TUBE_BPT5
ID TUBE_BPT5 Reviewed; 464 AA.
AC Q6QGE2;
DT 29-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 64.
DE RecName: Full=Tail tube protein pb6 {ECO:0000303|PubMed:24198424};
DE Short=TTP-pb6;
DE AltName: Full=Major tail protein pb6;
DE Short=MTP pb6;
DE AltName: Full=Tail protein pb6 {ECO:0000303|PubMed:24198424};
GN Name=N4 {ECO:0000312|EMBL:AAS77184.1};
GN ORFNames=ORF134, T5.145 {ECO:0000312|EMBL:AAS77184.1},
GN T5p141 {ECO:0000312|EMBL:AAU05280.1};
OS Escherichia phage T5 (Enterobacteria phage T5).
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Caudovirales; Demerecviridae; Markadamsvirinae; Tequintavirus.
OX NCBI_TaxID=2695836;
OH NCBI_TaxID=562; Escherichia coli.
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Ksenzenko V.N., Kaliman A.V., Krutilina A.I., Shlyapnikov M.G.;
RT "Bacteriophage T5 complete genome.";
RL Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND INDUCTION.
RC STRAIN=ATCC 11303-B5 {ECO:0000312|EMBL:AAX12071.1};
RX PubMed=15661140; DOI=10.1016/j.virol.2004.10.049;
RA Wang J., Jiang Y., Vincent M., Sun Y., Yu H., Wang J., Bao Q., Kong H.,
RA Hu S.;
RT "Complete genome sequence of bacteriophage T5.";
RL Virology 332:45-65(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], SUBCELLULAR LOCATION, AND
RP FUNCTION.
RC STRAIN=St0 deletion mutant;
RX PubMed=24198424; DOI=10.1128/jvi.02262-13;
RA Zivanovic Y., Confalonieri F., Ponchon L., Lurz R., Chami M., Flayhan A.,
RA Renouard M., Huet A., Decottignies P., Davidson A.R., Breyton C.,
RA Boulanger P.;
RT "Insights into bacteriophage T5 structure from analysis of its
RT morphogenesis genes and protein components.";
RL J. Virol. 88:1162-1174(2014).
RN [4]
RP FUNCTION, AND SUBUNIT.
RX PubMed=16876823; DOI=10.1016/j.jmb.2006.06.081;
RA Effantin G., Boulanger P., Neumann E., Letellier L., Conway J.F.;
RT "Bacteriophage T5 structure reveals similarities with HK97 and T4
RT suggesting evolutionary relationships.";
RL J. Mol. Biol. 361:993-1002(2006).
RN [5] {ECO:0007744|PDB:5NGJ}
RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS), SUBUNIT, STRUCTURE BY ELECTRON
RP MICROSCOPY (6.0 ANGSTROMS) OF THE TAIL TUBE, DOMAIN, AND FUNCTION.
RX PubMed=29209037; DOI=10.1038/s41467-017-02049-3;
RA Arnaud C.A., Effantin G., Vives C., Engilberge S., Bacia M., Boulanger P.,
RA Girard E., Schoehn G., Breyton C.;
RT "Bacteriophage T5 tail tube structure suggests a trigger mechanism for
RT Siphoviridae DNA ejection.";
RL Nat. Commun. 8:1953-1953(2017).
CC -!- FUNCTION: Polymerizes to form the tail tube of the phage (Probable)
CC (PubMed:29209037). Tail tube protein polymerization takes place around
CC the tape measure protein (TMP-pb2) and is probably directed by
CC chaperone proteins (Probable). The tail tube is involved in viral
CC genome delivery during ejection (Probable).
CC {ECO:0000269|PubMed:29209037, ECO:0000305|PubMed:16876823,
CC ECO:0000305|PubMed:24198424}.
CC -!- SUBUNIT: Homotrimer (PubMed:16876823, PubMed:29209037). The tail tube
CC is made of 40 stacked trimeric rings (PubMed:16876823,
CC PubMed:29209037). {ECO:0000269|PubMed:16876823,
CC ECO:0000269|PubMed:29209037}.
CC -!- SUBCELLULAR LOCATION: Virion. Note=Main component of the tail tube.
CC {ECO:0000269|PubMed:24198424}.
CC -!- DOMAIN: The C-terminus possesses an Ig-like fold of the Big-2 family.
CC {ECO:0000269|PubMed:29209037}.
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DR EMBL; AY543070; AAS77184.1; -; Genomic_DNA.
DR EMBL; AY692264; AAU05280.1; -; Genomic_DNA.
DR EMBL; AY587007; AAX12071.1; -; Genomic_DNA.
DR RefSeq; YP_006973.1; NC_005859.1.
DR PDB; 5NGJ; X-ray; 2.20 A; A/B=1-464.
DR PDBsum; 5NGJ; -.
DR SMR; Q6QGE2; -.
DR GeneID; 2777634; -.
DR KEGG; vg:2777634; -.
DR Proteomes; UP000002107; Genome.
DR Proteomes; UP000002141; Genome.
DR Proteomes; UP000002503; Genome.
DR GO; GO:0098015; C:virus tail; IDA:UniProtKB.
DR GO; GO:0098026; C:virus tail, tube; IEA:UniProtKB-KW.
DR GO; GO:0099001; P:viral genome ejection through host cell envelope, long flexible tail mechanism; IEA:UniProtKB-KW.
DR GO; GO:0044659; P:viral release from host cell by cytolysis; IMP:CACAO.
DR InterPro; IPR003343; Big_2.
