ID   LYS4_ENTHI              Reviewed;         198 AA.
AC   Q27650;
DT   15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 2.
DT   25-MAY-2022, entry version 76.
DE   RecName: Full=Lysozyme;
DE            EC=3.2.1.17;
DE   AltName: Full=1,4-beta-N-acetylmuramidase;
GN   Name=LYS4;
OS   Entamoeba histolytica.
OC   Eukaryota; Amoebozoa; Evosea; Archamoebae; Mastigamoebida; Entamoebidae;
OC   Entamoeba.
OX   NCBI_TaxID=5759;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 26-198, AND PROTEIN SEQUENCE OF 1-47; 133-144
RP   AND 180-197.
RC   STRAIN=ATCC 30459 / HM-1:IMSS;
RX   PubMed=7649184; DOI=10.1111/j.1432-1033.1995.0831d.x;
RA   Jacobs T., Leippe M.;
RT   "Purification and molecular cloning of a major antibacterial protein of the
RT   protozoan parasite Entamoeba histolytica with lysozyme-like properties.";
RL   Eur. J. Biochem. 231:831-838(1995).
CC   -!- FUNCTION: Has antibacterial activity against Gram-positive bacteria. No
CC       activity against S.aureus.
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   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimally active at acid pH.;
CC   -!- SUBCELLULAR LOCATION: Cytoplasmic granule.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 25 family.
CC       {ECO:0000255|PROSITE-ProRule:PRU01252, ECO:0000305}.
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DR   EMBL; X87610; CAA60916.1; -; mRNA.
DR   PIR; S66599; S66599.
DR   AlphaFoldDB; Q27650; -.
DR   SMR; Q27650; -.
DR   VEuPathDB; AmoebaDB:EHI5A_045850; -.
DR   VEuPathDB; AmoebaDB:EHI7A_025140; -.
DR   VEuPathDB; AmoebaDB:EHI8A_022330; -.
DR   VEuPathDB; AmoebaDB:EHI_199110; -.
DR   VEuPathDB; AmoebaDB:KM1_024570; -.
DR   eggNOG; ENOG502S1SN; Eukaryota.
DR   GO; GO:0031410; C:cytoplasmic vesicle; IDA:WormBase.
DR   GO; GO:0003796; F:lysozyme activity; IDA:WormBase.
DR   GO; GO:0016998; P:cell wall macromolecule catabolic process; IEA:InterPro.
DR   GO; GO:0019835; P:cytolysis; IEA:UniProtKB-KW.
DR   GO; GO:0050830; P:defense response to Gram-positive bacterium; IDA:WormBase.
DR   GO; GO:0009253; P:peptidoglycan catabolic process; IDA:WormBase.
DR   InterPro; IPR002053; Glyco_hydro_25.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   Pfam; PF01183; Glyco_hydro_25; 1.
DR   SUPFAM; SSF51445; SSF51445; 1.
DR   PROSITE; PS51904; GLYCOSYL_HYDROL_F25_2; 1.
PE   1: Evidence at protein level;
KW   Antibiotic; Antimicrobial; Bacteriolytic enzyme; Direct protein sequencing;
KW   Glycosidase; Hydrolase.
FT   CHAIN           1..198
FT                   /note="Lysozyme"
FT                   /id="PRO_0000084536"
FT   DOMAIN          1..198
FT                   /note="Ch-type lysozyme"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01252"
FT   ACT_SITE        5
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01252"
FT   ACT_SITE        96
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01252"
FT   ACT_SITE        98
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01252"
FT   UNSURE          17
SQ   SEQUENCE   198 AA;  22379 MW;  1AF3B73CDAEBBCE9 CRC64;
     KLGIDVSQPT STSSFTCLRN KGFTTMVIVR AWKSTGSFDT NAPQTLKNAN AAGFSIENSD
     VYYYPCISCG NMAGQVRTFW QKVGQYSLKV KRVWFDIEGT WTSSVSTNQN YLMQMMNEAR
     AIGIVHGIYG SKYYWGNLFG SSYKYRYRSS TPLWYPHYDN SPSFSDFSSF GGWTSPSMKQ
     YRGDVSVCSA GVDYNYKP