ID   ENLYS_BPP2              Reviewed;         165 AA.
AC   P51771;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   12-AUG-2020, entry version 91.
DE   RecName: Full=Endolysin {ECO:0000255|HAMAP-Rule:MF_04109};
DE            EC=4.2.2.n2 {ECO:0000255|HAMAP-Rule:MF_04109};
DE   AltName: Full=Lysis protein {ECO:0000255|HAMAP-Rule:MF_04109};
DE   AltName: Full=Lysozyme {ECO:0000255|HAMAP-Rule:MF_04109};
DE   AltName: Full=Protein gpK {ECO:0000305};
DE   AltName: Full=Transglycosylase {ECO:0000255|HAMAP-Rule:MF_04109};
GN   Name=K;
OS   Escherichia phage P2 (Bacteriophage P2).
OC   Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC   Caudovirales; Myoviridae; Peduovirinae; Peduovirus.
OX   NCBI_TaxID=10679;
OH   NCBI_TaxID=543; Enterobacteriaceae.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8051010; DOI=10.1128/jb.176.16.4974-4984.1994;
RA   Ziermann R., Bartlett B., Calendar R., Christie G.E.;
RT   "Functions involved in bacteriophage P2-induced host cell lysis and
RT   identification of a new tail gene.";
RL   J. Bacteriol. 176:4974-4984(1994).
CC   -!- FUNCTION: Endolysin with transglycosylase activity that degrades host
CC       peptidoglycans and participates with the holin and spanin proteins in
CC       the sequential events which lead to the programmed host cell lysis
CC       releasing the mature viral particles. Once the holin has permeabilized
CC       the host cell membrane, the endolysin can reach the periplasm and break
CC       down the peptidoglycan layer. {ECO:0000255|HAMAP-Rule:MF_04109}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endolytic cleavage of the (1->4)-beta-glycosidic linkage
CC         between N-acetylmuramic acid (MurNAc) and N-acetylglucosamine
CC         (GlcNAc) residues in peptidoglycan with concomitant formation of a
CC         1,6-anhydrobond in the MurNAc residue.; EC=4.2.2.n2;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_04109};
CC   -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_04109}.
CC   -!- SUBCELLULAR LOCATION: Host cytoplasm {ECO:0000255|HAMAP-Rule:MF_04109}.
CC       Note=The endolysin is cytoplasmic, but can reach the periplasmic space
CC       with the help of the holins which disrupt the host cell membrane.
CC       {ECO:0000255|HAMAP-Rule:MF_04109}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 24 family.
CC       {ECO:0000255|HAMAP-Rule:MF_04109}.
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DR   EMBL; AF063097; AAD03276.1; -; Genomic_DNA.
DR   PIR; D55855; D55855.
DR   RefSeq; NP_046765.1; NC_001895.1.
DR   SMR; P51771; -.
DR   CAZy; GH104; Glycoside Hydrolase Family 104.
DR   GeneID; 1261544; -.
DR   KEGG; vg:1261544; -.
DR   Proteomes; UP000009092; Genome.
DR   GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0003796; F:lysozyme activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0016998; P:cell wall macromolecule catabolic process; IEA:InterPro.
DR   GO; GO:0019835; P:cytolysis; IEA:UniProtKB-KW.
DR   GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR   GO; GO:0009253; P:peptidoglycan catabolic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0044659; P:viral release from host cell by cytolysis; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_04109; ENDOLYSIN_LAMBDA; 1.
DR   InterPro; IPR034691; Endolysin_lambda_type.
DR   InterPro; IPR002196; Glyco_hydro_24.
DR   InterPro; IPR023346; Lysozyme-like_dom_sf.
DR   Pfam; PF00959; Phage_lysozyme; 1.
DR   SUPFAM; SSF53955; SSF53955; 1.
PE   3: Inferred from homology;
KW   Antimicrobial; Bacteriolytic enzyme; Cytolysis; Host cell lysis by virus;
KW   Host cytoplasm; Lyase; Reference proteome; Viral release from host cell.
FT   CHAIN           1..165
FT                   /note="Endolysin"
FT                   /id="PRO_0000218100"
FT   ACT_SITE        21
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04109"
FT   VARIANT         40
FT                   /note="G -> R (in temperature-sensitive KTS60)"
SQ   SEQUENCE   165 AA;  18538 MW;  82388A6A86C2B35E CRC64;
     MPVINTHQNI AAFLDMLAVS EGTANHPLTK NRGYDVIVTG LDGKPEIFTD YSDHPFAHGR
     PAKVFNRRGE KSTASGRYQQ LYLFWPHYRK QLALPDFSPL SQDRLAIQLI RERGALDDIR
     AGRIERAISR CRNIWASLPG AGYGQREHSL EKLVTVWRTA GGVPA