CAPSD_BPG4
ID CAPSD_BPG4 Reviewed; 427 AA.
AC P03642;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 23-FEB-2022, entry version 111.
DE RecName: Full=Capsid protein F;
DE AltName: Full=F protein;
DE AltName: Full=GPF;
GN Name=F;
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 X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS), AND SEQUENCE REVISION TO 36-37; 69
RP AND 282.
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: Assembles to form an icosahedral capsid with a T=1 symmetry,
CC about 30 nm in diameter, and consisting of 60 capsid proteins F. Upon
CC virus binding to host cell, one of the spikes dissociates from the
CC capsid and the virus interacts with LPS through the exposed EF loops on
CC the F proteins. After the genome had been ejected, the channel formed
CC by the F proteins at the unique fivefold axis remains open.
CC {ECO:0000250|UniProtKB:P03641}.
CC -!- SUBUNIT: Pentamerizes and interacts with H protein, G and B pentamers
CC to form 12S pre-assembly complex. By binding with protein D, induces
CC joining of twelve 12S complex to form the procapsid. The procapsid has
CC an external scaffold made of 240 copies of protein D, 60 copies of the
CC internally located B protein, and contains 60 copies of each of the
CC viral structural proteins F and G. Upon genome packaging, interacts
CC with protein J. The mature virion is composed of 60 copies each of the
CC F, G, and J proteins, and 12 copies of the H protein.
CC {ECO:0000250|UniProtKB:P03641}.
CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000250|UniProtKB:P03641}.
CC -!- SIMILARITY: Belongs to the microviridae F protein family.
CC {ECO:0000305}.
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DR EMBL; V00657; CAA24019.1; -; Genomic_DNA.
DR PIR; A04250; ZFBPG4.
DR PDB; 1GFF; X-ray; 3.00 A; 1=2-427.
DR PDBsum; 1GFF; -.
DR SMR; P03642; -.
DR DIP; DIP-6177N; -.
DR MINT; P03642; -.
DR PRIDE; P03642; -.
DR EvolutionaryTrace; P03642; -.
DR Proteomes; UP000002140; Genome.
DR GO; GO:0039615; C:T=1 icosahedral viral capsid; IEA:UniProtKB-KW.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR GO; GO:0046718; P:viral entry into host cell; IEA:UniProtKB-KW.
DR Gene3D; 2.60.169.10; -; 1.
DR InterPro; IPR016184; Capsid/spike_ssDNA_virus.
DR InterPro; IPR003514; Microviridae_protein_F.
DR InterPro; IPR037002; Microviridae_protein_F_sf.
DR Pfam; PF02305; Phage_F; 1.
DR SUPFAM; SSF88645; SSF88645; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Capsid protein; Reference proteome;
KW T=1 icosahedral capsid protein;
KW Viral genome ejection through host cell envelope;
KW Viral penetration into host cytoplasm; Virion; Virus entry into host cell.
