ID BP27_BPT4 Reviewed; 391 AA. AC P17172; Q9T0T8; DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot. DT 19-DEC-2001, sequence version 4. DT 24-JAN-2024, entry version 118. DE RecName: Full=Baseplate central spike complex protein gp27 {ECO:0000303|PubMed:27193680}; DE AltName: Full=Gene product 27; DE Short=gp27; DE AltName: Full=Hub protein 27; GN Name=27; 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]. RC STRAIN=D; RX PubMed=2349100; DOI=10.1093/nar/18.10.3046; RA Bova R., Cascino A., Cipollaro M., Grau O., Micheli M.R., Santoro M., RA Storlazzi A., Scarlato V., Gargano S.; RT "Bacteriophage T4 gene 27."; RL Nucleic Acids Res. 18:3046-3046(1990). RN [2] 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 [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-53. RC STRAIN=D; RX PubMed=2763463; DOI=10.1016/0042-6822(89)90617-x; RA Scarlato V., Storlazzi A., Gargano S., Cascino A.; RT "Bacteriophage T4 late gene expression: overlapping promoters direct RT divergent transcription of the base plate gene cluster."; RL Virology 171:475-483(1989). RN [4] RP PROTEIN SEQUENCE OF 2-8, 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 [5] RP SUBCELLULAR LOCATION. 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 [6] RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH GP5, AND SUBUNIT. RX PubMed=12837775; DOI=10.1128/jb.185.14.4022-4030.2003; RA Weigele P.R., Scanlon E., King J.; RT "Homotrimeric, beta-stranded viral adhesins and tail proteins."; RL J. Bacteriol. 185:4022-4030(2003). 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 X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS), AND SUBUNIT. RX PubMed=11823865; DOI=10.1038/415553a; RA Kanamaru S., Leiman P.G., Kostyuchenko V.A., Chipman P.R., RA Mesyanzhinov V.V., Arisaka F., Rossmann M.G.; RT "Structure of the cell-puncturing device of bacteriophage T4."; RL Nature 415:553-557(2002). RN [11] RP STRUCTURE BY ELECTRON MICROSCOPY (12.0 ANGSTROMS). RX PubMed=12923574; DOI=10.1038/nsb970; RA Kostyuchenko V.A., Leiman P.G., Chipman P.R., Kanamaru S., van Raaij M.J., RA Arisaka F., Mesyanzhinov V.V., Rossmann M.G.; RT "Three-dimensional structure of bacteriophage T4 baseplate."; RL Nat. Struct. Biol. 10:688-693(2003). RN [12] 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 [13] RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS). RX PubMed=15701513; DOI=10.1016/j.jmb.2004.12.042; RA Kanamaru S., Ishiwata Y., Suzuki T., Rossmann M.G., Arisaka F.; RT "Control of bacteriophage T4 tail lysozyme activity during the infection RT process."; RL J. Mol. Biol. 346:1013-1020(2005). RN [14] RP STRUCTURE BY ELECTRON MICROSCOPY (4.11 ANGSTROMS), SUBUNIT, SUBCELLULAR RP LOCATION, FUNCTION, INTERACTION WITH GP5, AND INTERACTION WITH GP5.4. 