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BP09_BPT4
ID   BP09_BPT4               Reviewed;         288 AA.
AC   P10927;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1989, sequence version 1.
DT   29-SEP-2021, entry version 114.
DE   RecName: Full=Baseplate protein gp9 {ECO:0000305};
DE   AltName: Full=Gene product 9 {ECO:0000305};
DE            Short=gp9;
GN   Name=9;
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   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   [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   X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS), FUNCTION, SUBUNIT, DOMAIN, AND
RP   COILED COIL.
RX   PubMed=10545330; DOI=10.1016/s0969-2126(00)80055-6;
RA   Kostyuchenko V.A., Navruzbekov G.A., Kurochkina L.P., Strelkov S.V.,
RA   Mesyanzhinov V.V., Rossmann M.G.;
RT   "The structure of bacteriophage T4 gene product 9: the trigger for tail
RT   contraction.";
RL   Structure 7:1213-1222(1999).
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   STRUCTURE BY ELECTRON MICROSCOPY (4.11 ANGSTROMS), SUBUNIT, SUBCELLULAR
RP   LOCATION, FUNCTION, AND IDENTIFICATION IN THE TAIL FIBER NETWORK.
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 (PubMed:10545330, PubMed:27193680). Connects the long tail
CC       fibers to the baseplate and, after virus attachment to a host cell,
CC       probably changes its conformation to trigger the signal for tail
CC       contraction (PubMed:10545330). Involved in the tail assembly
CC       (PubMed:21129200). {ECO:0000269|PubMed:10545330,
CC       ECO:0000269|PubMed:27193680, ECO:0000303|PubMed:21129200}.
CC   -!- SUBUNIT: Homotrimer (PubMed:27193680). The gp9 trimer interacts with
CC       the long tail fiber (LTF) that comprises gp34 trimer, gp35, gp36 and a
CC       gp37 trimer. 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       {ECO:0000269|PubMed:10545330, ECO:0000269|PubMed:19896486,
CC       ECO:0000269|PubMed:27193680}.
CC   -!- SUBCELLULAR LOCATION: Virion {ECO:0000269|PubMed:15315755,
CC       ECO:0000269|PubMed:2403438, ECO:0000269|PubMed:27193680}. Note=Present
CC       in 18 copies in the baseplate. {ECO:0000303|PubMed:21129200}.
CC   -!- INDUCTION: Expressed in the late phase of the viral replicative cycle.
CC       {ECO:0000305}.
CC   -!- DOMAIN: The C-terminus is bound to the baseplate, and the N-terminus
CC       coiled-coil domain is associated with the long tail fibers.
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DR   EMBL; X14192; CAA32395.1; -; Genomic_DNA.
DR   EMBL; AF158101; AAD42520.1; -; Genomic_DNA.
DR   PIR; S04082; GNBPT4.
DR   RefSeq; NP_049767.1; NC_000866.4.
DR   PDB; 1PDP; EM; 12.00 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R=1-288.
DR   PDB; 1QEX; X-ray; 2.30 A; A/B=1-288.
DR   PDB; 1S2E; X-ray; 2.30 A; A/B=1-288.
DR   PDB; 1TJA; EM; 16.00 A; C/D/E=1-288.
DR   PDB; 1ZKU; EM; 15.00 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R=1-288.
DR   PDB; 5IV5; EM; 4.11 A; AA/AB/CC/CD/CE/EF/EG/EH/F/G/GI/GJ/H/HA/c/d/e/z=1-288.
DR   PDB; 5IV7; EM; 6.77 A; AB/AC/AD/CD/CE/CF/EF/EG/F/FA/G/H/V/W/X/l/m/n=1-288.
DR   PDBsum; 1PDP; -.
DR   PDBsum; 1QEX; -.
DR   PDBsum; 1S2E; -.
DR   PDBsum; 1TJA; -.
DR   PDBsum; 1ZKU; -.
DR   PDBsum; 5IV5; -.
DR   PDBsum; 5IV7; -.
DR   SMR; P10927; -.
DR   TCDB; 1.K.1.1.1; the gp27/5 t4-baseplate (t4-bp) family.
DR   GeneID; 1258617; -.
DR   KEGG; vg:1258617; -.
DR   EvolutionaryTrace; P10927; -.
