BP27_BPT4
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 23-FEB-2022, entry version 114.
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 Caudovirales; Myoviridae; 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}.
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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 EvolutionaryTrace; P17172; -.
DR Proteomes; UP000009087; Genome.
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; 2.40.10.10; -; 1.
DR Gene3D; 2.40.30.150; -; 1.
DR Gene3D; 3.30.1920.40; -; 1.
DR Gene3D; 3.55.50.20; -; 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.
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
