BP54_BPT4
ID BP54_BPT4 Reviewed; 320 AA.
AC P13341;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1990, sequence version 1.
DT 23-FEB-2022, entry version 80.
DE RecName: Full=Baseplate tail-tube junction protein gp54 {ECO:0000305};
DE AltName: Full=Gene product 54;
DE Short=gp54;
GN Name=54;
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 FUNCTION.
RX PubMed=3363870; DOI=10.1016/0042-6822(88)90622-8;
RA Ishimoto L.K., Ishimoto K.S., Cascino A., Cipollaro M., Eiserling F.A.;
RT "The structure of three bacteriophage T4 genes required for tail-tube
RT assembly.";
RL Virology 164:81-90(1988).
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 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 [4]
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 [5]
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 [6]
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 [7]
RP STRUCTURE BY ELECTRON MICROSCOPY (17.0 ANGSTROMS) OF THE CONTRACTED TAIL,
RP AND SUBCELLULAR LOCATION.
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 [8]
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 forms, together with gp48, the
CC baseplate-tail tube junction. The tail tube first 2 annuli are formed
CC by gp48 and gp54, which are in continuation of the spike complex.
CC Involved in the tail assembly. Morphogenesis of the baseplate is
CC completed by association of gp48 and gp54, which bind the upper part of
CC the baseplate dome to form the platform for polymerization of the tail
CC tube. {ECO:0000269|PubMed:27193680, ECO:0000269|PubMed:3363870,
CC ECO:0000303|PubMed:21129200}.
CC -!- SUBUNIT: Homohexamer (PubMed:27193680). The tube second annulus is
CC composed of a gp54 hexameric ring. Interacts with the tail tube protein
CC gp19. Interacts with the first layer of sheath proteins gp18. Part of
CC the baseplate macromolecular complex which consists of gp5, gp5.4, gp27
CC (central 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:2403438, ECO:0000269|PubMed:27193680}. Note=Present
CC in 6 copies in the 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; M20298; AAA32540.1; -; Genomic_DNA.
DR EMBL; AF158101; AAD42490.1; -; Genomic_DNA.
DR PIR; JF0037; GDBPT4.
DR RefSeq; NP_049807.1; NC_000866.4.
DR PDB; 5IV5; EM; 4.11 A; BG/DJ/GC/IF/W/t=1-320.
DR PDBsum; 5IV5; -.
DR SMR; P13341; -.
DR TCDB; 1.K.1.1.1; the gp27/5 t4-baseplate (t4-bp) family.
DR GeneID; 1258631; -.
DR KEGG; vg:1258631; -.
DR Proteomes; UP000009087; Genome.
DR GO; GO:0098025; C:virus tail, baseplate; IDA:UniProtKB.
DR GO; GO:0098003; P:viral tail assembly; IEA:UniProtKB-KW.
PE 1: Evidence at protein level;
KW 3D-structure; Late protein; Reference proteome; Viral baseplate protein;
KW Viral release from host cell; Viral tail assembly; Viral tail protein;
KW Virion.
FT CHAIN 1..320
FT /note="Baseplate tail-tube junction protein gp54"
FT /id="PRO_0000165043"
SQ SEQUENCE 320 AA; 34977 MW; EFA4A925223D9CBD CRC64;
MYSLEEFNNQ AINADFQRNN MFSCVFATTP STKSSSLISS ISNFSYNNLG LNSDWLGLTQ
GDINQGITTL ITAGTQKLIR KSGVSKYLIG AMSQRTVQSL LGSFTVGTYL IDFFNMAYNS
SGLMIYSVKM PENRLSYETD WNYNSPNIRI TGRELDPLVI SFRMDSEACN YRAMQDWVNS
VQDPVTGLRA LPQDVEADIQ VNLHSRNGLP HTAVMFTMHS ISVSAPELSY DGDNQITTFD
VTFAYRVMQA GAVDRQRALE WLESAAINGI QSVLGNSGGV TGLSNSLSRL SRLGGTAGSI
SNINTMTGIV NSQSKILGAI
