ID   TSP_BPMU                Reviewed;         495 AA.
AC   P79678;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   03-AUG-2022, entry version 77.
DE   RecName: Full=Tail sheath protein;
DE            Short=TSP;
DE   AltName: Full=Gene product 39;
DE            Short=gp39;
DE   AltName: Full=Gene product L;
DE            Short=gpL;
GN   Name=L; OrderedLocusNames=Mup39;
OS   Escherichia phage Mu (Bacteriophage Mu).
OC   Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC   Caudovirales; Myoviridae; Muvirus.
OX   NCBI_TaxID=10677;
OH   NCBI_TaxID=543; Enterobacteriaceae.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], IDENTIFICATION, FUNCTION, AND PROTEIN
RP   SEQUENCE OF 2-11.
RX   PubMed=9714755; DOI=10.1016/s0167-4781(98)00102-x;
RA   Takeda S., Sasaki T., Ritani A., Howe M.M., Arisaka F.;
RT   "Discovery of the tail tube gene of bacteriophage Mu and sequence analysis
RT   of the sheath and tube genes.";
RL   Biochim. Biophys. Acta 1399:88-92(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND PROTEIN SEQUENCE OF
RP   1-11.
RX   PubMed=11922669; DOI=10.1006/jmbi.2002.5437;
RA   Morgan G.J., Hatfull G.F., Casjens S., Hendrix R.W.;
RT   "Bacteriophage Mu genome sequence: analysis and comparison with Mu-like
RT   prophages in Haemophilus, Neisseria and Deinococcus.";
RL   J. Mol. Biol. 317:337-359(2002).
RN   [3]
RP   DISRUPTION PHENOTYPE.
RX   PubMed=3904174; DOI=10.1016/0042-6822(85)90388-5;
RA   Grundy F.J., Howe M.M.;
RT   "Morphogenetic structures present in lysates of amber mutants of
RT   bacteriophage Mu.";
RL   Virology 143:485-504(1985).
RN   [4]
RP   INDUCTION.
RX   PubMed=8293968; DOI=10.1093/genetics/135.3.619;
RA   Chiang L.W., Howe M.M.;
RT   "Mutational analysis of a C-dependent late promoter of bacteriophage Mu.";
RL   Genetics 135:619-629(1993).
RN   [5]
RP   SUBCELLULAR LOCATION.
RX   PubMed=8599204; DOI=10.1006/viro.1996.0107;
RA   Grimaud R.;
RT   "Bacteriophage Mu head assembly.";
RL   Virology 217:200-210(1996).
RN   [6]
RP   REVIEW.
RX   PubMed=22297511; DOI=10.1007/978-1-4614-0980-9_5;
RA   Leiman P.G., Shneider M.M.;
RT   "Contractile tail machines of bacteriophages.";
RL   Adv. Exp. Med. Biol. 726:93-114(2012).
RN   [7]
RP   STRUCTURE BY ELECTRON MICROSCOPY OF THE SHEATH, AND SUBUNIT.
RX   PubMed=948102; DOI=10.1016/s0022-5320(76)80140-2;
RA   Admiraal G., Mellema J.E.;
RT   "The structure of the contractile sheath of bacteriophage Mu.";
RL   J. Ultrastruct. Res. 56:48-64(1976).
RN   [8]
RP   STRUCTURE BY ELECTRON MICROSCOPY OF THE SHEATH.
RX   PubMed=923585; DOI=10.1111/j.1432-1033.1977.tb11894.x;
RA   Cremers A.F., Schepman A.M., Visser M.P., Mellema J.E.;
RT   "An analysis of the contracted sheath structure of bacteriophage Mu.";
RL   Eur. J. Biochem. 80:393-400(1977).
CC   -!- FUNCTION: Polymerizes as an extended helical structure around the
CC       baseplate-tail tube complex. During ejection, the sheath shifts to a
CC       contracted form, thereby making the inner tail tube protrude through
CC       the host cell envelope. {ECO:0000269|PubMed:9714755}.
CC   -!- SUBUNIT: Homomultimer. {ECO:0000305|PubMed:948102}.
CC   -!- SUBCELLULAR LOCATION: Virion {ECO:0000269|PubMed:8599204}. Host
CC       cytoplasm {ECO:0000305|PubMed:8599204}. Note=Tail. {ECO:0000305}.
CC   -!- INDUCTION: Expressed in the late phase of the viral replicative cycle.
CC       Expression of late genes is activated by the viral late transcription
CC       activator C. {ECO:0000269|PubMed:8293968}.
CC   -!- DISRUPTION PHENOTYPE: No tail is synthesized.
CC       {ECO:0000269|PubMed:3904174}.
CC   -!- SIMILARITY: Belongs to the myoviridae tail sheath protein family.
CC       {ECO:0000305}.
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DR   EMBL; AB000833; BAA19195.1; -; Genomic_DNA.
DR   EMBL; AF083977; AAF01117.1; -; Genomic_DNA.
DR   RefSeq; NP_050643.1; NC_000929.1.
DR   PRIDE; P79678; -.
DR   GeneID; 2636269; -.
DR   KEGG; vg:2636269; -.
DR   Proteomes; UP000002611; Genome.
DR   GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0098027; C:virus tail, sheath; IDA:UniProtKB.
DR   GO; GO:0099000; P:viral genome ejection through host cell envelope, contractile tail mechanism; IEA:UniProtKB-KW.
DR   InterPro; IPR035089; Phage_sheath_subtilisin.
DR   InterPro; IPR007067; Tail_sheath.
DR   InterPro; IPR020287; Tail_sheath_C.
DR   Pfam; PF04984; Phage_sheath_1; 1.
DR   Pfam; PF17482; Phage_sheath_1C; 1.
DR   PIRSF; PIRSF007349; Tsp_L; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Host cytoplasm; Late protein;
KW   Reference proteome; 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 sheath protein; Virion; Virus entry into host cell.
FT   INIT_MET        1
FT                   /note="Removed; by host"
FT                   /evidence="ECO:0000269|PubMed:9714755"
FT   CHAIN           2..495
FT                   /note="Tail sheath protein"
FT                   /id="PRO_0000077686"
SQ   SEQUENCE   495 AA;  53092 MW;  56E999885916AB0E CRC64;
     MSDISFNAIP SDVRVPLTYI EFDNSNAVSG TPAPRQRVLM FGQSGSKASA APNVPVRIRS
     GSQASAAFGQ GSMLALMADA FLNANRVAEL WCIPQGNGTG NAAVGEISLS GTAGENGSLV
     TYIAGQRLAV SVAAGATGAA LADLLVARIK GQPDLPVTAE VRADSGDDDT HADVVLSAKF
     TGALSAVDVR WNYYAGETTP YGIITAFKAA SGKNGNPDIS ASIAGMGDLQ YKYIVMPYTD
     EPNLNLLRTE LQERWGPVNQ ADGFAVTVLS GTYGDISTFG VSRNDHLISC MGIAGAPEPS
     YLYAATLCAV ASQALSIDPA RPLQTLTLPG RMPPAVGDRF TWSERNALLF DGISTFNVND
     GGEMQIERMI TMYRTNKYGD SDPSYLNVNT IATLSYLRYS LRTRITQKFP NYKLASDGTR
     FATGQAVVTP SVIKTELLAL FEEWENAGLV EDFDTFKEEL YVARNKDDKD RLDVLCGPNL
     INQFRIFAAQ VQFIL