FT INIT_MET 1
FT /note="Removed; by host"
FT /evidence="ECO:0000250|UniProtKB:P03641"
FT CHAIN 2..427
FT /note="Capsid protein F"
FT /id="PRO_0000164888"
FT STRAND 17..23
FT /evidence="ECO:0007829|PDB:1GFF"
FT STRAND 25..27
FT /evidence="ECO:0007829|PDB:1GFF"
FT STRAND 29..36
FT /evidence="ECO:0007829|PDB:1GFF"
FT STRAND 41..52
FT /evidence="ECO:0007829|PDB:1GFF"
FT STRAND 55..58
FT /evidence="ECO:0007829|PDB:1GFF"
FT STRAND 63..74
FT /evidence="ECO:0007829|PDB:1GFF"
FT HELIX 75..78
FT /evidence="ECO:0007829|PDB:1GFF"
FT HELIX 80..88
FT /evidence="ECO:0007829|PDB:1GFF"
FT HELIX 89..91
FT /evidence="ECO:0007829|PDB:1GFF"
FT HELIX 108..110
FT /evidence="ECO:0007829|PDB:1GFF"
FT STRAND 118..120
FT /evidence="ECO:0007829|PDB:1GFF"
FT HELIX 122..135
FT /evidence="ECO:0007829|PDB:1GFF"
FT HELIX 149..151
FT /evidence="ECO:0007829|PDB:1GFF"
FT TURN 154..159
FT /evidence="ECO:0007829|PDB:1GFF"
FT HELIX 193..211
FT /evidence="ECO:0007829|PDB:1GFF"
FT HELIX 216..221
FT /evidence="ECO:0007829|PDB:1GFF"
FT TURN 222..224
FT /evidence="ECO:0007829|PDB:1GFF"
FT TURN 229..233
FT /evidence="ECO:0007829|PDB:1GFF"
FT STRAND 236..245
FT /evidence="ECO:0007829|PDB:1GFF"
FT STRAND 248..251
FT /evidence="ECO:0007829|PDB:1GFF"
FT TURN 255..259
FT /evidence="ECO:0007829|PDB:1GFF"
FT STRAND 261..264
FT /evidence="ECO:0007829|PDB:1GFF"
FT STRAND 266..277
FT /evidence="ECO:0007829|PDB:1GFF"
FT STRAND 280..291
FT /evidence="ECO:0007829|PDB:1GFF"
FT HELIX 302..305
FT /evidence="ECO:0007829|PDB:1GFF"
FT STRAND 306..308
FT /evidence="ECO:0007829|PDB:1GFF"
FT HELIX 311..314
FT /evidence="ECO:0007829|PDB:1GFF"
FT HELIX 318..321
FT /evidence="ECO:0007829|PDB:1GFF"
FT STRAND 327..330
FT /evidence="ECO:0007829|PDB:1GFF"
FT TURN 331..334
FT /evidence="ECO:0007829|PDB:1GFF"
FT STRAND 335..337
FT /evidence="ECO:0007829|PDB:1GFF"
FT STRAND 343..346
FT /evidence="ECO:0007829|PDB:1GFF"
FT HELIX 350..352
FT /evidence="ECO:0007829|PDB:1GFF"
FT TURN 361..365
FT /evidence="ECO:0007829|PDB:1GFF"
FT HELIX 381..383
FT /evidence="ECO:0007829|PDB:1GFF"
FT HELIX 388..394
FT /evidence="ECO:0007829|PDB:1GFF"
FT STRAND 395..397
FT /evidence="ECO:0007829|PDB:1GFF"
FT STRAND 402..414
FT /evidence="ECO:0007829|PDB:1GFF"
FT HELIX 420..423
FT /evidence="ECO:0007829|PDB:1GFF"
SQ SEQUENCE 427 AA; 48703 MW; 738F4D048FEDC367 CRC64;
MSNVQTSADR VPHDLSHLVF EAGKIGRLKT ISWTPVVAGD SFECDMVGAI RLSPLRRGLA
VDSRVDIFSF YIPHRHIYGQ QWINFMKDGV NASPLPPVTC SSGWDSAAYL GTIPSSTLKV
PKFLHQGYLN IYNNYFKPPW SDDLTYANPS NMPSEDYKWG VRVANLKSIW TAPLPPDTRT
SENMTTGTST IDIMGLQAAY AKLHTEQERD YFMTRYRDIM KEFGGHTSYD GDNRPLLLMR
SEFWASGYDV DGTDQSSLGQ FSGRVQQTFN HKVPRFYVPE HGVIMTLAVT RFPPTHEMEM
HYLVGKENLT YTDIACDPAL MANLPPREVS LKEFFHSSPD SAKFKIAEGQ WYRTQPDRVA
FPYNALDGFP FYSALPSTEL KDRVLVNTNN YDEIFQSMQL AHWNMQTKFN INVYRHMPTT
RDSIMTS
