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 02-SEP-2026, entry version 96. 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 Pantevenvirales; Straboviridae; 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 PDB; 9MKB; EM; 3.80 A; eB/eU/eW/f9/fA/fB/fR/fS/fU/fW/fr/fs=1-660. DR PDB; 9MOG; EM; 3.60 A; eB/eU/eW/f9/fA/fB/fR/fS/fU/fW/fr/fs=1-660. DR EMDB; EMD-48324; -. DR EMDB; EMD-48459; -. DR EMDB; EMD-8064; -. 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 OrthoDB; 668at10239; -. DR EvolutionaryTrace; P19060; -. DR Proteomes; UP000009087; Segment. 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 Gene3D; 3.30.300.200; -; 1. DR HAMAP; MF_04102; BP06_T4; 1. DR InterPro; IPR049026; Gp6-like_N. DR InterPro; IPR062297; Gp6_3rd. DR InterPro; IPR049027; Gp6_C-I. DR InterPro; IPR049028; gp6_C-II. DR InterPro; IPR054065; Gp6_C-III. DR InterPro; IPR049029; Gp6_II_1st. DR InterPro; IPR034698; GP6_T4. DR Pfam; PF21379; Gp6-like_1st; 1. DR Pfam; PF21515; Gp6_2nd; 1. DR Pfam; PF31222; Gp6_3rd; 1. DR Pfam; PF21472; gp6_C-domII; 1. DR Pfam; PF21387; Gp6_C-I; 1. DR Pfam; PF21871; Gp6_C-III; 1. DR PDBsum; 3H2T; -. DR PDBsum; 3H3W; -. DR PDBsum; 3H3Y; -. DR PDBsum; 5HX2; -. DR PDBsum; 5IV5; -. DR PDBsum; 5IV7; -. DR PDBsum; 9MKB; -. DR PDBsum; 9MOG; -. 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..447 FT /evidence="ECO:0007829|PDB:3H2T" FT HELIX 448..452 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 //