ID   U3L0J0_MYORI            Unreviewed;       148 AA.
AC   U3L0J0;
DT   11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT   11-DEC-2013, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   RecName: Full=lysozyme {ECO:0000256|ARBA:ARBA00012732};
DE            EC=3.2.1.17 {ECO:0000256|ARBA:ARBA00012732};
GN   Name=LYZ {ECO:0000313|EMBL:AFU52824.1};
OS   Myotis ricketti (Rickett's big-footed bat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Vespertilionidae;
OC   Myotis.
OX   NCBI_TaxID=203696 {ECO:0000313|EMBL:AFU52824.1};
RN   [1] {ECO:0000313|EMBL:AFU52824.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Liver {ECO:0000313|EMBL:AFU52824.1};
RX   PubMed=25135943;
RA   Liu Y., He G., Xu H., Han X., Jones G., Rossiter S.J., Zhang S.;
RT   "Adaptive functional diversification of lysozyme in insectivorous bats.";
RL   Mol. Biol. Evol. 31:2829-2835(2014).
CC   -!- FUNCTION: Lysozymes have primarily a bacteriolytic function; those in
CC       tissues and body fluids are associated with the monocyte-macrophage
CC       system and enhance the activity of immunoagents.
CC       {ECO:0000256|ARBA:ARBA00002647}.
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:0000256|ARBA:ARBA00000632};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 22 family.
CC       {ECO:0000256|RuleBase:RU004440}.
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DR   EMBL; JX064177; AFU52824.1; -; mRNA.
DR   AlphaFoldDB; U3L0J0; -.
DR   GO; GO:0003796; F:lysozyme activity; IEA:UniProtKB-EC.
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:0008152; P:metabolic process; IEA:UniProtKB-KW.
DR   CDD; cd16897; LYZ_C; 1.
DR   Gene3D; 1.10.530.10; -; 1.
DR   InterPro; IPR001916; Glyco_hydro_22.
DR   InterPro; IPR019799; Glyco_hydro_22_CS.
DR   InterPro; IPR000974; Glyco_hydro_22_lys.
DR   InterPro; IPR023346; Lysozyme-like_dom_sf.
DR   PANTHER; PTHR11407; LYSOZYME C; 1.
DR   PANTHER; PTHR11407:SF28; LYSOZYME C; 1.
DR   Pfam; PF00062; Lys; 1.
DR   PRINTS; PR00137; LYSOZYME.
DR   PRINTS; PR00135; LYZLACT.
DR   SMART; SM00263; LYZ1; 1.
DR   SUPFAM; SSF53955; Lysozyme-like; 1.
DR   PROSITE; PS00128; GLYCOSYL_HYDROL_F22_1; 1.
DR   PROSITE; PS51348; GLYCOSYL_HYDROL_F22_2; 1.
PE   2: Evidence at transcript level;
KW   Antimicrobial {ECO:0000256|ARBA:ARBA00022529};
KW   Bacteriolytic enzyme {ECO:0000256|ARBA:ARBA00022638};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           19..148
FT                   /note="lysozyme"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004646585"
FT   DOMAIN          95..113
FT                   /note="Glycosyl hydrolases family 22 (GH22)"
FT                   /evidence="ECO:0000259|PROSITE:PS00128"
SQ   SEQUENCE   148 AA;  16480 MW;  21F777C8299670A3 CRC64;
     MKALLTLGLL LLSVAVQAKV YERCDLARTL KRLGMDGHSG VKLADWVCLA KWESSYNTRA
     TNHNRGDKST DYGIFQINSR YWCNDGKTPG AVNACGINCN DLLQDDITKA VTCAKRVVKD
     PQGIKAWVAW RNHCQNKDLT EYTRGCGV
//