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BP25_BPT4
ID   BP25_BPT4               Reviewed;         132 AA.
AC   P09425;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1989, sequence version 1.
DT   23-FEB-2022, entry version 110.
DE   RecName: Full=Baseplate wedge protein gp25 {ECO:0000305};
DE   AltName: Full=Outer wedge of baseplate protein;
DE   AltName: Full=Protein Gp25;
GN   Name=25;
OS   Enterobacteria phage T4 (Bacteriophage T4).
OC   Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC   Caudovirales; Myoviridae; Tevenvirinae; Tequatrovirus.
OX   NCBI_TaxID=10665;
OH   NCBI_TaxID=562; Escherichia coli.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION.
RC   STRAIN=D;
RX   PubMed=3186452; DOI=10.1093/nar/16.20.9862;
RA   Gruidl M.E., Canan N., Mosig G.;
RT   "Bacteriophage T4 gene 25.";
RL   Nucleic Acids Res. 16:9862-9862(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1871975; DOI=10.1016/0042-6822(91)90852-3;
RA   Gruidl M.E., Chen T.C., Gargano S., Storlazzi A., Cascino A., Mosig G.;
RT   "Two bacteriophage T4 base plate genes (25 and 26) and the DNA repair gene
RT   uvsY belong to spatially and temporally overlapping transcription units.";
RL   Virology 184:359-369(1991).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=12626685; DOI=10.1128/mmbr.67.1.86-156.2003;
RA   Miller E.S., Kutter E., Mosig G., Arisaka F., Kunisawa T., Ruger W.;
RT   "Bacteriophage T4 genome.";
RL   Microbiol. Mol. Biol. Rev. 67:86-156(2003).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 6-132.
RX   PubMed=3026891; DOI=10.1093/genetics/114.4.1061;
RA   Gruidl M.E., Mosig G.;
RT   "Sequence and transcripts of the bacteriophage T4 DNA repair gene uvsY.";
RL   Genetics 114:1061-1079(1986).
RN   [5]
RP   PROTEIN SEQUENCE OF 2-11, AND SUBCELLULAR LOCATION.
RX   PubMed=15342608; DOI=10.1128/jb.186.18.6335-6339.2004;
RA   Ye N., Nemoto N.;
RT   "Processing of the tail lysozyme (gp5) of bacteriophage T4.";
RL   J. Bacteriol. 186:6335-6339(2004).
RN   [6]
RP   SUBCELLULAR LOCATION, AND SUBUNIT.
RX   PubMed=2403438; DOI=10.1128/jvi.64.1.143-154.1990;
RA   Watts N.R., Coombs D.H.;
RT   "Structure of the bacteriophage T4 baseplate as determined by chemical
RT   cross-linking.";
RL   J. Virol. 64:143-154(1990).
RN   [7]
RP   REVIEW.
RX   PubMed=14625682; DOI=10.1007/s00018-003-3072-1;
RA   Leiman P.G., Kanamaru S., Mesyanzhinov V.V., Arisaka F., Rossmann M.G.;
RT   "Structure and morphogenesis of bacteriophage T4.";
RL   Cell. Mol. Life Sci. 60:2356-2370(2003).
RN   [8]
RP   REVIEW ON FUNCTION.
RX   PubMed=21129200; DOI=10.1186/1743-422x-7-355;
RA   Leiman P.G., Arisaka F., van Raaij M.J., Kostyuchenko V.A., Aksyuk A.A.,
RA   Kanamaru S., Rossmann M.G.;
RT   "Morphogenesis of the T4 tail and tail fibers.";
RL   Virol. J. 7:355-355(2010).
RN   [9]
RP   SUBUNIT.
RX   PubMed=19896486; DOI=10.1016/j.jmb.2009.10.071;
RA   Yap M.L., Mio K., Leiman P.G., Kanamaru S., Arisaka F.;
RT   "The baseplate wedges of bacteriophage T4 spontaneously assemble into
RT   hubless baseplate-like structure in vitro.";
RL   J. Mol. Biol. 395:349-360(2010).
RN   [10]
RP   STRUCTURE BY ELECTRON MICROSCOPY (17.0 ANGSTROMS) OF THE CONTRACTED TAIL,
RP   SUBCELLULAR LOCATION, AND FUNCTION.
RX   PubMed=15315755; DOI=10.1016/j.cell.2004.07.022;
RA   Leiman P.G., Chipman P.R., Kostyuchenko V.A., Mesyanzhinov V.V.,
RA   Rossmann M.G.;
RT   "Three-dimensional rearrangement of proteins in the tail of bacteriophage
RT   T4 on infection of its host.";
RL   Cell 118:419-429(2004).
RN   [11]
RP   STRUCTURE BY ELECTRON MICROSCOPY (4.11 ANGSTROMS), SUBUNIT, SUBCELLULAR
RP   LOCATION, AND FUNCTION.
