ID   CAPSD_BPMU              Reviewed;         305 AA.
AC   Q9T1W1;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   23-FEB-2022, entry version 60.
DE   RecName: Full=Major capsid protein {ECO:0000303|PubMed:8599204};
DE   AltName: Full=Gene product 34;
DE            Short=gp34;
DE   AltName: Full=Gene product T;
DE            Short=gpT;
DE   AltName: Full=Major head protein {ECO:0000305};
GN   Name=T; OrderedLocusNames=Mup34;
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 [LARGE SCALE GENOMIC DNA], PROTEIN SEQUENCE OF 1-8, AND
RP   FUNCTION.
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   [2]
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   [3]
RP   FUNCTION, SUBUNIT, AND 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   [4]
RP   FUNCTION.
RX   PubMed=9495752; DOI=10.1128/jb.180.5.1148-1153.1998;
RA   Grimaud R., Toussaint A.;
RT   "Assembly of both the head and tail of bacteriophage Mu is blocked in
RT   Escherichia coli groEL and groES mutants.";
RL   J. Bacteriol. 180:1148-1153(1998).
CC   -!- FUNCTION: Capsid protein that self-assembles to form an icosahedral
CC       capsid, about 54 nm in diameter. {ECO:0000269|PubMed:11922669,
CC       ECO:0000269|PubMed:8599204, ECO:0000269|PubMed:9495752}.
CC   -!- SUBUNIT: Part of the immature prohead complex. Interaction between the
CC       viral portal protein and the viral protease I may give rise to an early
CC       25S initiator complex. The scaffolding protein Z and the capsid protein
CC       T should then be added to the initiator complex to yield immature
CC       procapsid (Probable). Host GroEL and GroES are also essential for the
CC       correct assembly of viral capsids. {ECO:0000269|PubMed:8599204,
CC       ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Virion {ECO:0000269|PubMed:8599204}. Host
CC       cytoplasm {ECO:0000305|PubMed:8599204}. Note=Capsid.
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}.
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DR   EMBL; AF083977; AAF01112.1; -; Genomic_DNA.
DR   RefSeq; NP_050638.1; NC_000929.1.
DR   GeneID; 2636267; -.
DR   KEGG; vg:2636267; -.
DR   Proteomes; UP000002611; Genome.
DR   GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0098017; C:viral capsid, major subunit; IMP:CACAO.
DR   InterPro; IPR018774; Phage_Mu_GpT.
DR   Pfam; PF10124; Mu-like_gpT; 1.
PE   1: Evidence at protein level;
KW   Capsid protein; Direct protein sequencing; Host cytoplasm; Late protein;
KW   Reference proteome; Viral capsid assembly; Viral release from host cell;
KW   Virion.
FT   CHAIN           1..305
FT                   /note="Major capsid protein"
FT                   /id="PRO_0000077695"
SQ   SEQUENCE   305 AA;  34160 MW;  01B4925C16EDC4CF CRC64;
     MIVTPASIKA LMTSWRKDFQ GGLEDAPSQY NKIAMVVNSS TRSNTYGWLG KFPTLKEWVG
     KRTIQQMEAH GYSIANKTFE GTVGISRDDF EDDNLGIYAP IFQEMGRSAA VQPDELIFKL
     LKDGFTQPCY DGQNFFDKEH PVYPNVDGTG SAVNTSNIVE QDSFSGLPFY LLDCSRAVKP
     LIFQERRKPE LVARTRIDDD HVFMDNEFLF GASTRRAAGY GFWQMAVAVK GDLTLDNLWK
     GWQLMRSFEG DGGKKLGLKP THIVVPVGLE KAAEQLLNRE LFADGNTTVS NEMKGKLQLV
     VADYL