CAPSD_BPPHS
ID CAPSD_BPPHS Reviewed; 427 AA.
AC P03641;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 23-FEB-2022, entry version 127.
DE RecName: Full=Capsid protein F;
DE AltName: Full=F protein;
DE AltName: Full=GPF;
GN Name=F;
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 2-95.
RX PubMed=794486; DOI=10.1016/s0022-2836(76)80076-9;
RA Air G.M.;
RT "Amino acid sequences from the gene F (capsid) protein of bacteriophage
RT phiX174.";
RL J. Mol. Biol. 107:433-443(1976).
RN [4]
RP PROTEIN SEQUENCE OF 86-427.
RX PubMed=731694; DOI=10.1016/0022-2836(78)90347-9;
RA Air G.M., Coulson A.R., Fiddes J.C., Friedmann T., Hutchison C.A. III,
RA Sanger F., Slocombe P.M., Smith A.J.H.;
RT "Nucleotide sequence of the F protein coding region of bacteriophage
RT phiX174 and the amino acid sequence of its product.";
RL J. Mol. Biol. 125:247-254(1978).
RN [5]
RP FUNCTION.
RX PubMed=11991963; DOI=10.1128/jvi.76.11.5350-5356.2002;
RA Hafenstein S., Fane B.A.;
RT "phi X174 genome-capsid interactions influence the biophysical properties
RT of the virion: evidence for a scaffolding-like function for the genome
RT during the final stages of morphogenesis.";
RL J. Virol. 76:5350-5356(2002).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) OF 2-427, SUBCELLULAR LOCATION, AND
RP FUNCTION.
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 [7]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS), SUBCELLULAR LOCATION, AND FUNCTION.
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 [8]
RP X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS), INTERACTION WITH J PROTEIN, AND
RP SUBCELLULAR LOCATION.
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).
RN [9] {ECO:0007744|PDB:1CD3}
RP X-RAY CRYSTALLOGRAPHY (3.50 ANGSTROMS) OF 2-427, SUBUNIT, AND SUBCELLULAR
RP LOCATION.
RX PubMed=10329166; DOI=10.1006/jmbi.1999.2699;
RA Dokland T., Bernal R.A., Burch A., Pletnev S., Fane B.A., Rossmann M.G.;
RT "The role of scaffolding proteins in the assembly of the small, single-
RT stranded DNA virus phiX174.";
RL J. Mol. Biol. 288:595-608(1999).
RN [10]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=29229840; DOI=10.1073/pnas.1716614114;
RA Sun Y., Roznowski A.P., Tokuda J.M., Klose T., Mauney A., Pollack L.,
RA Fane B.A., Rossmann M.G.;
RT "Structural changes of tailless bacteriophage PhiX174 during penetration of
RT bacterial cell walls.";
RL Proc. Natl. Acad. Sci. U.S.A. 114:13708-13713(2017).
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
CC (PubMed:11991963, PubMed:1370343, PubMed:8158636). Upon virus binding
CC to host cell, one of the spikes dissociates from the capsid and the
CC virus interacts with LPS through the exposed EF loops on the F proteins
CC (PubMed:29229840). After the genome had been ejected, the channel
CC formed by the F proteins at the unique fivefold axis remains open
CC (PubMed:29229840). {ECO:0000269|PubMed:11991963,
CC ECO:0000269|PubMed:1370343, ECO:0000269|PubMed:29229840,
CC ECO:0000269|PubMed:8158636}.
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:0000269|PubMed:10329166, ECO:0000269|PubMed:9305849}.
CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000269|PubMed:10329166,
CC ECO:0000269|PubMed:1370343, ECO:0000269|PubMed:29229840,
CC ECO:0000269|PubMed:8158636, ECO:0000269|PubMed:9305849}.
CC -!- SIMILARITY: Belongs to the microviridae F protein family.
CC {ECO:0000305}.
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DR EMBL; J02482; AAA32578.1; -; Genomic_DNA.
DR PIR; B93185; ZFBPF4.
DR PDB; 1AL0; X-ray; 3.50 A; F=2-427.
DR PDB; 1CD3; X-ray; 3.50 A; F=2-427.
DR PDB; 1KVP; EM; 27.00 A; A=2-427.
DR PDB; 2BPA; X-ray; 3.00 A; 1=2-427.
DR PDBsum; 1AL0; -.
DR PDBsum; 1CD3; -.
DR PDBsum; 1KVP; -.
DR PDBsum; 2BPA; -.
DR SMR; P03641; -.
DR DIP; DIP-6198N; -.
DR IntAct; P03641; 2.
DR EvolutionaryTrace; P03641; -.
DR Proteomes; UP000005893; Genome.
DR GO; GO:0039615; C:T=1 icosahedral viral capsid; IDA:UniProtKB.
