BP06_BPT4
ID BP06_BPT4 Reviewed; 660 AA.
AC P19060;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1990, sequence version 1.
DT 29-SEP-2021, entry version 88.
DE RecName: Full=Baseplate wedge protein gp6 {ECO:0000255|HAMAP-Rule:MF_04102, ECO:0000305};
DE AltName: Full=Gene product 6;
DE Short=gp6;
GN Name=6;
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=2402473; DOI=10.1093/nar/18.17.5313;
RA Efimov V.P., Prilipov A.G., Mesyanzhinov V.V.;
RT "Nucleotide sequences of bacteriophage T4 genes 6, 7 and 8.";
RL Nucleic Acids Res. 18:5313-5313(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 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 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 [8] {ECO:0007744|PDB:3H2T, ECO:0007744|PDB:3H3W, ECO:0007744|PDB:3H3Y}
RP X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF 334-660.
RX PubMed=19523898; DOI=10.1016/j.str.2009.04.005;
RA Aksyuk A.A., Leiman P.G., Shneider M.M., Mesyanzhinov V.V., Rossmann M.G.;
RT "The structure of gene product 6 of bacteriophage T4, the hinge-pin of the
RT baseplate.";
RL Structure 17:800-808(2009).
RN [9] {ECO:0007744|PDB:5IV5, ECO:0007744|PDB:5IV7}
RP STRUCTURE BY ELECTRON MICROSCOPY (4.11 ANGSTROMS), SUBUNIT, SUBCELLULAR
RP LOCATION, FUNCTION, AND INTERACTION WITH GP7.
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) (PubMed:27193680). Involved in the tail assembly
CC (PubMed:21129200). The gp25-(gp6)2-gp7 module is involved in sheath
CC contraction (PubMed:27193680). {ECO:0000269|PubMed:15315755,
CC ECO:0000269|PubMed:27193680, ECO:0000303|PubMed:21129200}.
CC -!- SUBUNIT: Homodimer (PubMed:2403438, PubMed:19896486, PubMed:27193680);
CC each gp6 molecule in the ring interacts with its two neighbors, forming
CC an N-terminal dimer with one and a C-terminal dimer with the other
CC (PubMed:27193680). Heterotrimer with gp7; gp6 is part of a (gp6)2-gp7
CC heterotrimeric molecule (PubMed:27193680). The (gp6)2-gp7
CC heterotrimeric molecule further interacts with gp25 and gp53; the gp25-
CC (gp6)2-gp7 module is involved in sheath contraction (PubMed:27193680).
CC Part of the baseplate macromolecular complex which consists of gp5,
CC gp5.4, gp27 (central spike complex); gp6, gp25, gp53 (inner baseplate);
CC gp7, gp8 (intermediate baseplate); gp9, gp10, gp11, gp12 (peripheral);
CC gp48 and gp54 (proximal region of the tail tube) (PubMed:27193680).
CC {ECO:0000269|PubMed:19896486, ECO:0000269|PubMed:2403438,
CC ECO:0000269|PubMed:27193680}.
CC -!- INTERACTION:
CC P19060; P19060: 6; NbExp=3; IntAct=EBI-15787824, EBI-15787824;
CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000255|HAMAP-Rule:MF_04102,
CC ECO:0000269|PubMed:15315755, ECO:0000269|PubMed:2403438,
CC ECO:0000269|PubMed:27193680}. Note=12 copies of gp6 form a continuous
CC ring that makes up most of the inner baseplate. {ECO:0000255|HAMAP-
CC Rule:MF_04102, ECO:0000269|PubMed:27193680}.
CC -!- INDUCTION: Expressed in the late phase of the viral replicative cycle.
CC {ECO:0000255|HAMAP-Rule:MF_04102}.
CC -!- SIMILARITY: Belongs to the T4likevirus baseplate wedge protein gp6
CC family. {ECO:0000255|HAMAP-Rule:MF_04102}.
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DR EMBL; X15907; CAA34021.1; -; Genomic_DNA.
DR EMBL; AF158101; AAD42505.1; -; Genomic_DNA.
DR PIR; JQ0656; G6BPT4.
DR RefSeq; NP_049764.1; NC_000866.4.
DR PDB; 3H2T; X-ray; 3.20 A; A/B=334-660.
DR PDB; 3H3W; EM; 12.00 A; A/B/C/D/E/F/G/H/I/J/K/L=334-660.
DR PDB; 3H3Y; EM; 16.00 A; A/B/C/D/E/F/G/H/I/J/K/L=334-660.
DR PDB; 5HX2; EM; 3.80 A; D/E=1-660.
DR PDB; 5IV5; EM; 4.11 A; A/B/BH/BI/EA/EB/GD/GE/X/Y/u/v=1-660.
DR PDB; 5IV7; EM; 6.77 A; A/B/BF/BG/EA/EB/Q/R/g/h/w/x=1-660.
DR PDBsum; 3H2T; -.
DR PDBsum; 3H3W; -.
DR PDBsum; 3H3Y; -.
DR PDBsum; 5HX2; -.
DR PDBsum; 5IV5; -.
DR PDBsum; 5IV7; -.
DR SMR; P19060; -.
DR DIP; DIP-48306N; -.