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   Gene3D; 2.60.40.1680; -; 1.
DR   InterPro; IPR008987; Baseplate_struct_prot_Gp9/10.
DR   InterPro; IPR036240; Gp9-like_sf.
DR   InterPro; IPR027411; Gp9/Gp10_mid_dom_sf.
DR   InterPro; IPR027412; Gp9_C_dom_sf.
DR   Pfam; PF07880; T4_gp9_10; 1.
DR   SUPFAM; SSF50017; SSF50017; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Coiled coil; Reference proteome; Viral baseplate protein;
KW   Viral release from host cell; Viral tail assembly; Viral tail protein;
KW   Virion.
FT   CHAIN           1..288
FT                   /note="Baseplate protein gp9"
FT                   /id="PRO_0000164999"
FT   COILED          20..80
FT                   /evidence="ECO:0000269|PubMed:10545330"
FT   STRAND          15..19
FT                   /evidence="ECO:0007829|PDB:1QEX"
FT   HELIX           20..39
FT                   /evidence="ECO:0007829|PDB:1QEX"
FT   HELIX           45..49
FT                   /evidence="ECO:0007829|PDB:1QEX"
FT   STRAND          50..53
FT                   /evidence="ECO:0007829|PDB:1QEX"
FT   HELIX           74..76
FT                   /evidence="ECO:0007829|PDB:1QEX"
FT   STRAND          84..86
FT                   /evidence="ECO:0007829|PDB:1QEX"
FT   STRAND          90..92
FT                   /evidence="ECO:0007829|PDB:1QEX"
FT   STRAND          94..98
FT                   /evidence="ECO:0007829|PDB:1QEX"
FT   STRAND          106..110
FT                   /evidence="ECO:0007829|PDB:1QEX"
FT   STRAND          118..120
FT                   /evidence="ECO:0007829|PDB:1QEX"
FT   STRAND          122..130
FT                   /evidence="ECO:0007829|PDB:1QEX"
FT   STRAND          134..139
FT                   /evidence="ECO:0007829|PDB:1QEX"
FT   STRAND          144..152
FT                   /evidence="ECO:0007829|PDB:1QEX"
FT   STRAND          154..156
FT                   /evidence="ECO:0007829|PDB:1QEX"
FT   STRAND          159..169
FT                   /evidence="ECO:0007829|PDB:1QEX"
FT   STRAND          176..180
FT                   /evidence="ECO:0007829|PDB:1QEX"
FT   STRAND          185..193
FT                   /evidence="ECO:0007829|PDB:1QEX"
FT   TURN            194..196
FT                   /evidence="ECO:0007829|PDB:1QEX"
FT   STRAND          198..208
FT                   /evidence="ECO:0007829|PDB:1QEX"
FT   STRAND          214..224
FT                   /evidence="ECO:0007829|PDB:1QEX"
FT   TURN            225..228
FT                   /evidence="ECO:0007829|PDB:1QEX"
FT   STRAND          229..241
FT                   /evidence="ECO:0007829|PDB:1QEX"
FT   STRAND          243..247
FT                   /evidence="ECO:0007829|PDB:1QEX"
FT   STRAND          251..257
FT                   /evidence="ECO:0007829|PDB:1QEX"
FT   STRAND          260..266
FT                   /evidence="ECO:0007829|PDB:1QEX"
FT   STRAND          268..282
FT                   /evidence="ECO:0007829|PDB:1QEX"
SQ   SEQUENCE   288 AA;  30997 MW;  8028FCEBA25BB760 CRC64;
     MFIQEPKKLI DTGEIGNAST GDILFDGGNK INSDFNAIYN AFGDQRKMAV ANGTGADGQI
     IHATGYYQKH SITEYATPVK VGTRHDIDTS TVGVKVIIER GELGDCVEFI NSNGSISVTN
     PLTIQAIDSI KGVSGNLVVT SPYSKVTLRC ISSDNSTSVW NYSIESMFGQ KESPAEGTWN
     ISTSGSVDIP LFHRTEYNMA KLLVTCQSVD GRKIKTAEIN ILVDTVNSEV ISSEYAVMRV
     GNETEEDEIA NIAFSIKENY VTATISSSTV GMRAAVKVIA TQKIGVAQ
 
 
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