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 central spike complex-associated protein involved CC in the tail assembly. {ECO:0000269|PubMed:12837775, CC ECO:0000269|PubMed:27193680, ECO:0000303|PubMed:21129200}. CC -!- SUBUNIT: Homotrimer (PubMed:12837775, PubMed:19896486, CC PubMed:11823865). Heteromultimer with gp5 trimer and gp5.4 monomer; CC this interaction forms the tail lysozyme complex that creates an CC extension of the tail tube (PubMed:12837775, PubMed:27193680). The T4 CC tail lysozyme complex is made up of three copies of the proteolytically CC processed gp5 and three copies of gp27.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) (PubMed:27193680). CC {ECO:0000269|PubMed:11823865, ECO:0000269|PubMed:12837775, CC ECO:0000269|PubMed:19896486, ECO:0000269|PubMed:27193680, CC ECO:0000303|PubMed:21129200}. CC -!- INTERACTION: CC P17172; P16009: 5; NbExp=2; IntAct=EBI-1032762, EBI-1032754; CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000269|PubMed:12837775, CC ECO:0000269|PubMed:15342608, ECO:0000269|PubMed:2403438, CC ECO:0000269|PubMed:27193680}. Note=Present in 3 copies in the CC baseplate. {ECO:0000303|PubMed:21129200}. CC -!- INDUCTION: Expressed in the late phase of the viral replicative cycle. 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; X52236; CAA36481.1; -; Genomic_DNA. DR EMBL; AF158101; AAD42435.2; -; Genomic_DNA. DR EMBL; J04354; AAA88466.1; -; Genomic_DNA. DR PIR; JU0285; GZBPT4. DR RefSeq; NP_049803.1; NC_000866.4. DR PDB; 1K28; X-ray; 2.90 A; D=1-391. DR PDB; 1PDJ; EM; 12.00 A; D/E/F=1-391. DR PDB; 1WTH; X-ray; 2.80 A; D=1-391. DR PDB; 2Z6B; X-ray; 3.11 A; D=1-391. DR PDB; 5IV5; EM; 4.11 A; YD/YE/YF=1-391. DR PDBsum; 1K28; -. DR PDBsum; 1PDJ; -. DR PDBsum; 1WTH; -. DR PDBsum; 2Z6B; -. DR PDBsum; 5IV5; -. DR SMR; P17172; -. DR IntAct; P17172; 1. DR MINT; P17172; -. DR TCDB; 1.K.1.1.1; the gp27/5 t4-baseplate (t4-bp) family. DR GeneID; 1258643; -. DR KEGG; vg:1258643; -. DR OrthoDB; 2757at10239; -. DR EvolutionaryTrace; P17172; -. DR Proteomes; UP000009087; Segment. DR GO; GO:0098015; C:virus tail; IDA:CAFA. DR GO; GO:0098025; C:virus tail, baseplate; IDA:UniProtKB. DR GO; GO:0098003; P:viral tail assembly; IEA:UniProtKB-KW. DR Gene3D; 3.30.1920.40; -; 1. DR Gene3D; 3.55.50.20; -; 1. DR Gene3D; 2.40.30.150; Bacteriophage T4, Gp27, baseplate hub, domain 3; 1. DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 1. DR InterPro; IPR043085; Gp27_dom2. DR InterPro; IPR043083; Gp27_dom3. DR InterPro; IPR043084; Gp27_dom4. DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin. DR InterPro; IPR015180; Phage_T4_Gp27_C. DR InterPro; IPR015181; Phage_T4_Gp27_N. DR Pfam; PF09097; Phage-tail_1; 1. DR Pfam; PF09096; Phage-tail_2; 1. DR SUPFAM; SSF69279; Phage tail proteins; 2. PE 1: Evidence at protein level; KW 3D-structure; Direct protein sequencing; Late protein; Reference proteome; KW Viral baseplate protein; Viral release from host cell; Viral tail assembly; KW Viral tail protein; Virion. