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Baseplate wedge protein gp6 (Gene product 6) (gp6)

 BP06_BPT4               Reviewed;         660 AA.
P19060;
01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
01-NOV-1990, sequence version 1.
22-NOV-2017, entry version 75.
RecName: Full=Baseplate wedge protein gp6 {ECO:0000255|HAMAP-Rule:MF_04102, ECO:0000305};
AltName: Full=Gene product 6;
Short=gp6;
Name=6;
Enterobacteria phage T4 (Bacteriophage T4).
Viruses; dsDNA viruses, no RNA stage; Caudovirales; Myoviridae;
Tevenvirinae; T4virus.
NCBI_TaxID=10665;
NCBI_TaxID=562; Escherichia coli.
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=D;
PubMed=2402473; DOI=10.1093/nar/18.17.5313;
Efimov V.P., Prilipov A.G., Mesyanzhinov V.V.;
"Nucleotide sequences of bacteriophage T4 genes 6, 7 and 8.";
Nucleic Acids Res. 18:5313-5313(1990).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=12626685; DOI=10.1128/MMBR.67.1.86-156.2003;
Miller E.S., Kutter E., Mosig G., Arisaka F., Kunisawa T., Ruger W.;
"Bacteriophage T4 genome.";
Microbiol. Mol. Biol. Rev. 67:86-156(2003).
[3]
SUBCELLULAR LOCATION, AND SUBUNIT.
PubMed=2403438;
Watts N.R., Coombs D.H.;
"Structure of the bacteriophage T4 baseplate as determined by chemical
cross-linking.";
J. Virol. 64:143-154(1990).
[4]
REVIEW.
PubMed=14625682; DOI=10.1007/s00018-003-3072-1;
Leiman P.G., Kanamaru S., Mesyanzhinov V.V., Arisaka F.,
Rossmann M.G.;
"Structure and morphogenesis of bacteriophage T4.";
Cell. Mol. Life Sci. 60:2356-2370(2003).
[5]
REVIEW ON FUNCTION.
PubMed=21129200; DOI=10.1186/1743-422X-7-355;
Leiman P.G., Arisaka F., van Raaij M.J., Kostyuchenko V.A.,
Aksyuk A.A., Kanamaru S., Rossmann M.G.;
"Morphogenesis of the T4 tail and tail fibers.";
Virol. J. 7:355-355(2010).
[6]
SUBUNIT.
PubMed=19896486; DOI=10.1016/j.jmb.2009.10.071;
Yap M.L., Mio K., Leiman P.G., Kanamaru S., Arisaka F.;
"The baseplate wedges of bacteriophage T4 spontaneously assemble into
hubless baseplate-like structure in vitro.";
J. Mol. Biol. 395:349-360(2010).
[7]
STRUCTURE BY ELECTRON MICROSCOPY (17.0 ANGSTROMS) OF THE CONTRACTED
TAIL, SUBCELLULAR LOCATION, AND FUNCTION.
PubMed=15315755; DOI=10.1016/j.cell.2004.07.022;
Leiman P.G., Chipman P.R., Kostyuchenko V.A., Mesyanzhinov V.V.,
Rossmann M.G.;
"Three-dimensional rearrangement of proteins in the tail of
bacteriophage T4 on infection of its host.";
Cell 118:419-429(2004).
[8] {ECO:0000244|PDB:3H2T, ECO:0000244|PDB:3H3W, ECO:0000244|PDB:3H3Y}
X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF 334-660.
PubMed=19523898; DOI=10.1016/j.str.2009.04.005;
Aksyuk A.A., Leiman P.G., Shneider M.M., Mesyanzhinov V.V.,
Rossmann M.G.;
"The structure of gene product 6 of bacteriophage T4, the hinge-pin of
the baseplate.";
Structure 17:800-808(2009).
[9] {ECO:0000244|PDB:5IV5, ECO:0000244|PDB:5IV7}
STRUCTURE BY ELECTRON MICROSCOPY (4.11 ANGSTROMS), SUBUNIT,
SUBCELLULAR LOCATION, FUNCTION, AND INTERACTION WITH GP7.
PubMed=27193680; DOI=10.1038/nature17971;
Taylor N.M., Prokhorov N.S., Guerrero-Ferreira R.C., Shneider M.M.,
Browning C., Goldie K.N., Stahlberg H., Leiman P.G.;
"Structure of the T4 baseplate and its function in triggering sheath
contraction.";
Nature 533:346-352(2016).
-!- FUNCTION: Baseplate protein that is located next to the tail tube
(inner baseplate) (PubMed:27193680). Involved in the tail assembly
(PubMed:21129200). The gp25-(gp6)2-gp7 module is involved in
sheath contraction (PubMed:27193680).
{ECO:0000269|PubMed:15315755, ECO:0000269|PubMed:27193680,
ECO:0000303|PubMed:21129200}.
-!- SUBUNIT: Homodimer (PubMed:2403438, PubMed:19896486,
PubMed:27193680); each gp6 molecule in the ring interacts with its
two neighbors, forming an N-terminal dimer with one and a C-
terminal dimer with the other (PubMed:27193680). Heterotrimer with
gp7; gp6 is part of a (gp6)2-gp7 heterotrimeric molecule
(PubMed:27193680). The (gp6)2-gp7 heterotrimeric molecule further
interacts with gp25 and gp53; the gp25-(gp6)2-gp7 module is
involved in sheath contraction (PubMed:27193680). Part of the
baseplate macromolecular complex which consists of gp5, gp5.4,
gp27 (central spike complex); gp6, gp25, gp53 (inner baseplate);
gp7, gp8 (intermediate baseplate); gp9, gp10, gp11, gp12
(peripheral); gp48 and gp54 (proximal region of the tail tube)
(PubMed:27193680). {ECO:0000269|PubMed:19896486,
ECO:0000269|PubMed:2403438, ECO:0000269|PubMed:27193680}.
