BP11_BPT4
ID BP11_BPT4 Reviewed; 219 AA.
AC P10929;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 29-SEP-2021, entry version 112.
DE RecName: Full=Baseplate wedge protein gp11 {ECO:0000305};
DE AltName: Full=Gene product 11;
DE Short=gp11;
GN Name=11;
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=2726468; DOI=10.1093/nar/17.8.3303;
RA Prilipov A.G., Selivanov N.A., Efimov V.P., Marusich E.I.,
RA Mesyanzhinov V.V.;
RT "Nucleotide sequences of bacteriophage T4 genes 9, 10 and 11.";
RL Nucleic Acids Res. 17:3303-3303(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=D;
RX PubMed=2548819; DOI=10.1089/dna.1.1989.8.287;
RA Barrett B.K., Berget P.B.;
RT "Using transposon Tn5 insertions to sequence bacteriophage T4 gene 11.";
RL DNA 8:287-295(1989).
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 211-219.
RC STRAIN=D;
RX PubMed=3357780; DOI=10.1093/nar/16.5.2334;
RA Selivanov N.A., Prilipov A.G., Mesyanzhinov V.V.;
RT "Nucleotide and deduced amino acid sequence of bacteriophage T4 gene 12.";
RL Nucleic Acids Res. 16:2334-2334(1988).
RN [5]
RP PROTEIN SEQUENCE OF 2-10, 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.
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 X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 12-219, AND SUBUNIT.
RX PubMed=10966799; DOI=10.1006/jmbi.2000.3989;
RA Leiman P.G., Kostyuchenko V.A., Shneider M.M., Kurochkina L.P.,
RA Mesyanzhinov V.V., Rossmann M.G.;
RT "Structure of bacteriophage T4 gene product 11, the interface between the
RT baseplate and short tail fibers.";
RL J. Mol. Biol. 301:975-985(2000).
RN [12]
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 part of the baseplate wedge and
CC that connects the short tail fibers to the baseplate (PubMed:15315755).
CC Involved in the tail assembly. {ECO:0000269|PubMed:15315755,
CC ECO:0000269|PubMed:27193680, ECO:0000303|PubMed:21129200}.
CC -!- SUBUNIT: Homotrimer (PubMed:27193680, PubMed:19896486). The gp11 trimer
CC interacts with gp10 trimer and with the short tail fiber (STF) composed
CC of the gp12 trimer (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) (PubMed:27193680).
CC {ECO:0000269|PubMed:19896486, 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 18 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; X14192; CAA32397.1; -; Genomic_DNA.
DR EMBL; X06792; CAA29950.1; -; Genomic_DNA.
DR EMBL; AF158101; AAD42416.1; -; Genomic_DNA.
DR EMBL; M26253; AAA32494.1; -; Genomic_DNA.
DR PIR; S04084; GLBPT4.
DR RefSeq; NP_049769.1; NC_000866.4.
DR PDB; 1EL6; X-ray; 2.00 A; A/B/C=1-219.
DR PDB; 1PDF; EM; 12.00 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R=1-219.
DR PDB; 1TJA; EM; 16.00 A; F/G/H=1-219.
DR PDB; 5IV5; EM; 4.11 A; AF/AG/AH/CI/CJ/DA/FB/FC/FD/HE/HF/HG/L/M/N/i/j/k=1-219.
DR PDB; 5IV7; EM; 6.77 A; BA/BB/BC/DC/DD/DE/FE/FF/FG/L/M/N/b/c/d/r/s/t=1-219.
DR PDBsum; 1EL6; -.
DR PDBsum; 1PDF; -.
DR PDBsum; 1TJA; -.
DR PDBsum; 5IV5; -.
DR PDBsum; 5IV7; -.
DR SMR; P10929; -.
DR TCDB; 1.K.1.1.1; the gp27/5 t4-baseplate (t4-bp) family.
DR GeneID; 1258638; -.
DR KEGG; vg:1258638; -.
DR EvolutionaryTrace; P10929; -.
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.
DR Gene3D; 1.10.286.30; -; 1.
DR Gene3D; 2.20.20.20; -; 1.
DR Gene3D; 3.90.1160.10; -; 1.
DR InterPro; IPR014791; Baseplate_struct_Gp11.
DR InterPro; IPR043180; Baseplate_struct_Gp11_C.
DR InterPro; IPR015982; Baseplate_struct_Gp11_N_sf.
DR InterPro; IPR036214; Gp11_sf.
DR InterPro; IPR015976; Phage_T4_Gp11_C.
DR Pfam; PF08677; GP11; 1.
DR SUPFAM; SSF56558; SSF56558; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; 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..219
FT /note="Baseplate wedge protein gp11"
FT /id="PRO_0000165001"
FT HELIX 15..17
FT /evidence="ECO:0007829|PDB:1EL6"
FT TURN 30..32
FT /evidence="ECO:0007829|PDB:1EL6"
FT HELIX 40..43
FT /evidence="ECO:0007829|PDB:1EL6"
FT TURN 44..46
FT /evidence="ECO:0007829|PDB:1EL6"
FT HELIX 52..63
FT /evidence="ECO:0007829|PDB:1EL6"
FT STRAND 69..75
FT /evidence="ECO:0007829|PDB:1EL6"
FT STRAND 85..93
FT /evidence="ECO:0007829|PDB:1EL6"
FT STRAND 104..109
FT /evidence="ECO:0007829|PDB:1EL6"
FT STRAND 112..117
FT /evidence="ECO:0007829|PDB:1EL6"
FT HELIX 122..138
FT /evidence="ECO:0007829|PDB:1EL6"
FT STRAND 141..148
FT /evidence="ECO:0007829|PDB:1EL6"
FT STRAND 155..162
FT /evidence="ECO:0007829|PDB:1EL6"
FT STRAND 171..173
FT /evidence="ECO:0007829|PDB:1EL6"
FT STRAND 176..184
FT /evidence="ECO:0007829|PDB:1EL6"
FT STRAND 193..201
FT /evidence="ECO:0007829|PDB:1EL6"
FT STRAND 210..217
FT /evidence="ECO:0007829|PDB:1EL6"
SQ SEQUENCE 219 AA; 23707 MW; C33CDA772470A281 CRC64;
MSLLNNKAGV ISRLADFLGF RPKTGDIDVM NRQSVGSVTI SQLAKGFYEP NIESAINDVH
NFSIKDVGTI ITNKTGVSPE GVSQTDYWAF SGTVTDDSLP PGSPITVLVF GLPVSATTGM
TAIEFVAKVR VALQEAIASF TAINSYKDHP TDGSKLEVTY LDNQKHVLST YSTYGITISQ
EIISESKPGY GTWNLLGAQT VTLDNQQTPT VFYHFERTA