RX   PubMed=27193680; DOI=10.1038/nature17971;
RA   Taylor N.M., Prokhorov N.S., Guerrero-Ferreira R.C., Shneider M.M.,
RA   Browning C., Goldie K.N., Stahlberg H., Leiman P.G.;
RT   "Structure of the T4 baseplate and its function in triggering sheath
RT   contraction.";
RL   Nature 533:346-352(2016).
CC   -!- FUNCTION: Baseplate protein that is located next to the tail tube
CC       (inner baseplate). Involved in sheath assembly. The gp25-(gp6)2-gp7
CC       module is involved in sheath contraction (PubMed:27193680).
CC       {ECO:0000269|PubMed:15315755, ECO:0000269|PubMed:27193680}.
CC   -!- SUBUNIT: Homodimer. Interacts with gp53 and with the (gp6)2-gp7
CC       heterotrimeric molecule; The gp25-(gp6)2-gp7 module is involved in
CC       sheath contraction (PubMed:27193680). Part of the baseplate
CC       macromolecular complex which consists of gp5, gp5.4, gp27 (central
CC       spike complex); gp6, gp25, gp53 (inner baseplate); gp7, gp8
CC       (intermediate baseplate); gp9, gp10, gp11, gp12 (peripheral); gp48 and
CC       gp54 (proximal region of the tail tube). {ECO:0000269|PubMed:19896486,
CC       ECO:0000269|PubMed:2403438, ECO:0000269|PubMed:27193680}.
CC   -!- SUBCELLULAR LOCATION: Virion {ECO:0000269|PubMed:15315755,
CC       ECO:0000269|PubMed:15342608, ECO:0000269|PubMed:2403438,
CC       ECO:0000269|PubMed:27193680}. Note=Present in 6 copies in the
CC       baseplate. {ECO:0000303|PubMed:21129200}.
CC   -!- INDUCTION: Expressed in the late phase of the viral replicative cycle.
CC       {ECO:0000269|PubMed:3186452}.
CC   -!- SIMILARITY: Belongs to the GpW/Gp25 family. {ECO:0000305}.
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DR   EMBL; X05134; CAA28777.1; -; Genomic_DNA.
DR   EMBL; M77695; AAA32549.1; -; Genomic_DNA.
DR   EMBL; AF158101; AAD42433.1; -; Genomic_DNA.
DR   EMBL; X04856; CAA28547.1; -; Genomic_DNA.
DR   PIR; JF0054; GYBPT4.
DR   RefSeq; NP_049800.1; NC_000866.4.
DR   PDB; 5IV5; EM; 4.11 A; BD/DG/FJ/IC/T/q=1-132.
DR   PDB; 5IV7; EM; 6.77 A; BD/DF/GA/O/e/u=1-132.
DR   PDB; 5IW9; X-ray; 2.47 A; A/B=2-132.
DR   PDBsum; 5IV5; -.
DR   PDBsum; 5IV7; -.
DR   PDBsum; 5IW9; -.
DR   SMR; P09425; -.
DR   TCDB; 1.K.1.1.1; the gp27/5 t4-baseplate (t4-bp) family.
DR   GeneID; 1258633; -.
DR   KEGG; vg:1258633; -.
DR   Proteomes; UP000009087; Genome.
DR   GO; GO:0098025; C:virus tail, baseplate; IDA:UniProtKB.
DR   InterPro; IPR007048; IraD/Gp25-like.
DR   Pfam; PF04965; GPW_gp25; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Direct protein sequencing; Late protein; Reference proteome;
KW   Viral baseplate protein; Viral tail protein; Virion.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:15342608"
FT   CHAIN           2..132
FT                   /note="Baseplate wedge protein gp25"
FT                   /id="PRO_0000165013"
FT   HELIX           21..41
FT                   /evidence="ECO:0007829|PDB:5IW9"
FT   HELIX           59..63
FT                   /evidence="ECO:0007829|PDB:5IW9"
FT   HELIX           69..84
FT                   /evidence="ECO:0007829|PDB:5IW9"
FT   STRAND          88..98
FT                   /evidence="ECO:0007829|PDB:5IW9"
FT   TURN            99..102
FT                   /evidence="ECO:0007829|PDB:5IW9"
FT   STRAND          103..114
FT                   /evidence="ECO:0007829|PDB:5IW9"
FT   STRAND          120..126
FT                   /evidence="ECO:0007829|PDB:5IW9"
SQ   SEQUENCE   132 AA;  15095 MW;  16C2803EE5B12B0B CRC64;
     MANINKLYSD IDPEMKMDWN KDVSRSLGLR SIKNSLLGII TTRKGSRPFD PEFGCDLSDQ
     LFENMTPLTA DTVERNIESA VRNYEPRIDK LAVNVIPVYD DYTLIVEIRF SVIDNPDDIE
     QIKLQLASSN RV
 
 
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