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 08-NOV-2023, entry version 113. 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 Straboviridae; 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}. 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; 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 OrthoDB; 13602at10239; -. DR Proteomes; UP000009087; Segment. DR GO; GO:0098025; C:virus tail, baseplate; IDA:UniProtKB. DR Gene3D; 3.10.450.40; -; 1. DR InterPro; IPR007048; IraD/Gp25-like. DR Pfam; PF04965; GPW_gp25; 1. DR SUPFAM; SSF160719; gpW/gp25-like; 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 //