SPIKE_BPP2
ID SPIKE_BPP2 Reviewed; 211 AA.
AC P31340;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Spike protein {ECO:0000305};
DE AltName: Full=Baseplate assembly protein gpV {ECO:0000305};
DE AltName: Full=Gene V protein {ECO:0000305};
DE Short=GpV;
GN Name=V;
OS Escherichia phage P2 (Bacteriophage P2).
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Caudovirales; Myoviridae; Peduovirinae; Peduovirus.
OX NCBI_TaxID=10679;
OH NCBI_TaxID=543; Enterobacteriaceae.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX PubMed=7483254; DOI=10.1006/viro.1995.1551;
RA Haggaard-Ljungquist E., Jacobsen E., Rishovd S., Six E.W., Nilssen O.,
RA Sunshine M.G., Lindqvist B.H., Kim K.-J., Barreiro V., Koonin E.V.,
RA Calendar R.;
RT "Bacteriophage P2: genes involved in baseplate assembly.";
RL Virology 213:109-121(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-72.
RX PubMed=3981640; DOI=10.1016/0022-2836(85)90226-8;
RA Christie G.E., Calendar R.;
RT "Bacteriophage P2 late promoters. II. Comparison of the four late promoter
RT sequences.";
RL J. Mol. Biol. 181:373-382(1985).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND SEQUENCE REVISION.
RA Christie G.E.;
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-24.
RX PubMed=8178426; DOI=10.1006/viro.1994.1199;
RA Linderoth N.A., Julien B., Flick K.E., Calendar R., Christie G.E.;
RT "Molecular cloning and characterization of bacteriophage P2 genes R and S
RT involved in tail completion.";
RL Virology 200:347-359(1994).
RN [5] {ECO:0007744|PDB:3AQJ}
RP X-RAY CRYSTALLOGRAPHY (1.27 ANGSTROMS) OF 87-211, FUNCTION, SUBCELLULAR
RP LOCATION, COFACTOR, AND SUBUNIT.
RX PubMed=21821878; DOI=10.1107/s1744309111005999;
RA Yamashita E., Nakagawa A., Takahashi J., Tsunoda K., Yamada S., Takeda S.;
RT "The host-binding domain of the P2 phage tail spike reveals a trimeric
RT iron-binding structure.";
RL Acta Crystallogr. F 67:837-841(2011).
RN [6] {ECO:0007744|PDB:3QR7, ECO:0007744|PDB:3QR8}
RP X-RAY CRYSTALLOGRAPHY (0.94 ANGSTROMS) OF 97-211 IN COMPLEX WITH CHLORIDE,
RP AND COFACTOR.
RX PubMed=22325780; DOI=10.1016/j.str.2011.12.009;
RA Browning C., Shneider M.M., Bowman V.D., Schwarzer D., Leiman P.G.;
RT "Phage pierces the host cell membrane with the iron-loaded spike.";
RL Structure 20:326-339(2012).
CC -!- FUNCTION: Forms the small spikes on the baseplate that plug the end of
CC the tube before DNA ejection and form a channel perforating the host
CC membrane during ejection. Involved in baseplate assembly.
CC {ECO:0000269|PubMed:21821878, ECO:0000305|PubMed:22325780}.
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000269|PubMed:21821878};
CC Note=Binds 1 calcium ion per spike trimer.;
CC -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC Evidence={ECO:0000269|PubMed:21821878, ECO:0000269|PubMed:22325780};
CC Note=Binds 1 Fe cation per spike trimer.;
CC -!- COFACTOR:
CC Name=chloride; Xref=ChEBI:CHEBI:17996;
CC Evidence={ECO:0000269|PubMed:21821878, ECO:0000269|PubMed:22325780};
CC Note=Binds 1 chloride per spike trimer.;
CC -!- SUBUNIT: homotrimer.
CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000269|PubMed:21821878}. Note=Part
CC of the virion tail. {ECO:0000269|PubMed:21821878}.
CC -!- INDUCTION: Expressed in the late phase of the viral replicative cycle.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the P2likevirus spike protein family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF063097; AAD03282.1; -; Genomic_DNA.
DR RefSeq; NP_046771.1; NC_001895.1.
DR PDB; 3AQJ; X-ray; 1.27 A; A/B/C/P/Q/R=87-211.
DR PDB; 3QR7; X-ray; 0.94 A; A/B=97-211.
DR PDB; 3QR8; X-ray; 2.03 A; A=1-211.
