ID   PRO_BPT5                Reviewed;         210 AA.
AC   Q6QGD7; Q66LR7;
DT   17-FEB-2016, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 67.
DE   RecName: Full=Prohead protease {ECO:0000303|PubMed:24198424};
DE            EC=3.4.21.-;
DE   Flags: Precursor;
GN   ORFNames=T5.150 {ECO:0000312|EMBL:AAS77189.1},
GN   T5p146 {ECO:0000312|EMBL:AAU05285.1};
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:AAX12076.1};
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,
RP   FUNCTION, AND PROTEOLYTIC CLEAVAGE.
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   STRUCTURE BY ELECTRON MICROSCOPY (30.0 ANGSTROMS) OF THE CAPSID, FUNCTION,
RP   MUTAGENESIS OF HIS-76; SER-122 AND GLU-148, AND ACTIVE SITE.
RX   PubMed=26616586; DOI=10.1016/j.jmb.2015.11.019;
RA   Huet A., Duda R.L., Hendrix R.W., Boulanger P., Conway J.F.;
RT   "Correct assembly of the bacteriophage T5 procapsid requires both the
RT   maturation protease and the portal complex.";
RL   J. Mol. Biol. 428:165-181(2016).
CC   -!- FUNCTION: Serine protease involved in capsid assembly and maturation.
CC       Cleaves the major capsid protein, the decoration protein, the portal
CC       protein to yield mature procapsids competent for DNA packaging
CC       (Probable). Acts as a trigger for assembly of the capsid protein.
CC       {ECO:0000269|PubMed:24198424, ECO:0000269|PubMed:26616586}.
CC   -!- SUBCELLULAR LOCATION: Virion {ECO:0000269|PubMed:24198424}.
CC       Note=Present in the prohead I. {ECO:0000269|PubMed:24198424}.
CC   -!- PTM: Cleaves itself autocatalytically to yield the mature form of the
CC       protease (Probable). {ECO:0000269|PubMed:24198424}.
CC   -!- SIMILARITY: Belongs to the HK97 prohead protease protein family.
CC       {ECO:0000305}.
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DR   EMBL; AY543070; AAS77189.1; -; Genomic_DNA.
DR   EMBL; AY587007; AAX12076.1; -; Genomic_DNA.
DR   EMBL; AY692264; AAU05285.1; -; Genomic_DNA.
DR   RefSeq; YP_006978.1; NC_005859.1.
DR   MEROPS; S78.002; -.
DR   GeneID; 2777674; -.
DR   KEGG; vg:2777674; -.
DR   Proteomes; UP000002107; Genome.
DR   Proteomes; UP000002141; Genome.
DR   Proteomes; UP000002503; Genome.
DR   GO; GO:0008233; F:peptidase activity; IDA:UniProtKB.
DR   GO; GO:0008236; F:serine-type peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   GO; GO:0046797; P:viral procapsid maturation; IEA:UniProtKB-KW.
DR   InterPro; IPR006433; Prohead_protease.
DR   Pfam; PF04586; Peptidase_S78; 1.
DR   TIGRFAMs; TIGR01543; proheadase_HK97; 1.
PE   1: Evidence at protein level;
KW   Hydrolase; Late protein; Protease; Reference proteome; Serine protease;
KW   Viral capsid assembly; Viral capsid maturation;
KW   Viral release from host cell; Virion.
FT   PROPEP          1..23
FT                   /evidence="ECO:0000269|PubMed:24198424"
FT                   /id="PRO_0000435557"
FT   CHAIN           24..166
FT                   /note="Prohead protease"
FT                   /id="PRO_0000435558"
FT   PROPEP          167..210
FT                   /evidence="ECO:0000269|PubMed:24198424"
FT                   /id="PRO_0000435559"
FT   ACT_SITE        76
FT                   /evidence="ECO:0000269|PubMed:26616586"
FT   ACT_SITE        122
FT                   /evidence="ECO:0000269|PubMed:26616586"
FT   ACT_SITE        148
FT                   /evidence="ECO:0000269|PubMed:26616586"
FT   SITE            23..24
FT                   /note="Cleavage; by autolysis"
FT                   /evidence="ECO:0000269|PubMed:24198424"
FT   SITE            166..167
FT                   /note="Cleavage; by autolysis"
FT                   /evidence="ECO:0000269|PubMed:24198424"
FT   MUTAGEN         76
FT                   /note="H->A,Y: Complete loss of protease activity."
FT                   /evidence="ECO:0000269|PubMed:26616586"
FT   MUTAGEN         122
FT                   /note="S->A: Complete loss of protease activity."
FT                   /evidence="ECO:0000269|PubMed:26616586"
FT   MUTAGEN         148
FT                   /note="E->A: Complete loss of protease activity."
FT                   /evidence="ECO:0000269|PubMed:26616586"
FT   CONFLICT        102
FT                   /note="N -> Y (in Ref. 2; AAX12076 and 3; AAU05285)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   210 AA;  23379 MW;  B1531997730D48CF CRC64;
     MTQAAIDYNK LKSAPVHLDA YIKSIDSESK EGVVKIRGFA NTISKDRAGD VIPASAWKTS
     NALTNYMKNP IILFGHDHRR PIGKCIDLNP TEMGLEIECE INESSDPAIF SLIKNGVLKT
     FSIGFRCLDA EWDEATDIFI IKDLELYEVS VVSVPCNQDS TFNLAKSMNG HDYTEWRKSF
     TAISSKAVPA QERNLSELEK LAIALGYVKE