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; Direct protein sequencing;
KW Reference proteome; 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:0000269|PubMed:794486"
FT CHAIN 2..427
FT /note="Capsid protein F"
FT /id="PRO_0000164890"
FT TURN 6..8
FT /evidence="ECO:0007829|PDB:1AL0"
FT STRAND 11..14
FT /evidence="ECO:0007829|PDB:2BPA"
FT STRAND 17..23
FT /evidence="ECO:0007829|PDB:2BPA"
FT STRAND 25..36
FT /evidence="ECO:0007829|PDB:2BPA"
FT STRAND 41..52
FT /evidence="ECO:0007829|PDB:2BPA"
FT STRAND 55..58
FT /evidence="ECO:0007829|PDB:2BPA"
FT STRAND 63..73
FT /evidence="ECO:0007829|PDB:2BPA"
FT HELIX 74..88
FT /evidence="ECO:0007829|PDB:2BPA"
FT HELIX 89..91
FT /evidence="ECO:0007829|PDB:2BPA"
FT STRAND 97..99
FT /evidence="ECO:0007829|PDB:2BPA"
FT TURN 104..107
FT /evidence="ECO:0007829|PDB:2BPA"
FT HELIX 108..110
FT /evidence="ECO:0007829|PDB:2BPA"
FT STRAND 119..121
FT /evidence="ECO:0007829|PDB:2BPA"
FT HELIX 122..135
FT /evidence="ECO:0007829|PDB:2BPA"
FT HELIX 149..151
FT /evidence="ECO:0007829|PDB:2BPA"
FT HELIX 154..159
FT /evidence="ECO:0007829|PDB:2BPA"
FT TURN 169..171
FT /evidence="ECO:0007829|PDB:2BPA"
FT HELIX 193..211
FT /evidence="ECO:0007829|PDB:2BPA"
FT HELIX 216..222
FT /evidence="ECO:0007829|PDB:2BPA"
FT TURN 229..233
FT /evidence="ECO:0007829|PDB:2BPA"
FT STRAND 236..245
FT /evidence="ECO:0007829|PDB:2BPA"
FT STRAND 248..251
FT /evidence="ECO:0007829|PDB:2BPA"
FT TURN 255..259
FT /evidence="ECO:0007829|PDB:2BPA"
FT STRAND 261..264
FT /evidence="ECO:0007829|PDB:2BPA"
FT STRAND 266..277
FT /evidence="ECO:0007829|PDB:2BPA"
FT STRAND 280..291
FT /evidence="ECO:0007829|PDB:2BPA"
FT STRAND 296..299
FT /evidence="ECO:0007829|PDB:2BPA"
FT HELIX 302..305
FT /evidence="ECO:0007829|PDB:2BPA"
FT STRAND 306..308
FT /evidence="ECO:0007829|PDB:2BPA"
FT HELIX 311..314
FT /evidence="ECO:0007829|PDB:2BPA"
FT HELIX 318..321
FT /evidence="ECO:0007829|PDB:2BPA"
FT STRAND 327..330
FT /evidence="ECO:0007829|PDB:2BPA"
FT HELIX 331..333
FT /evidence="ECO:0007829|PDB:2BPA"
FT STRAND 343..346
FT /evidence="ECO:0007829|PDB:2BPA"
FT HELIX 350..352
FT /evidence="ECO:0007829|PDB:2BPA"
FT HELIX 361..363
FT /evidence="ECO:0007829|PDB:2BPA"
FT HELIX 380..384
FT /evidence="ECO:0007829|PDB:2BPA"
FT HELIX 388..394
FT /evidence="ECO:0007829|PDB:2BPA"
FT STRAND 402..415
FT /evidence="ECO:0007829|PDB:2BPA"
FT HELIX 420..424
FT /evidence="ECO:0007829|PDB:2BPA"
SQ SEQUENCE 427 AA; 48483 MW; 837DE99C73F426BC CRC64;
MSNIQTGAER MPHDLSHLGF LAGQIGRLIT ISTTPVIAGD SFEMDAVGAL RLSPLRRGLA
IDSTVDIFTF YVPHRHVYGE QWIKFMKDGV NATPLPTVNT TGYIDHAAFL GTINPDTNKI
PKHLFQGYLN IYNNYFKAPW MPDRTEANPN ELNQDDARYG FRCCHLKNIW TAPLPPETEL
SRQMTTSTTS IDIMGLQAAY ANLHTDQERD YFMQRYHDVI SSFGGKTSYD ADNRPLLVMR
SNLWASGYDV DGTDQTSLGQ FSGRVQQTYK HSVPRFFVPE HGTMFTLALV RFPPTATKEI
QYLNAKGALT YTDIAGDPVL YGNLPPREIS MKDVFRSGDS SKKFKIAEGQ WYRYAPSYVS
PAYHLLEGFP FIQEPPSGDL QERVLIRHHD YDQCFQSVQL LQWNSQVKFN VTVYRNLPTT
RDSIMTS
