ID   TIPK_LAMBD              Reviewed;         199 AA.
AC   P03729;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   03-AUG-2022, entry version 82.
DE   RecName: Full=Tail tip assembly protein K;
DE   AltName: Full=Probable endopeptidase;
DE            EC=3.4.-.-;
DE   AltName: Full=Tail assembly protein K;
GN   Name=K; OrderedLocusNames=lambdap19;
OS   Escherichia phage lambda (Bacteriophage lambda).
OC   Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC   Caudovirales; Siphoviridae; Lambdavirus.
OX   NCBI_TaxID=10710;
OH   NCBI_TaxID=562; Escherichia coli.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=6221115; DOI=10.1016/0022-2836(82)90546-0;
RA   Sanger F., Coulson A.R., Hong G.F., Hill D.F., Petersen G.B.;
RT   "Nucleotide sequence of bacteriophage lambda DNA.";
RL   J. Mol. Biol. 162:729-773(1982).
RN   [2]
RP   FUNCTION.
RX   PubMed=1003470; DOI=10.1016/s0022-2836(76)80007-1;
RA   Katsura I.;
RT   "Morphogenesis of bacteriophage lambda tail. Polymorphism in the assembly
RT   of the major tail protein.";
RL   J. Mol. Biol. 107:307-326(1976).
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:0000269|PubMed:1003470}.
CC   -!- SUBCELLULAR LOCATION: Host cytoplasm.
CC   -!- SIMILARITY: Belongs to the peptidase C40 family. {ECO:0000255|PROSITE-
CC       ProRule:PRU01284, ECO:0000305}.
CC   -!- CAUTION: It is uncertain whether Met-1 or Met-11 is the initiator.
CC       {ECO:0000305}.
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DR   EMBL; J02459; AAA96551.1; -; Genomic_DNA.
DR   PIR; H43009; TJBPKL.
DR   RefSeq; NP_040598.1; NC_001416.1.
DR   SMR; P03729; -.
DR   IntAct; P03729; 2.
DR   GeneID; 2703514; -.
DR   KEGG; vg:2703514; -.
DR   Proteomes; UP000001711; 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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   GO; GO:0098003; P:viral tail assembly; IEA:UniProtKB-KW.
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   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..199
FT                   /note="Tail tip assembly protein K"
FT                   /id="PRO_0000109872"
FT   DOMAIN          1..77
FT                   /note="MPN"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT   DOMAIN          40..186
FT                   /note="NlpC/P60"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01284"
FT   MOTIF           20..33
FT                   /note="JAMM motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT   ACT_SITE        73
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01284"
FT   ACT_SITE        139
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01284"
FT   ACT_SITE        151
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01284"
FT   BINDING         20
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT   BINDING         22
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT   BINDING         33
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
SQ   SEQUENCE   199 AA;  23011 MW;  CEEB88F01E31ABAE CRC64;
     MSPEDWLQAE MQGEIVALVH SHPGGLPWLS EADRRLQVQS DLPWWLVCRG TIHKFRCVPH
     LTGRRFEHGV TDCYTLFRDA YHLAGIEMPD FHREDDWWRN GQNLYLDNLE ATGLYQVPLS
     AAQPGDVLLC CFGSSVPNHA AIYCGDGELL HHIPEQLSKR ERYTDKWQRR THSLWRHRAW
     RASAFTGIYN DLVAASTFV