DR InterPro; IPR008964; Invasin/intimin_cell_adhesion.
DR Pfam; PF02368; Big_2; 1.
DR SMART; SM00635; BID_2; 1.
DR SUPFAM; SSF49373; SSF49373; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Late protein; Reference proteome;
KW Viral genome ejection through host cell envelope;
KW Viral long flexible tail ejection system;
KW Viral penetration into host cytoplasm; Viral tail protein;
KW Viral tail tube protein; Virion; Virus entry into host cell.
FT CHAIN 1..464
FT /note="Tail tube protein pb6"
FT /id="PRO_0000432944"
FT DOMAIN 375..453
FT /note="BIG2"
FT /evidence="ECO:0000269|PubMed:29209037"
FT REGION 40..59
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT STRAND 9..15
FT /evidence="ECO:0007829|PDB:5NGJ"
FT STRAND 17..19
FT /evidence="ECO:0007829|PDB:5NGJ"
FT TURN 22..24
FT /evidence="ECO:0007829|PDB:5NGJ"
FT STRAND 25..28
FT /evidence="ECO:0007829|PDB:5NGJ"
FT STRAND 34..37
FT /evidence="ECO:0007829|PDB:5NGJ"
FT STRAND 44..47
FT /evidence="ECO:0007829|PDB:5NGJ"
FT STRAND 68..75
FT /evidence="ECO:0007829|PDB:5NGJ"
FT TURN 82..84
FT /evidence="ECO:0007829|PDB:5NGJ"
FT HELIX 92..99
FT /evidence="ECO:0007829|PDB:5NGJ"
FT STRAND 108..114
FT /evidence="ECO:0007829|PDB:5NGJ"
FT STRAND 119..122
FT /evidence="ECO:0007829|PDB:5NGJ"
FT STRAND 128..130
FT /evidence="ECO:0007829|PDB:5NGJ"
FT STRAND 134..140
FT /evidence="ECO:0007829|PDB:5NGJ"
FT STRAND 143..158
FT /evidence="ECO:0007829|PDB:5NGJ"
FT STRAND 166..181
FT /evidence="ECO:0007829|PDB:5NGJ"
FT HELIX 186..189
FT /evidence="ECO:0007829|PDB:5NGJ"
FT HELIX 193..200
FT /evidence="ECO:0007829|PDB:5NGJ"
FT STRAND 209..215
FT /evidence="ECO:0007829|PDB:5NGJ"
FT TURN 216..219
FT /evidence="ECO:0007829|PDB:5NGJ"
FT STRAND 220..234
FT /evidence="ECO:0007829|PDB:5NGJ"
FT STRAND 253..255
FT /evidence="ECO:0007829|PDB:5NGJ"
FT STRAND 260..267
FT /evidence="ECO:0007829|PDB:5NGJ"
FT HELIX 271..274
FT /evidence="ECO:0007829|PDB:5NGJ"
FT HELIX 277..289
FT /evidence="ECO:0007829|PDB:5NGJ"
FT STRAND 292..299
FT /evidence="ECO:0007829|PDB:5NGJ"
FT STRAND 307..320
FT /evidence="ECO:0007829|PDB:5NGJ"
FT TURN 322..325
FT /evidence="ECO:0007829|PDB:5NGJ"
FT STRAND 332..338
FT /evidence="ECO:0007829|PDB:5NGJ"
FT STRAND 350..357
FT /evidence="ECO:0007829|PDB:5NGJ"
FT HELIX 359..368
FT /evidence="ECO:0007829|PDB:5NGJ"
FT STRAND 378..383
FT /evidence="ECO:0007829|PDB:5NGJ"
FT HELIX 384..386
FT /evidence="ECO:0007829|PDB:5NGJ"
FT STRAND 388..391
FT /evidence="ECO:0007829|PDB:5NGJ"
FT STRAND 395..403
FT /evidence="ECO:0007829|PDB:5NGJ"
FT STRAND 412..418
FT /evidence="ECO:0007829|PDB:5NGJ"
FT STRAND 420..424
FT /evidence="ECO:0007829|PDB:5NGJ"
FT STRAND 429..432
FT /evidence="ECO:0007829|PDB:5NGJ"
FT STRAND 438..450
FT /evidence="ECO:0007829|PDB:5NGJ"
FT STRAND 453..461
FT /evidence="ECO:0007829|PDB:5NGJ"
SQ SEQUENCE 464 AA; 50414 MW; C2B06343B355CBB4 CRC64;
MSLQLLRNTR IFVSTVKTGH NKTNTQEILV QDDISWGQDS NSTDITVNEA GPRPTRGSKR
FNDSLNAAEW SFSTYILPYK DKNTSKQIVP DYMLWHALSS GRAINLEGTT GAHNNATNFM
VNFKDNSYHE LAMLHIYILT DKTWSYIDSC QINQAEVNVD IEDIGRVTWS GNGNQLIPLD
EQPFDPDQIG IDDETYMTIQ GSYIKNKLTI LKIKDMDTNK SYDIPITGGT FTINNNITYL
TPNVMSRVTI PIGSFTGAFE LTGSLTAYLN DKSLGSMELY KDLIKTLKVV NRFEIALVLG
GEYDDERPAA ILVAKQAHVN IPTIETDDVL GTSVEFKAIP SDLDAGDEGY LGFSSKYTRT
TINNLIVNGD GATDAVTAIT VKSAGNVTTL NRSATLQMSV EVTPSSARNK EVTWAITAGD
AATINATGLL RADASKTGAV TVEATAKDGS GVKGTKVITV TAGG
