ID   TIPK_BPN15              Reviewed;         243 AA.
AC   O64333;
DT   29-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   03-AUG-2022, entry version 74.
DE   RecName: Full=Tail tip assembly protein K {ECO:0000303|PubMed:10860722};
DE   AltName: Full=Gene product 19 {ECO:0000305};
DE            Short=gp19 {ECO:0000305};
DE   AltName: Full=Probable endopeptidase;
DE            EC=3.4.-.-;
DE   AltName: Full=Tail assembly protein K;
GN   Name=gene 19 {ECO:0000312|EMBL:AAC19055.1};
OS   Escherichia phage N15 (Bacteriophage N15).
OC   Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC   Caudovirales; Siphoviridae; Ravinvirus.
OX   NCBI_TaxID=40631 {ECO:0000312|Proteomes:UP000002132};
OH   NCBI_TaxID=562; Escherichia coli.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND IDENTIFICATION.
RX   PubMed=10860722; DOI=10.1006/jmbi.2000.3731;
RA   Ravin V., Ravin N., Casjens S., Ford M.E., Hatfull G.F., Hendrix R.W.;
RT   "Genomic sequence and analysis of the atypical temperate bacteriophage
RT   N15.";
RL   J. Mol. Biol. 299:53-73(2000).
CC   -!- FUNCTION: Plays a role in tail tip complex assembly. The tail tip
CC       complex is assembled successively with three tail tip proteins J, one
CC       tail tip protein I, one tail tip protein L and one tail tip protein K.
CC       The tail tip complex interacts with tail measure protein to initiate
CC       tail tube assembly. The formation of the tail tip complex is completed
CC       by the addition of tail tip protein M, which is followed by tail tube
CC       polymerization. May be excluded form tail tip during maturation and
CC       would be absent from virions. May be involved in tail measure protein
CC       processing. {ECO:0000250|UniProtKB:P03729}.
CC   -!- SUBCELLULAR LOCATION: Host cytoplasm {ECO:0000250|UniProtKB:P03729}.
CC   -!- SIMILARITY: Belongs to the peptidase C40 family. {ECO:0000255|PROSITE-
CC       ProRule:PRU01284, ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AF064539; AAC19055.1; -; Genomic_DNA.
DR   PIR; T13105; T13105.
DR   RefSeq; NP_046914.1; NC_001901.1.
DR   SMR; O64333; -.
DR   GeneID; 1261658; -.
DR   KEGG; vg:1261658; -.
DR   Proteomes; UP000002132; Genome.
DR   GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008234; F:cysteine-type peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0070122; F:isopeptidase activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0140492; F:metal-dependent deubiquitinase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   GO; GO:0098003; P:viral tail assembly; IEA:UniProtKB-KW.
DR   InterPro; IPR028090; JAB_dom_prok.
DR   InterPro; IPR000555; JAMM/MPN+_dom.
DR   InterPro; IPR037518; MPN.
DR   InterPro; IPR000064; NLP_P60_dom.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   Pfam; PF00877; NLPC_P60; 1.
DR   Pfam; PF14464; Prok-JAB; 1.
DR   SMART; SM00232; JAB_MPN; 1.
DR   SUPFAM; SSF54001; SSF54001; 1.
DR   PROSITE; PS50249; MPN; 1.
DR   PROSITE; PS51935; NLPC_P60; 1.
PE   3: Inferred from homology;
KW   Host cytoplasm; Hydrolase; Late protein; Metal-binding; Metalloprotease;
KW   Protease; Reference proteome; Thiol protease; Viral release from host cell;
KW   Viral tail assembly; Zinc.
FT   CHAIN           1..243
FT                   /note="Tail tip assembly protein K"
FT                   /id="PRO_0000432900"
FT   DOMAIN          1..120
FT                   /note="MPN"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT   DOMAIN          96..233
FT                   /note="NlpC/P60"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01284"
FT   MOTIF           69..82
FT                   /note="JAMM motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT   ACT_SITE        126
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01284"
FT   ACT_SITE        194
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01284"
FT   ACT_SITE        206
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01284"
FT   BINDING         69
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT   BINDING         71
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT   BINDING         82
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
SQ   SEQUENCE   243 AA;  28325 MW;  570ED22D52776FDF CRC64;
     MRQKTIDAIM AHAAAEYPRE CCGVVAQKSR VERYFPCRNL SAEPTEHFHL SPEDYAAAED
     WGTVVAIVHS HPDATTQPSE LDKAQCDATL LPWHIVSWPE GDLRTIQPRG ELPLLERPFV
     LGHFDCWGLV MSYFRQTHGI ELHDYRVDYP WWENSYPDNF YQDCWYECGF REFDGPPQEG
     DLVIMQVQAD KWNHAGILLE GNMLLHHLYG HLSQRVPYGG YWQERTMKIV RYKDVRGNEA
     CRK