ID   ENLYS_BPLC2             Reviewed;         226 AA.
AC   P62692; P13003; Q38298; Q38562; Q38651;
DT   19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   08-NOV-2023, entry version 77.
DE   RecName: Full=Endolysin {ECO:0000255|HAMAP-Rule:MF_04110};
DE            EC=3.2.1.17 {ECO:0000255|HAMAP-Rule:MF_04110};
DE   AltName: Full=Lysis protein {ECO:0000255|HAMAP-Rule:MF_04110};
DE   AltName: Full=Lysozyme {ECO:0000255|HAMAP-Rule:MF_04110};
DE   AltName: Full=Muramidase {ECO:0000255|HAMAP-Rule:MF_04110};
GN   Name=L3;
OS   Lactococcus phage c2.
OC   Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC   Ceduovirus; Ceduovirus c2.
OX   NCBI_TaxID=2681624;
OH   NCBI_TaxID=1357; Lactococcus (lactic streptococci).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8221377; DOI=10.1139/m93-113;
RA   Ward L.J., Beresford T.P., Lubbers M.W., Jarvis B.D., Jarvis A.W.;
RT   "Sequence analysis of the lysin gene region of the prolate lactococcal
RT   bacteriophage c2.";
RL   Can. J. Microbiol. 39:767-774(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8534101; DOI=10.1128/aem.61.12.4348-4356.1995;
RA   Lubbers M.W., Waterfield N.R., Beresford T.P., Le Page R.W., Jarvis A.W.;
RT   "Sequencing and analysis of the prolate-headed lactococcal bacteriophage c2
RT   genome and identification of the structural genes.";
RL   Appl. Environ. Microbiol. 61:4348-4356(1995).
CC   -!- FUNCTION: Endolysin with lysozyme 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_04110}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of (1->4)-beta-linkages between N-acetylmuramic
CC         acid and N-acetyl-D-glucosamine residues in a peptidoglycan and
CC         between N-acetyl-D-glucosamine residues in chitodextrins.;
CC         EC=3.2.1.17; Evidence={ECO:0000255|HAMAP-Rule:MF_04110};
CC   -!- SUBCELLULAR LOCATION: Host cytoplasm {ECO:0000255|HAMAP-Rule:MF_04110}.
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_04110}.
CC   -!- MISCELLANEOUS: The bacteriophage lysin is a powerful lytic agent with a
CC       narrow target specifically for dairy lactic streptococci.
CC       {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 24 family.
CC       {ECO:0000255|HAMAP-Rule:MF_04110}.
CC   -!- CAUTION: Lacks the conserved Asp active site. {ECO:0000255|HAMAP-
CC       Rule:MF_04110}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA84289.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; Z34528; CAA84289.1; ALT_INIT; Genomic_DNA.
DR   EMBL; L48605; AAA92182.1; -; Genomic_DNA.
DR   PIR; S49014; S49014.
DR   RefSeq; NP_043551.1; NC_001706.1.
DR   SMR; P62692; -.
DR   CAZy; GH24; Glycoside Hydrolase Family 24.
DR   GeneID; 1261153; -.
DR   KEGG; vg:1261153; -.
DR   OrthoDB; 6670at10239; -.
DR   Proteomes; UP000001835; Genome.
DR   GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
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: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   CDD; cd00737; lyz_endolysin_autolysin; 1.
DR   Gene3D; 1.10.530.40; -; 1.
DR   HAMAP; MF_04110; ENDOLYSIN_T4; 1.
DR   InterPro; IPR033907; Endolysin_autolysin.
DR   InterPro; IPR034690; Endolysin_T4_type.
DR   InterPro; IPR002196; Glyco_hydro_24.
DR   InterPro; IPR023346; Lysozyme-like_dom_sf.
DR   InterPro; IPR023347; Lysozyme_dom_sf.
DR   PANTHER; PTHR38107; -; 1.
DR   PANTHER; PTHR38107:SF3; LYSOZYME RRRD-RELATED; 1.
DR   Pfam; PF00959; Phage_lysozyme; 1.
DR   SUPFAM; SSF53955; Lysozyme-like; 1.
PE   3: Inferred from homology;
KW   Antimicrobial; Bacteriolytic enzyme; Cytolysis; Glycosidase;
KW   Host cell lysis by virus; Host cytoplasm; Hydrolase; Reference proteome;
KW   Viral release from host cell.
FT   CHAIN           1..226
FT                   /note="Endolysin"
FT                   /id="PRO_0000218094"
FT   ACT_SITE        15
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04110"
SQ   SEQUENCE   226 AA;  25370 MW;  30EDC142BE07B0DE CRC64;
     MKVSQNGLNL IKEFEGCRLT AYKPVPWEQM YTIGWGHYGV TAGTTWTQAQ ADSQLEIDIN
     NKYAPMVDAY VKGKANQNEF DALVSLAYNC GNVFVADGWA PFSHAYCASM IPKYRNAGGQ
     VLQGLVRRRQ AELNLFNKPV SSNSNQNNQT GGMIKMYLII GLDNSGKAKH WYVSDGVSVR
     HVRTIRMLEN YQNKWAKLNL PVDTMFIAEI EAEFGRKIDM ASGEVK
//