BP10_BPT4
ID BP10_BPT4 Reviewed; 602 AA.
AC P10928;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 29-SEP-2021, entry version 107.
DE RecName: Full=Baseplate wedge protein gp10 {ECO:0000255|HAMAP-Rule:MF_04106, ECO:0000305};
DE AltName: Full=Gene product 10 {ECO:0000305};
DE Short=gp10;
GN Name=10;
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 [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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 535-602.
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 [4]
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 [5]
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 [6]
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 [7]
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 [8]
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 [9]
RP X-RAY CRYSTALLOGRAPHY (1.2 ANGSTROMS) OF 397-602, AND FUNCTION.
RX PubMed=16554069; DOI=10.1016/j.jmb.2006.02.058;
RA Leiman P.G., Shneider M.M., Mesyanzhinov V.V., Rossmann M.G.;
RT "Evolution of bacteriophage tails: Structure of T4 gene product 10.";
RL J. Mol. Biol. 358:912-921(2006).
RN [10]
RP STRUCTURE BY ELECTRON MICROSCOPY (4.11 ANGSTROMS), SUBUNIT, SUBCELLULAR
RP LOCATION, FUNCTION, IDENTIFICATION IN THE TAIL FIBER NETWORK, DISULFIDE
RP BOND, INTERACTION WITH GP7, INTERACTION WITH GP11, AND INTERACTION WITH
RP GP12.
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: Peripheral baseplate protein that is part of the tail fiber
CC network. Connects the short tail fibers to the baseplate
CC (PubMed:16554069). During infection, the baseplate undergoes a
CC conformational change from a dome-shaped to a star-shaped structure. At
CC this point, gp10 rotates and acts as a lever that unfolds the short
CC tail fibers, which then interact with host cell surface receptors.
CC Involved in the tail assembly. {ECO:0000269|PubMed:16554069,
CC ECO:0000269|PubMed:27193680, ECO:0000303|PubMed:21129200}.
CC -!- SUBUNIT: Homotrimer; disulfide-linked (PubMed:19896486,
CC PubMed:27193680). Heteromultimer with gp7 (PubMed:19896486,
CC PubMed:27193680); a gp10 molecule is disulfide-linked to gp7 and the
CC other two remaining gp10 molecules form a disulfide bond
CC (PubMed:27193680). The gp10 trimer interacts with gp11 trimer and with
CC the short tail fiber (STF) composed of the gp12 trimer
CC (PubMed:27193680). Part of the baseplate macromolecular complex which
CC consists of gp5, gp5.4, gp27 (central spike complex); gp6, gp25, gp53
CC (inner baseplate); gp7, gp8 (intermediate baseplate); gp9, gp10, gp11,
CC gp12 (peripheral); gp48 and gp54 (proximal region of the tail tube)
CC (PubMed:27193680). {ECO:0000255|HAMAP-Rule:MF_04106,
CC ECO:0000269|PubMed:19896486, ECO:0000269|PubMed:27193680}.
CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000255|HAMAP-Rule:MF_04106,
CC ECO:0000269|PubMed:15315755, 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:0000255|HAMAP-Rule:MF_04106}.
CC -!- SIMILARITY: Belongs to the T4likevirus baseplate wedge protein gp10
CC family. {ECO:0000255|HAMAP-Rule:MF_04106}.
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DR EMBL; X14192; CAA32396.1; -; Genomic_DNA.
DR EMBL; AF158101; AAD42415.1; -; Genomic_DNA.
DR EMBL; M26253; AAA32493.1; -; Genomic_DNA.
DR PIR; S04083; GEBPT4.
DR RefSeq; NP_049768.1; NC_000866.4.
DR PDB; 2FKK; X-ray; 1.20 A; A=397-602.
DR PDB; 2FL8; EM; 1.20 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R=1-602.
DR PDB; 2FL9; EM; 17.00 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R=1-602.
DR PDB; 5HX2; EM; 3.80 A; G/H/I=1-602.
DR PDB; 5IV5; EM; 4.11 A; AC/AD/AE/CF/CG/CH/EI/EJ/FA/HB/HC/HD/I/J/K/f/g/h=1-602.
DR PDB; 5IV7; EM; 6.77 A; AE/AF/AG/CG/DA/DB/FB/FC/FD/I/J/K/Y/Z/a/o/p/q=1-602.
DR PDBsum; 2FKK; -.
DR PDBsum; 2FL8; -.
DR PDBsum; 2FL9; -.
DR PDBsum; 5HX2; -.
DR PDBsum; 5IV5; -.
DR PDBsum; 5IV7; -.
