BPG4
ID   G_BPG4                  Reviewed;         177 AA.
AC   P03644;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   23-FEB-2022, entry version 126.
DE   RecName: Full=Major spike protein G;
DE   AltName: Full=G protein;
DE   AltName: Full=GPG;
GN   Name=G;
OS   Escherichia phage G4 (Bacteriophage G4).
OC   Viruses; Monodnaviria; Sangervirae; Phixviricota; Malgrandaviricetes;
OC   Petitvirales; Microviridae; Bullavirinae; Gequatrovirus.
OX   NCBI_TaxID=10843;
OH   NCBI_TaxID=562; Escherichia coli.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=714153; DOI=10.1038/276236a0;
RA   Godson G.N., Barrell B.G., Staden R., Fiddes J.C.;
RT   "Nucleotide sequence of bacteriophage G4 DNA.";
RL   Nature 276:236-247(1978).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-81.
RX   PubMed=277911; DOI=10.1073/pnas.75.7.3094;
RA   Sims J., Dressler D.;
RT   "Site-specific initiation of a DNA fragment: nucleotide sequence of the
RT   bacteriophage G4 negative-strand initiation site.";
RL   Proc. Natl. Acad. Sci. U.S.A. 75:3094-3098(1978).
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
RX   PubMed=8642594; DOI=10.1006/jmbi.1996.0121;
RA   McKenna R., Bowman B.R., Iiag L.L., Rossmann M.G., Fane B.A.;
RT   "Atomic structure of the degraded procapsid particle of the bacteriophage
RT   G4: induced structural changes in the presence of calcium ions and
RT   functional implications.";
RL   J. Mol. Biol. 256:736-750(1996).
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}.
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DR   EMBL; V00657; CAA24020.1; -; Genomic_DNA.
DR   EMBL; M25080; AAA32328.1; -; Genomic_DNA.
DR   PIR; A04252; ZGBPG4.
DR   PDB; 1GFF; X-ray; 3.00 A; 2=1-177.
DR   PDBsum; 1GFF; -.
DR   SMR; P03644; -.
DR   DIP; DIP-6178N; -.
DR   MINT; P03644; -.
DR   EvolutionaryTrace; P03644; -.
DR   Proteomes; UP000002140; 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; Host-virus interaction; Reference proteome;
KW   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..177
FT                   /note="Major spike protein G"
FT                   /id="PRO_0000164893"
FT   CONFLICT        27
FT                   /note="A -> T (in Ref. 2; AAA32328)"
FT                   /evidence="ECO:0000305"
FT   STRAND          19..22
FT                   /evidence="ECO:0007829|PDB:1GFF"
FT   STRAND          29..32
FT                   /evidence="ECO:0007829|PDB:1GFF"
FT   STRAND          36..41
FT                   /evidence="ECO:0007829|PDB:1GFF"
FT   STRAND          44..47
FT                   /evidence="ECO:0007829|PDB:1GFF"
FT   STRAND          50..53
FT                   /evidence="ECO:0007829|PDB:1GFF"
FT   STRAND          55..61
FT                   /evidence="ECO:0007829|PDB:1GFF"
FT   STRAND          69..81
FT                   /evidence="ECO:0007829|PDB:1GFF"
FT   STRAND          87..96
FT                   /evidence="ECO:0007829|PDB:1GFF"
FT   STRAND          109..111
FT                   /evidence="ECO:0007829|PDB:1GFF"
FT   STRAND          115..117
FT                   /evidence="ECO:0007829|PDB:1GFF"
FT   STRAND          122..124
FT                   /evidence="ECO:0007829|PDB:1GFF"
FT   STRAND          126..131
FT                   /evidence="ECO:0007829|PDB:1GFF"
FT   STRAND          139..148
FT                   /evidence="ECO:0007829|PDB:1GFF"
FT   STRAND          150..152
FT                   /evidence="ECO:0007829|PDB:1GFF"
FT   STRAND          154..157
FT                   /evidence="ECO:0007829|PDB:1GFF"
FT   STRAND          159..168
FT                   /evidence="ECO:0007829|PDB:1GFF"
SQ   SEQUENCE   177 AA;  18820 MW;  40ED2E63CA9EC384 CRC64;
     MFQKFISKHN APINSTQLAA TKTPAVAAPV LSVPNLSRST ILINATTTAV TTHSGLCHVV
     RIDETNPTNH HALSIAGSLS NVPADMIAFA IRFEVADGVV PTAVPALYDV YPIETFNNGK
     AISFKDAVTI DSHPRTVGND VYAGIMLWSN AWTASTISGV LSVNQVNREA TVLQPLK
 
 
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