TUBE_BPT4
ID TUBE_BPT4 Reviewed; 163 AA.
AC P13333;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1990, sequence version 1.
DT 29-SEP-2021, entry version 91.
DE RecName: Full=Tail tube protein gp19 {ECO:0000305};
DE AltName: Full=Gene product 19 {ECO:0000305};
DE Short=gp19;
GN Name=19;
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], AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=2963141; DOI=10.1128/jvi.62.3.882-886.1988;
RA Arisaka F., Ishimoto L., Kassavetis G., Kumazaki T., Ishii S.;
RT "Nucleotide sequence of the tail tube structural gene of bacteriophage
RT T4.";
RL J. Virol. 62:882-886(1988).
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 FUNCTION.
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 [4]
RP SUBCELLULAR LOCATION AND SUBUNIT.
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 [5]
RP STRUCTURE BY ELECTRON MICROSCOPY (4.11 ANGSTROMS), SUBUNIT, SUBCELLULAR
RP LOCATION, AND FUNCTION.
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: Forms the central cylindrical rigid tube, which is surrounded
CC by the outer contractile sheath assembled from gp18 subunits. The tail
CC tube first 2 annuli are formed by gp48 and gp54, which are in
CC continuation of the spike complex. During infection, contraction of the
CC sheath drives the central tube through the host outer membrane,
CC creating a channel for DNA ejection from the capsid into the host cell.
CC {ECO:0000269|PubMed:14625682, ECO:0000269|PubMed:27193680}.
CC -!- SUBUNIT: Homohexamer. The tube is composed of gp19 hexameric rings.
CC Interacts with gp54. {ECO:0000269|PubMed:27193680}.
CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000269|PubMed:15315755,
CC ECO:0000269|PubMed:27193680}.
CC -!- SIMILARITY: Belongs to the T4-like viruses Gp19 protein family.
CC {ECO:0000305}.
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DR EMBL; M19085; AAA32542.1; -; Genomic_DNA.
DR EMBL; AF158101; AAD42424.1; -; Genomic_DNA.
DR PIR; JF0022; JF0022.
DR RefSeq; NP_049781.1; NC_000866.4.
DR PDB; 5IV5; EM; 4.11 A; BB/BC/DE/DF/FH/FI/IA/IB/R/S/o/p=1-163.
DR PDB; 5W5F; EM; 3.40 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R=1-163.
DR PDBsum; 5IV5; -.
DR PDBsum; 5W5F; -.
DR SMR; P13333; -.
DR TCDB; 1.K.1.1.1; the gp27/5 t4-baseplate (t4-bp) family.
DR GeneID; 1258727; -.
DR KEGG; vg:1258727; -.
DR Proteomes; UP000009087; Genome.
DR GO; GO:0098026; C:virus tail, tube; IDA:UniProtKB.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR GO; GO:0099000; P:viral genome ejection through host cell envelope, contractile tail mechanism; IEA:UniProtKB-KW.
DR InterPro; IPR010667; Phage_T4_Gp19.
DR Pfam; PF06841; Phage_T4_gp19; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Late protein; Reference proteome;
KW Viral contractile tail ejection system;
KW Viral genome ejection through host cell envelope;
KW Viral penetration into host cytoplasm; Viral tail protein;
KW Viral tail tube protein; Virion; Virus entry into host cell.
FT CHAIN 1..163
FT /note="Tail tube protein gp19"
FT /id="PRO_0000165008"
FT HELIX 5..9
FT /evidence="ECO:0007829|PDB:5W5F"
FT HELIX 11..13
FT /evidence="ECO:0007829|PDB:5W5F"
FT STRAND 18..24
FT /evidence="ECO:0007829|PDB:5W5F"
FT TURN 26..28
FT /evidence="ECO:0007829|PDB:5W5F"
FT HELIX 32..34
FT /evidence="ECO:0007829|PDB:5W5F"
FT STRAND 36..41
FT /evidence="ECO:0007829|PDB:5W5F"
FT STRAND 44..53
FT /evidence="ECO:0007829|PDB:5W5F"
FT STRAND 56..66
FT /evidence="ECO:0007829|PDB:5W5F"
FT STRAND 69..74
FT /evidence="ECO:0007829|PDB:5W5F"
FT HELIX 80..92
FT /evidence="ECO:0007829|PDB:5W5F"
FT STRAND 96..98
FT /evidence="ECO:0007829|PDB:5W5F"
FT HELIX 104..107
FT /evidence="ECO:0007829|PDB:5W5F"
FT STRAND 109..116
FT /evidence="ECO:0007829|PDB:5W5F"
FT STRAND 123..138
FT /evidence="ECO:0007829|PDB:5W5F"
FT STRAND 140..145
FT /evidence="ECO:0007829|PDB:5W5F"
FT STRAND 152..158
FT /evidence="ECO:0007829|PDB:5W5F"
FT STRAND 160..163
FT /evidence="ECO:0007829|PDB:5W5F"
SQ SEQUENCE 163 AA; 18462 MW; 4F39B2DA401B3CD9 CRC64;
MFVDDVTRAF ESGDFARPNL FQVEISYLGQ NFTFQCKATA LPAGIVEKIP VGFMNRKINV
AGDRTFDDWT VTVMNDEAHD ARQKFVDWQS IAAGQGNEIT GGKPAEYKKS AIVRQYARDA
KTVTKEIEIK GLWPTNVGEL QLDWDSNNEI QTFEVTLALD YWE
