ID   LYS_OSTED               Reviewed;         137 AA.
AC   Q6L6Q5;
DT   20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-MAY-2023, entry version 57.
DE   RecName: Full=Lysozyme;
DE            EC=3.2.1.17 {ECO:0000250|UniProtKB:Q8IU26};
DE   AltName: Full=1,4-beta-N-acetylmuramidase;
DE   AltName: Full=Invertebrate-type lysozyme {ECO:0000305};
DE   Flags: Precursor;
GN   Name=lysoz;
OS   Ostrea edulis (Native oyster) (European flat oyster).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Bivalvia;
OC   Autobranchia; Pteriomorphia; Ostreida; Ostreoidea; Ostreidae; Ostrea.
OX   NCBI_TaxID=37623;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=16996284; DOI=10.1016/j.cbpb.2006.08.003;
RA   Matsumoto T., Nakamura A.M., Takahashi K.G.;
RT   "Cloning of cDNAs and hybridization analysis of lysozymes from two oyster
RT   species, Crassostrea gigas and Ostrea edulis.";
RL   Comp. Biochem. Physiol. 145B:325-330(2006).
CC   -!- FUNCTION: Has bacteriolytic activity (By similarity). May play a role
CC       in digestion and in the host defense mechanisms against invading
CC       microbes (PubMed:16996284). {ECO:0000250|UniProtKB:Q8IU26,
CC       ECO:0000303|PubMed:16996284}.
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:0000250|UniProtKB:Q8IU26};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P83673}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 22 family. Type-I
CC       lysozyme subfamily. {ECO:0000255|PROSITE-ProRule:PRU01257}.
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DR   EMBL; AB179776; BAD19060.1; -; mRNA.
DR   AlphaFoldDB; Q6L6Q5; -.
DR   SMR; Q6L6Q5; -.
DR   CAZy; GH22; Glycoside Hydrolase Family 22.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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   Gene3D; 1.10.530.10; -; 1.
DR   InterPro; IPR008597; Invert_lysozyme.
DR   InterPro; IPR023346; Lysozyme-like_dom_sf.
DR   PANTHER; PTHR11195; DESTABILASE-RELATED; 1.
DR   PANTHER; PTHR11195:SF13; INVERTEBRATE-TYPE LYSOZYME 2-RELATED; 1.
DR   Pfam; PF05497; Destabilase; 1.
DR   SUPFAM; SSF53955; Lysozyme-like; 1.
DR   PROSITE; PS51909; LYSOZYME_I; 1.
PE   2: Evidence at transcript level;
KW   Antibiotic; Antimicrobial; Bacteriolytic enzyme; Disulfide bond;
KW   Glycosidase; Hydrolase; Secreted; Signal.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..137
FT                   /note="Lysozyme"
FT                   /id="PRO_0000280512"
FT   DOMAIN          21..134
FT                   /note="I-type lysozyme"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01257"
FT   ACT_SITE        33
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01257"
FT   ACT_SITE        45
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01257"
FT   BINDING         57..63
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q8IU26"
FT   BINDING         88
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q8IU26"
FT   BINDING         109..111
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q8IU26"
FT   DISULFID        25..102
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01257"
FT   DISULFID        30..37
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01257"
FT   DISULFID        42..51
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01257"
FT   DISULFID        64..84
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01257"
FT   DISULFID        74..80
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01257"
FT   DISULFID        98..116
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01257"
SQ   SEQUENCE   137 AA;  14918 MW;  5E267529DE695722 CRC64;
     MSAVLVLALV LLSLTCVTDA ISDACLTCIC KQESYGCTQI GCRMDGRSLS CGYFQIKKSY
     WIDCGRLGSS WEACADDYNC AVRCVRAYMK KYIGKSGCTA NCKNYARLHN GGPKGCTKPS
     TLTYWNAVKN QGCSINS
//