DR PDBsum; 3AQJ; -.
DR PDBsum; 3QR7; -.
DR PDBsum; 3QR8; -.
DR SMR; P31340; -.
DR GeneID; 1261526; -.
DR KEGG; vg:1261526; -.
DR Proteomes; UP000009092; Genome.
DR GO; GO:0098025; C:virus tail, baseplate; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0098670; P:entry receptor-mediated virion attachment to host cell; IEA:UniProtKB-KW.
DR GO; GO:0044694; P:pore-mediated entry of viral genome into host cell; IEA:UniProtKB-KW.
DR GO; GO:0098003; P:viral tail assembly; IEA:UniProtKB-KW.
DR Gene3D; 2.40.50.230; -; 1.
DR InterPro; IPR006531; Gp5/Vgr_OB.
DR InterPro; IPR013046; GpV/Gp45.
DR InterPro; IPR040629; Phage_spike.
DR InterPro; IPR037026; Vgr_OB-fold_dom_sf.
DR Pfam; PF04717; Phage_base_V; 1.
DR Pfam; PF18715; Phage_spike; 1.
DR TIGRFAMs; TIGR01644; phage_P2_V; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Host-virus interaction; Late protein; Metal-binding;
KW Pore-mediated penetration of viral genome into host cell;
KW Reference proteome; Viral attachment to host cell;
KW Viral attachment to host entry receptor; Viral baseplate protein;
KW Viral penetration into host cytoplasm; Viral release from host cell;
KW Viral tail assembly; Viral tail protein; Virion;
KW Virus entry into host cell.
FT CHAIN 1..211
FT /note="Spike protein"
FT /id="PRO_0000165263"
FT REGION 183..211
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 50
FT /ligand="chloride"
FT /ligand_id="ChEBI:CHEBI:17996"
FT /evidence="ECO:0007744|PDB:3QR8"
FT BINDING 197
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT BINDING 199
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT BINDING 202
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT BINDING 203
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT HELIX 10..17
FT /evidence="ECO:0007829|PDB:3QR8"
FT STRAND 18..27
FT /evidence="ECO:0007829|PDB:3QR8"
FT TURN 28..31
FT /evidence="ECO:0007829|PDB:3QR8"
FT STRAND 32..37
FT /evidence="ECO:0007829|PDB:3QR8"
FT STRAND 45..47
FT /evidence="ECO:0007829|PDB:3QR8"
FT STRAND 52..56
FT /evidence="ECO:0007829|PDB:3QR8"
FT STRAND 66..71
FT /evidence="ECO:0007829|PDB:3QR8"
FT TURN 74..76
FT /evidence="ECO:0007829|PDB:3QR8"
FT STRAND 79..85
FT /evidence="ECO:0007829|PDB:3QR8"
FT STRAND 88..90
FT /evidence="ECO:0007829|PDB:3QR8"
FT STRAND 100..103
FT /evidence="ECO:0007829|PDB:3QR7"
FT STRAND 109..113
FT /evidence="ECO:0007829|PDB:3QR7"
FT TURN 114..117
FT /evidence="ECO:0007829|PDB:3QR7"
FT STRAND 118..123
FT /evidence="ECO:0007829|PDB:3QR7"
FT STRAND 140..145
FT /evidence="ECO:0007829|PDB:3AQJ"
FT STRAND 147..172
FT /evidence="ECO:0007829|PDB:3AQJ"
FT STRAND 174..178
FT /evidence="ECO:0007829|PDB:3AQJ"
FT STRAND 180..185
FT /evidence="ECO:0007829|PDB:3AQJ"
FT STRAND 187..189
FT /evidence="ECO:0007829|PDB:3AQJ"
FT TURN 194..196
FT /evidence="ECO:0007829|PDB:3QR7"
FT STRAND 204..206
FT /evidence="ECO:0007829|PDB:3QR7"
SQ SEQUENCE 211 AA; 22244 MW; B1CA7E47B19B91FB CRC64;
MNTLANIQEL ARALRNMIRT GIIVETDLNA GRCRVQTGGM CTDWLQWLTH RAGRSRTWWA
PSVGEQVLIL AVGGELDTAF VLPGIYSGDN PSPSVSADAL HIRFPDGAVI EYEPETSALT
VSGIKTASVT ASGSVTATVP VVMVKASTRV TLDTPEVVCT NRLITGTLEV QKGGTMRGNI
EHTGGELSSN GKVLHTHKHP GDSGGTTGSP L
