CAPSF_BPPH2
ID CAPSF_BPPH2 Reviewed; 280 AA.
AC B3VMP4; P20344;
DT 29-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 1.
DT 29-SEP-2021, entry version 38.
DE RecName: Full=Capsid fiber protein {ECO:0000305};
DE AltName: Full=Gene product 8.5 {ECO:0000305};
DE Short=gp8.5 {ECO:0000305};
DE AltName: Full=Head fiber protein {ECO:0000305};
DE AltName: Full=Protein p8.5 {ECO:0000305};
GN Name=8.5 {ECO:0000312|EMBL:ACE96031.1};
OS Bacillus phage phi29 (Bacteriophage phi-29).
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Caudovirales; Salasmaviridae; Picovirinae; Salasvirus.
OX NCBI_TaxID=10756 {ECO:0000312|Proteomes:UP000001207};
OH NCBI_TaxID=1423; Bacillus subtilis.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Villegas A.P., Lingohr E.J., Ceyssens P.-J., Kropinski A.M.;
RL Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3803926; DOI=10.1016/0378-1119(86)90406-3;
RA Vlcek C., Paces V.;
RT "Nucleotide sequence of the late region of Bacillus phage phi 29 completes
RT the 19,285-bp sequence of phi 29 genome. Comparison with the homologous
RT sequence of phage PZA.";
RL Gene 46:215-225(1986).
RN [3]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=409854; DOI=10.1128/jvi.24.1.363-377.1977;
RA Reilly B.E., Nelson R.A., Anderson D.L.;
RT "Morphogenesis of bacteriophage phi 29 of Bacillus subtilis: mapping and
RT functional analysis of the head fiber gene.";
RL J. Virol. 24:363-377(1977).
RN [4]
RP SUBCELLULAR LOCATION.
RX PubMed=11562162; DOI=10.1006/jsbi.2001.4375;
RA Peterson C., Simon M., Hodges J., Mertens P., Higgins L., Egelman E.,
RA Anderson D.;
RT "Composition and mass of the bacteriophage phi29 prohead and virion.";
RL J. Struct. Biol. 135:18-25(2001).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.52 ANGSTROMS) OF 110-280, AND SUBUNIT.
RX PubMed=21383126; DOI=10.1073/pnas.1018097108;
RA Xiang Y., Rossmann M.G.;
RT "Structure of bacteriophage phi29 head fibers has a supercoiled triple
RT repeating helix-turn-helix motif.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:4806-4810(2011).
CC -!- FUNCTION: Protein that forms the 55 capsid fibers. These fibers are not
CC always present and may have been lost in some lab strains. They may
CC enhance the attachment of the virions onto the host cell wall.
CC {ECO:0000269|PubMed:409854}.
CC -!- SUBUNIT: Homotrimer. Forms a super helix coiled coil in the homotrimer.
CC {ECO:0000269|PubMed:21383126}.
CC -!- INTERACTION:
CC B3VMP4; B3VMP4: 8.5; NbExp=2; IntAct=EBI-15914419, EBI-15914419;
CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000269|PubMed:11562162,
CC ECO:0000269|PubMed:409854}.
CC -!- SIMILARITY: Belongs to the phi29likevirus major capsid fiber protein
CC family. {ECO:0000305}.
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DR EMBL; EU771092; ACE96031.1; -; Genomic_DNA.
DR EMBL; M14782; AAA32281.1; -; Genomic_DNA.
DR PIR; C25816; WMBPHF.
DR RefSeq; YP_002004537.1; NC_011048.1.
DR PDB; 3QC7; X-ray; 1.52 A; A=110-280.
DR PDB; 6QVK; EM; 3.60 A; 1e/1f/1g/1h/1i/1j/1k/1l/1m/1n/1o/1p/1q/1r/1s/1t/1u/1v/1w/1x/2Z/2a/2b/2c/2d/2e/2f/2g/2h/2i=1-280.
DR PDB; 6QYD; EM; 3.20 A; 1e/1f/1g/1h/1i/1j/1k/1l/1m/1n/1o/1p/1q/1r/1s/1t/1u/1v/1w/1x/2Z/2a/2b/2c/2d/2e/2f/2g/2h/2i=1-280.
DR PDB; 6QYY; X-ray; 1.80 A; A/B/C/D/E/F=1-116.
