ID   LYS_BPMV1               Reviewed;         202 AA.
AC   P33486;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2000, sequence version 3.
DT   02-SEP-2026, entry version 90.
DE   RecName: Full=Lysozyme;
DE            EC=3.2.1.17;
DE   AltName: Full=Endolysin;
DE   AltName: Full=MV1 lysin;
DE   AltName: Full=Muramidase;
GN   Name=lysA;
OS   Lactococcus phage mv1 (Lactococcus delbrueckii bacteriophage mv1).
OC   Viruses.
OX   NCBI_TaxID=33769;
OH   NCBI_TaxID=1584; Lactobacillus delbrueckii.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RX   PubMed=2227453; DOI=10.1016/0378-1119(90)90468-7;
RA   Boizet B., Lahbib-Mansais Y., Dupont L., Ritzenthaler P., Mata M.;
RT   "Cloning, expression and sequence analysis of an endolysin-encoding gene of
RT   Lactobacillus bulgaricus bacteriophage mv1.";
RL   Gene 94:61-67(1990).
RN   [2]
RP   SEQUENCE REVISION TO C-TERMINUS.
RA   Boizet B., Lahbib-Mansais Y., Dupont L., Ritzenthaler P., Mata M.;
RL   Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Helps to release the mature phage particles from the cell
CC       wall by breaking down the peptidoglycan.
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;
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 25 family. {ECO:0000305}.
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DR   EMBL; M60167; AAA32264.1; -; Genomic_DNA.
DR   PIR; JQ0789; MUBPM1.
DR   SMR; P33486; -.
DR   CAZy; GH25; Glycoside Hydrolase Family 25.
DR   GO; GO:0003796; F:lysozyme activity; IEA:UniProtKB-EC.
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:0031640; P:killing of cells of another organism; IEA:UniProtKB-KW.
DR   GO; GO:0009253; P:peptidoglycan catabolic process; IEA:InterPro.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   InterPro; IPR017853; GH_hydrolase_sf.
DR   InterPro; IPR002053; Glyco_hydro_25.
DR   InterPro; IPR008270; Glyco_hydro_25_AS.
DR   InterPro; IPR018077; Glyco_hydro_fam25_subgr.
DR   PANTHER; PTHR34135; LYSOZYME; 1.
DR   PANTHER; PTHR34135:SF2; LYSOZYME; 1.
DR   Pfam; PF01183; Glyco_hydro_25; 1.
DR   SMART; SM00641; Glyco_25; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   PROSITE; PS00953; GLYCOSYL_HYDROL_F25_1; 1.
DR   PROSITE; PS51904; GLYCOSYL_HYDROL_F25_2; 1.
PE   1: Evidence at protein level;
KW   Antimicrobial; Bacteriolytic enzyme; Direct protein sequencing;
KW   Glycosidase; Hydrolase.
FT   CHAIN           1..202
FT                   /note="Lysozyme"
FT                   /id="PRO_0000208262"
FT   ACT_SITE        8
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10065"
FT   ACT_SITE        99
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10065"
SQ   SEQUENCE   202 AA;  21985 MW;  F40F125D936D6E8B CRC64;
     MTKTYGVDVA VYQPIDLAAY HKAGASFAIV KLTEGVDYVN RRGPSRWTAP GLTTSTLMPT
     ISRSFGSSVS RAKKEAAYFL KEAKKQDISK KRMLWLDWEA GSGNVVTGSK SSNTAAILDF
     MDAIKAAGWR PGLYSGASLM RTAIDTKQVV KKYGTCLWVA SYPTMAAVST ADFGYFRQWT
     GSPSGSLPVT AWPGRRRERC SG
//