ID   LYS3_CRAVI              Reviewed;         187 AA.
AC   B3A003; P85518;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   22-JUL-2008, sequence version 1.
DT   03-AUG-2022, entry version 33.
DE   RecName: Full=Lysozyme 3 {ECO:0000312|EMBL:BAG41979.1};
DE            EC=3.2.1.17 {ECO:0000269|PubMed:20633278};
DE   AltName: Full=1,4-beta-N-acetylmuramidase 3 {ECO:0000305};
DE   AltName: Full=Invertebrate-type lysozyme 3 {ECO:0000305};
DE   AltName: Full=cv-lysozyme 3 {ECO:0000303|PubMed:20633278};
DE   Flags: Precursor;
GN   Name=lysoz3 {ECO:0000312|EMBL:BAG41979.1};
OS   Crassostrea virginica (Eastern oyster).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Bivalvia;
OC   Autobranchia; Pteriomorphia; Ostreida; Ostreoidea; Ostreidae; Crassostrea.
OX   NCBI_TaxID=6565;
RN   [1] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 19-53 AND 55-186, FUNCTION,
RP   CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY, AND
RP   MASS SPECTROMETRY.
RX   PubMed=20633278; DOI=10.1186/1471-2148-10-213;
RA   Xue Q., Hellberg M.E., Schey K.L., Itoh N., Eytan R.I., Cooper R.K.,
RA   La Peyre J.F.;
RT   "A new lysozyme from the eastern oyster, Crassostrea virginica, and a
RT   possible evolutionary pathway for i-type lysozymes in bivalves from host
RT   defense to digestion.";
RL   BMC Evol. Biol. 10:213-213(2010).
CC   -!- FUNCTION: Has antibacterial activity against the Gram-negative
CC       bacterium E.coli. No antibacterial activity detected against the Gram-
CC       negative bacterium V.vulnificus. {ECO:0000269|PubMed:20633278}.
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:0000269|PubMed:20633278};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 7.5-8.5. {ECO:0000269|PubMed:20633278};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P83673}.
CC   -!- TISSUE SPECIFICITY: Highest levels of expression detected in the
CC       digestive glands. Lower levels in the mantle, labial palps, gills and
CC       style-midgut sac, and lowest levels detected in the hemocytes. Not
CC       detected in the gonads. {ECO:0000269|PubMed:20633278}.
CC   -!- MASS SPECTROMETRY: Mass=17782.3; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:20633278};
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; AB427186; BAG41979.1; -; mRNA.
DR   AlphaFoldDB; B3A003; -.
DR   SMR; B3A003; -.
DR   CAZy; GH22; Glycoside Hydrolase Family 22.
DR   Proteomes; UP000694844; Genome assembly.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0003796; F:lysozyme activity; IDA:UniProtKB.
DR   GO; GO:0019835; P:cytolysis; IEA:UniProtKB-KW.
DR   GO; GO:0050829; P:defense response to Gram-negative bacterium; IDA:UniProtKB.
DR   GO; GO:0008152; P:metabolic process; IEA:UniProtKB-KW.
DR   CDD; cd16890; lyz_i; 1.
DR   InterPro; IPR008597; Invert_lysozyme.
DR   InterPro; IPR023346; Lysozyme-like_dom_sf.
DR   PANTHER; PTHR11195; PTHR11195; 1.
DR   Pfam; PF05497; Destabilase; 1.
DR   SUPFAM; SSF53955; SSF53955; 1.
DR   PROSITE; PS51909; LYSOZYME_I; 1.
PE   1: Evidence at protein level;
KW   Antibiotic; Antimicrobial; Bacteriolytic enzyme; Direct protein sequencing;
KW   Disulfide bond; Glycosidase; Hydrolase; Reference proteome; Secreted;
KW   Signal.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000269|PubMed:20633278"
FT   CHAIN           19..187
FT                   /note="Lysozyme 3"
FT                   /evidence="ECO:0000269|PubMed:20633278"
FT                   /id="PRO_0000374069"
FT   DOMAIN          68..183
FT                   /note="I-type lysozyme"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01257"
FT   ACT_SITE        83
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01257"
FT   ACT_SITE        94
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01257"
FT   BINDING         106..112
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q8IU26"
FT   BINDING         137
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q8IU26"
FT   BINDING         158..160
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q8IU26"
FT   DISULFID        75..151
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01257"
FT   DISULFID        80..86
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01257"
FT   DISULFID        91..100
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01257"
FT   DISULFID        113..133
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01257"
FT   DISULFID        123..129
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01257"
FT   DISULFID        147..165
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01257"
SQ   SEQUENCE   187 AA;  19775 MW;  688F67BD2DB2B2A5 CRC64;
     MNGLFLFCVA TTAALAYGSD APCTNSGGVC QDDHLACHNG HYQSGLCTGG AHRRCCLTSA
     SHTGSFSTGI VSQQCLQCIC NVESGCKAIG CHFDVNSDSC GYFQIKEGYW HDCGSPGSSW
     RSCANDLACA SKCVQAYMSR YIGFSGCSHS CESYARIHNG GPAGCKHTNT LGYWSHVHAQ
     GCSHNSK