DR TCDB; 1.K.1.1.1; the gp27/5 t4-baseplate (t4-bp) family.
DR GeneID; 1258662; -.
DR KEGG; vg:1258662; -.
DR EvolutionaryTrace; P19060; -.
DR Proteomes; UP000009087; Genome.
DR GO; GO:0098025; C:virus tail, baseplate; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0098003; P:viral tail assembly; IEA:UniProtKB-KW.
DR HAMAP; MF_04102; BP06_T4; 1.
DR InterPro; IPR034698; GP6_T4.
PE 1: Evidence at protein level;
KW 3D-structure; Reference proteome; Viral baseplate protein;
KW Viral release from host cell; Viral tail assembly; Viral tail protein;
KW Virion.
FT CHAIN 1..660
FT /note="Baseplate wedge protein gp6"
FT /id="PRO_0000164996"
FT HELIX 342..352
FT /evidence="ECO:0007829|PDB:3H2T"
FT TURN 353..355
FT /evidence="ECO:0007829|PDB:3H2T"
FT STRAND 359..364
FT /evidence="ECO:0007829|PDB:3H2T"
FT STRAND 371..377
FT /evidence="ECO:0007829|PDB:3H2T"
FT STRAND 379..382
FT /evidence="ECO:0007829|PDB:3H2T"
FT TURN 384..388
FT /evidence="ECO:0007829|PDB:3H2T"
FT STRAND 389..391
FT /evidence="ECO:0007829|PDB:3H2T"
FT HELIX 393..396
FT /evidence="ECO:0007829|PDB:3H2T"
FT STRAND 403..409
FT /evidence="ECO:0007829|PDB:3H2T"
FT STRAND 412..425
FT /evidence="ECO:0007829|PDB:3H2T"
FT TURN 426..428
FT /evidence="ECO:0007829|PDB:3H2T"
FT HELIX 433..451
FT /evidence="ECO:0007829|PDB:3H2T"
FT HELIX 461..469
FT /evidence="ECO:0007829|PDB:3H2T"
FT STRAND 477..479
FT /evidence="ECO:0007829|PDB:3H2T"
FT STRAND 482..489
FT /evidence="ECO:0007829|PDB:3H2T"
FT STRAND 515..518
FT /evidence="ECO:0007829|PDB:3H2T"
FT STRAND 535..542
FT /evidence="ECO:0007829|PDB:3H2T"
FT STRAND 549..556
FT /evidence="ECO:0007829|PDB:3H2T"
FT TURN 560..562
FT /evidence="ECO:0007829|PDB:3H2T"
FT STRAND 590..596
FT /evidence="ECO:0007829|PDB:3H2T"
FT TURN 597..600
FT /evidence="ECO:0007829|PDB:3H2T"
FT STRAND 601..605
FT /evidence="ECO:0007829|PDB:3H2T"
FT HELIX 606..608
FT /evidence="ECO:0007829|PDB:3H2T"
FT HELIX 613..615
FT /evidence="ECO:0007829|PDB:3H2T"
FT STRAND 621..625
FT /evidence="ECO:0007829|PDB:3H2T"
FT STRAND 630..633
FT /evidence="ECO:0007829|PDB:3H2T"
FT STRAND 636..640
FT /evidence="ECO:0007829|PDB:3H2T"
FT TURN 644..646
FT /evidence="ECO:0007829|PDB:3H2T"
FT STRAND 650..653
FT /evidence="ECO:0007829|PDB:3H2T"
SQ SEQUENCE 660 AA; 74429 MW; DD233D4F26A7C1BF CRC64;
MANTPVNYQL TRTANAIPEI FVGGTFAEIK QNLIEWLNGQ NEFLDYDFEG SRLNVLCDLL
AYNTLYIQQF GNAAVYESFM RTANLRSSVV QAAQDNGYLP TSKSAAQTEI MLTCTDALNR
NYITIPRGTR FLAYAKDTSV NPYNFVSRED VIAIRDKNNQ YFPRLKLAQG RIVRTEIIYD
KLTPIIIYDK NIDRNQVKLY VDGAEWINWT RKSMVHAGST STIYYMRETI DGNTEFYFGE
GEISVNASEG ALTANYIGGL KPTQNSTIVI EYISTNGADA NGAVGFSYAD TLTNITVINI
NENPNDDPDF VGADGGGDPE DIERIRELGT IKRETQQRCV TATDYDTFVS ERFGSIIQAV
QTFTDSTKPG YAFIAAKPKS GLYLTTVQRE DIKNYLKDYN LAPITPSIIS PNYLFIKTNL
KVTYALNKLQ ESEQWLEGQI IDKIDRYYTE DVEIFNSSFA KSKMLTYVDD ADHSVIGSSA
TIQMVREVQN FYKTPEAGIK YNNQIKDRSM ESNTFSFNSG RKVVNPDTGL EEDVLYDVRI
VSTDRDSKGI GKVIIGPFAS GDVTENENIQ PYTGNDFNKL ANSDGRDKYY VIGEINYPAD
VIYWNIAKIN LTSEKFEVQT IELYSDPTDD VIFTRDGSLI VFENDLRPQY LTIDLEPISQ