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|PubMed:15342608" FT CHAIN 2..391 FT /note="Baseplate central spike complex protein gp27" FT /id="PRO_0000165015" FT CONFLICT 168 FT /note="N -> T (in Ref. 1; CAA36481)" FT /evidence="ECO:0000305" FT CONFLICT 262 FT /note="S -> E (in Ref. 1)" FT /evidence="ECO:0000305" FT CONFLICT 308 FT /note="A -> L (in Ref. 1; CAA36481)" FT /evidence="ECO:0000305" FT STRAND 13..20 FT /evidence="ECO:0007829|PDB:1WTH" FT HELIX 21..24 FT /evidence="ECO:0007829|PDB:1WTH" FT STRAND 32..43 FT /evidence="ECO:0007829|PDB:1WTH" FT STRAND 48..54 FT /evidence="ECO:0007829|PDB:1WTH" FT HELIX 60..62 FT /evidence="ECO:0007829|PDB:1WTH" FT STRAND 69..74 FT /evidence="ECO:0007829|PDB:1WTH" FT STRAND 76..78 FT /evidence="ECO:0007829|PDB:1WTH" FT STRAND 84..93 FT /evidence="ECO:0007829|PDB:1WTH" FT STRAND 99..101 FT /evidence="ECO:0007829|PDB:2Z6B" FT STRAND 105..110 FT /evidence="ECO:0007829|PDB:1WTH" FT HELIX 112..115 FT /evidence="ECO:0007829|PDB:1WTH" FT HELIX 128..139 FT /evidence="ECO:0007829|PDB:1WTH" FT TURN 140..146 FT /evidence="ECO:0007829|PDB:1WTH" FT STRAND 149..151 FT /evidence="ECO:0007829|PDB:1K28" FT HELIX 166..176 FT /evidence="ECO:0007829|PDB:1WTH" FT TURN 180..183 FT /evidence="ECO:0007829|PDB:1WTH" FT STRAND 184..190 FT /evidence="ECO:0007829|PDB:1WTH" FT STRAND 195..199 FT /evidence="ECO:0007829|PDB:1WTH" FT HELIX 200..204 FT /evidence="ECO:0007829|PDB:1WTH" FT STRAND 209..213 FT /evidence="ECO:0007829|PDB:1WTH" FT STRAND 230..239 FT /evidence="ECO:0007829|PDB:1WTH" FT HELIX 242..244 FT /evidence="ECO:0007829|PDB:1WTH" FT HELIX 247..250 FT /evidence="ECO:0007829|PDB:1WTH" FT STRAND 251..256 FT /evidence="ECO:0007829|PDB:1WTH" FT STRAND 258..261 FT /evidence="ECO:0007829|PDB:1WTH" FT STRAND 265..268 FT /evidence="ECO:0007829|PDB:1WTH" FT STRAND 273..278 FT /evidence="ECO:0007829|PDB:1WTH" FT HELIX 281..285 FT /evidence="ECO:0007829|PDB:1WTH" FT STRAND 286..291 FT /evidence="ECO:0007829|PDB:1WTH" FT HELIX 292..301 FT /evidence="ECO:0007829|PDB:1WTH" FT STRAND 306..313 FT /evidence="ECO:0007829|PDB:1WTH" FT STRAND 323..327 FT /evidence="ECO:0007829|PDB:1WTH" FT STRAND 335..346 FT /evidence="ECO:0007829|PDB:1WTH" FT STRAND 351..359 FT /evidence="ECO:0007829|PDB:1WTH" SQ SEQUENCE 391 AA; 44389 MW; 0DABEFE1D890B1FA CRC64; MSMLQRPGYP NLSVKLFDSY DAWSNNRFVE LAATITTLTM RDSLYGRNEG MLQFYDSKNI HTKMDGNEII QISVANANDI NNVKTRIYGC KHFSVSVDSK GDNIIAIELG TIHSIENLKF GRPFFPDAGE SIKEMLGVIY QDRTLLTPAI NAINAYVPDI PWTSTFENYL SYVREVALAV GSDKFVFVWQ DIMGVNMMDY DMMINQEPYP MIVGEPSLIG QFIQELKYPL AYDFVWLTKS NPHKRDPMKN ATIYAHSFLD SSIPMITTGK GENSIVVSRS GAYSEMTYRN GYEEAIRLQT MAQYDGYAKC STIGNFNLTP GVKIIFNDSK NQFKTEFYVD EVIHELSNNN SVTHLYMFTN ATKLETIDPV KVKNEFKSDT TTEESSSSNK Q //