DR PDB; 6QZ0; EM; 3.20 A; 1e/1f/1g/1h/1i/1j/1k/1l/1m/1n/1o/1p/1q/1r/1s/1t/1u/1v/1w/1x/2Z/2a/2b/2c/2d/2e/2f/2g/2h/2i=1-280.
DR PDBsum; 3QC7; -.
DR PDBsum; 6QVK; -.
DR PDBsum; 6QYD; -.
DR PDBsum; 6QYY; -.
DR PDBsum; 6QZ0; -.
DR SMR; B3VMP4; -.
DR DIP; DIP-59620N; -.
DR GeneID; 6446512; -.
DR KEGG; vg:6446512; -.
DR Proteomes; UP000001207; Genome.
DR GO; GO:0098022; C:viral capsid, fiber; IDA:UniProtKB.
DR GO; GO:0046729; C:viral procapsid; IDA:CACAO.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
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 InterPro; IPR022741; Phage_B103_Gp8.
DR Pfam; PF11133; Phage_head_fibr; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Host-virus interaction; Late protein; Reference proteome;
KW Viral attachment to host cell; Virion; Virus entry into host cell.
FT CHAIN 1..280
FT /note="Capsid fiber protein"
FT /id="PRO_0000432921"
FT CONFLICT 242
FT /note="L -> I (in Ref. 2; AAA32281)"
FT /evidence="ECO:0000305"
FT STRAND 3..11
FT /evidence="ECO:0007829|PDB:6QYY"
FT STRAND 18..23
FT /evidence="ECO:0007829|PDB:6QYY"
FT STRAND 25..32
FT /evidence="ECO:0007829|PDB:6QYY"
FT STRAND 40..42
FT /evidence="ECO:0007829|PDB:6QYY"
FT STRAND 52..57
FT /evidence="ECO:0007829|PDB:6QYY"
FT STRAND 60..69
FT /evidence="ECO:0007829|PDB:6QYY"
FT STRAND 76..79
FT /evidence="ECO:0007829|PDB:6QYY"
FT HELIX 81..83
FT /evidence="ECO:0007829|PDB:6QYY"
FT STRAND 85..87
FT /evidence="ECO:0007829|PDB:6QYY"
FT HELIX 91..93
FT /evidence="ECO:0007829|PDB:6QYY"
FT STRAND 96..100
FT /evidence="ECO:0007829|PDB:6QYY"
FT STRAND 106..112
FT /evidence="ECO:0007829|PDB:6QYY"
FT HELIX 122..124
FT /evidence="ECO:0007829|PDB:3QC7"
FT HELIX 130..137
FT /evidence="ECO:0007829|PDB:3QC7"
FT HELIX 141..148
FT /evidence="ECO:0007829|PDB:3QC7"
FT HELIX 152..158
FT /evidence="ECO:0007829|PDB:3QC7"
FT HELIX 164..174
FT /evidence="ECO:0007829|PDB:3QC7"
FT HELIX 178..184
FT /evidence="ECO:0007829|PDB:3QC7"
FT HELIX 190..200
FT /evidence="ECO:0007829|PDB:3QC7"
FT HELIX 204..210
FT /evidence="ECO:0007829|PDB:3QC7"
FT HELIX 216..226
FT /evidence="ECO:0007829|PDB:3QC7"
FT STRAND 239..241
FT /evidence="ECO:0007829|PDB:3QC7"
FT HELIX 259..275
FT /evidence="ECO:0007829|PDB:3QC7"
SQ SEQUENCE 280 AA; 29489 MW; DA95A0B9BCDF4BF4 CRC64;
MMVSFTARAK SNVMAYRLLA YSQGDDIIEI SHAAENTIPD YVAVKDVDKG DLTQVNMYPL
AAWQVIAGSD IKVGDNLTTG KDGTAVPTDD PSTVFGYAVE EAQEGQLVTL VISRSKEISI
EVDDIKDAGD TGKRLLKINT PSGARNIIIE NEDAKALING ETTNTNKKNL QDLLFSDGNV
KAFLQATTTD ENKTALQQLL VSNADVLGLL SGNPTSDNKI NLRTMIGAGV PYSLPAATTT
TLGGVKKGAA VTASTATDVA TAVKDLNSLI TVLKNAGIIS