-!- INTERACTION:
Self; NbExp=3; IntAct=EBI-15787824, EBI-15787824;
-!- SUBCELLULAR LOCATION: Virion {ECO:0000255|HAMAP-Rule:MF_04102,
ECO:0000269|PubMed:15315755, ECO:0000269|PubMed:2403438,
ECO:0000269|PubMed:27193680}. Note=12 copies of gp6 form a
continuous ring that makes up most of the inner baseplate.
{ECO:0000255|HAMAP-Rule:MF_04102, ECO:0000269|PubMed:27193680}.
-!- INDUCTION: Expressed in the late phase of the viral replicative
cycle. {ECO:0000255|HAMAP-Rule:MF_04102}.
-!- SIMILARITY: Belongs to the T4likevirus baseplate wedge protein gp6
family. {ECO:0000255|HAMAP-Rule:MF_04102}.
-----------------------------------------------------------------------
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EMBL; X15907; CAA34021.1; -; Genomic_DNA.
EMBL; AF158101; AAD42505.1; -; Genomic_DNA.
PIR; JQ0656; G6BPT4.
RefSeq; NP_049764.1; NC_000866.4.
PDB; 3H2T; X-ray; 3.20 A; A/B=334-660.
PDB; 3H3W; EM; 12.00 A; A/B/C/D/E/F/G/H/I/J/K/L=334-660.
PDB; 3H3Y; EM; 16.00 A; A/B/C/D/E/F/G/H/I/J/K/L=334-660.
PDB; 5HX2; EM; 3.80 A; D/E=1-660.
PDB; 5IV5; EM; 4.11 A; A/B/BH/BI/EA/EB/GD/GE/X/Y/u/v=1-660.
PDB; 5IV7; EM; 6.77 A; A/B/BF/BG/EA/EB/Q/R/g/h/w/x=1-660.
PDBsum; 3H2T; -.
PDBsum; 3H3W; -.
PDBsum; 3H3Y; -.
PDBsum; 5HX2; -.
PDBsum; 5IV5; -.
PDBsum; 5IV7; -.
SMR; P19060; -.
DIP; DIP-48306N; -.
TCDB; 1.K.1.1.1; the gp27/5 t4-baseplate (t4-bp) family.
GeneID; 1258662; -.
KEGG; vg:1258662; -.
OrthoDB; VOG090000P6; -.
EvolutionaryTrace; P19060; -.
Proteomes; UP000009087; Genome.
GO; GO:0019012; C:virion; IDA:CACAO.
GO; GO:0098025; C:virus tail, baseplate; IDA:UniProtKB.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0098003; P:viral tail assembly; IEA:UniProtKB-KW.
HAMAP; MF_04102; BP06_T4; 1.
InterPro; IPR034698; GP6_T4.
1: Evidence at protein level;
3D-structure; Complete proteome; Reference proteome;
Viral baseplate protein; Viral release from host cell;
Viral tail assembly; Viral tail protein; Virion.
CHAIN 1 660 Baseplate wedge protein gp6.
/FTId=PRO_0000164996.
HELIX 342 352 {ECO:0000244|PDB:3H2T}.
TURN 353 355 {ECO:0000244|PDB:3H2T}.
STRAND 359 364 {ECO:0000244|PDB:3H2T}.
STRAND 371 377 {ECO:0000244|PDB:3H2T}.
STRAND 379 382 {ECO:0000244|PDB:3H2T}.
TURN 384 388 {ECO:0000244|PDB:3H2T}.
STRAND 389 391 {ECO:0000244|PDB:3H2T}.
HELIX 393 396 {ECO:0000244|PDB:3H2T}.
STRAND 403 409 {ECO:0000244|PDB:3H2T}.
STRAND 412 425 {ECO:0000244|PDB:3H2T}.
TURN 426 428 {ECO:0000244|PDB:3H2T}.
HELIX 433 451 {ECO:0000244|PDB:3H2T}.
HELIX 461 469 {ECO:0000244|PDB:3H2T}.
STRAND 477 479 {ECO:0000244|PDB:3H2T}.
STRAND 482 489 {ECO:0000244|PDB:3H2T}.
STRAND 515 518 {ECO:0000244|PDB:3H2T}.
STRAND 535 542 {ECO:0000244|PDB:3H2T}.
STRAND 549 556 {ECO:0000244|PDB:3H2T}.
TURN 560 562 {ECO:0000244|PDB:3H2T}.
STRAND 590 596 {ECO:0000244|PDB:3H2T}.
TURN 597 600 {ECO:0000244|PDB:3H2T}.
STRAND 601 605 {ECO:0000244|PDB:3H2T}.
HELIX 606 608 {ECO:0000244|PDB:3H2T}.
HELIX 613 615 {ECO:0000244|PDB:3H2T}.
STRAND 621 625 {ECO:0000244|PDB:3H2T}.
STRAND 630 633 {ECO:0000244|PDB:3H2T}.
STRAND 636 640 {ECO:0000244|PDB:3H2T}.
TURN 644 646 {ECO:0000244|PDB:3H2T}.
STRAND 650 653 {ECO:0000244|PDB:3H2T}.
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


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