DR SMR; P10928; -.
DR TCDB; 1.K.1.1.1; the gp27/5 t4-baseplate (t4-bp) family.
DR GeneID; 1258808; -.
DR KEGG; vg:1258808; -.
DR EvolutionaryTrace; P10928; -.
DR Proteomes; UP000009087; Genome.
DR GO; GO:0098025; C:virus tail, baseplate; IDA:UniProtKB.
DR GO; GO:0019076; P:viral release from host cell; IEA:InterPro.
DR GO; GO:0098003; P:viral tail assembly; IEA:UniProtKB-KW.
DR Gene3D; 2.60.120.640; -; 1.
DR HAMAP; MF_04106; BP10_T4; 1.
DR InterPro; IPR008987; Baseplate_struct_prot_Gp9/10.
DR InterPro; IPR034695; BP10_T4.
DR InterPro; IPR036240; Gp9-like_sf.
DR InterPro; IPR027411; Gp9/Gp10_mid_dom_sf.
DR Pfam; PF07880; T4_gp9_10; 1.
DR SUPFAM; SSF50017; SSF50017; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Disulfide bond; Late protein; Reference proteome;
KW Viral baseplate protein; Viral release from host cell; Viral tail assembly;
KW Viral tail protein; Virion.
FT CHAIN 1..602
FT /note="Baseplate wedge protein gp10"
FT /id="PRO_0000165000"
FT REGION 501..523
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 555
FT /note="Interchain (with C-187 in GP7); alternate"
FT /evidence="ECO:0000269|PubMed:27193680"
FT DISULFID 555
FT /note="Interchain; alternate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04106,
FT ECO:0000269|PubMed:27193680"
FT STRAND 414..416
FT /evidence="ECO:0007829|PDB:2FKK"
FT STRAND 420..423
FT /evidence="ECO:0007829|PDB:2FKK"
FT STRAND 425..427
FT /evidence="ECO:0007829|PDB:2FKK"
FT STRAND 432..435
FT /evidence="ECO:0007829|PDB:2FKK"
FT STRAND 439..441
FT /evidence="ECO:0007829|PDB:2FKK"
FT HELIX 446..453
FT /evidence="ECO:0007829|PDB:2FKK"
FT STRAND 459..464
FT /evidence="ECO:0007829|PDB:2FKK"
FT HELIX 470..473
FT /evidence="ECO:0007829|PDB:2FKK"
FT STRAND 477..480
FT /evidence="ECO:0007829|PDB:2FKK"
FT TURN 497..499
FT /evidence="ECO:0007829|PDB:2FKK"
FT STRAND 500..506
FT /evidence="ECO:0007829|PDB:2FKK"
FT STRAND 512..516
FT /evidence="ECO:0007829|PDB:2FKK"
FT STRAND 523..525
FT /evidence="ECO:0007829|PDB:2FKK"
FT HELIX 529..531
FT /evidence="ECO:0007829|PDB:2FKK"
FT STRAND 596..602
FT /evidence="ECO:0007829|PDB:2FKK"
SQ SEQUENCE 602 AA; 66232 MW; 1159B8C7EBB8EF54 CRC64;
MKQNINIGNV VDDGTGDYLR KGGIKINENF DELYYELGDG DVPYSAGAWK TYNASSGQTL
TAEWGKSYAI NTSSGRVTIN LPKGTVNDYN KVIRARDVFA TWNVNPVTLV AASGDTIKGS
AVPVEINVRF SDLELVYCAP GRWEYVKNKQ IDKITSSDIS NVARKEFLVE VQGQTDFLDV
FRGTSYNVNN IRVKHRGNEL YYGDVFSENS DFGSPGENEG ELVPLDGFNI RLRQPCNIGD
TVQIETFMDG VSQWRSSYTR RQIRLLDSKL TSKTSLEGSI YVTDLSTMKS IPFSAFGLIP
GEPINPNSLE VRFNGILQEL AGTVGMPLFH CVGADSDDEV ECSVLGGTWE QSHTDYSVET
DENGIPEILH FDSVFEHGDI INITWFNNDL GTLLTKDEII DETDNLYVSQ GPGVDISGDV
NLTDFDKIGW PNVEAVQSYQ RAFNAVSNIF DTIYPIGTIY ENAVNPNNPV TYMGFGSWKL
FGQGKVLVGW NEDISDPNFA LNNNDLDSGG NPSHTAGGTG GSTSVTLENA NLPATETDEE
VLIVDENGSV IVGGCQYDPD ESGPIYTKYR EAKASTNSTH TPPTSITNIQ PYITVYRWIR
IA
