ID   LYS1_CRAVI              Reviewed;         184 AA.
AC   P83673; Q33DU2;
DT   13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   20-MAR-2007, sequence version 3.
DT   03-MAY-2023, entry version 63.
DE   RecName: Full=Lysozyme 1;
DE            EC=3.2.1.17 {ECO:0000269|PubMed:15364284};
DE   AltName: Full=1,4-beta-N-acetylmuramidase 1;
DE   AltName: Full=Invertebrate-type lysozyme 1 {ECO:0000305};
DE   AltName: Full=cv-lysozyme 1;
DE   Flags: Precursor;
GN   Name=lysoz1 {ECO:0000303|PubMed:17160350};
GN   Synonyms=lysoz {ECO:0000312|EMBL:BAE47520.1};
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].
RA   Itoh N., Xue Q.-G., Cooper R.K., La Peyre J.F.;
RT   "Lysozyme gene in the eastern oyster, Crassostrea virginica.";
RL   Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000305}
RP   PROTEIN SEQUENCE OF 21-85; 109-141; 146-157 AND 168-176, FUNCTION,
RP   CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION,
RP   AND MASS SPECTROMETRY.
RC   TISSUE=Hemolymph {ECO:0000269|PubMed:15364284};
RX   PubMed=15364284; DOI=10.1016/j.cbpc.2004.05.011;
RA   Xue Q.-G., Schey K.L., Volety A.K., Chu F.-L., La Peyre J.F.;
RT   "Purification and characterization of lysozyme from plasma of the eastern
RT   oyster (Crassostrea virginica).";
RL   Comp. Biochem. Physiol. 139B:11-25(2004).
RN   [3] {ECO:0000305}
RP   FUNCTION, AND TISSUE SPECIFICITY.
RX   PubMed=17160350; DOI=10.1007/s00018-006-6386-y;
RA   Xue Q.-G., Itoh N., Schey K.L., Li Y.-L., Cooper R.K., La Peyre J.F.;
RT   "A new lysozyme from the eastern oyster (Crassostrea virginica) indicates
RT   adaptive evolution of i-type lysozymes.";
RL   Cell. Mol. Life Sci. 64:82-95(2007).
CC   -!- FUNCTION: Has antibacterial activity against the Gram-positive bacteria
CC       L.garvieae, M.luteus and Enterococcus sp., and the Gram-negative
CC       bacteria E.coli and V.vulnificus. Weak antibacterial activity against
CC       the Gram-negative bacterium A.hydrophila. No antibacterial activity
CC       detected against the Gram-positive bacterium S.iniae or against the
CC       Gram-negative bacterium E.ictaluri. Shows some chitinase activity but
CC       no isopeptidase activity. {ECO:0000269|PubMed:15364284,
CC       ECO:0000269|PubMed:17160350}.
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:15364284};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 5.5-6.0. {ECO:0000269|PubMed:15364284};
CC       Temperature dependence:
CC         Activity increases as temperature increases from 0 to 45 degrees
CC         Celsius and decreases markedly at temperatures greater than 55
CC         degrees Celsius. {ECO:0000269|PubMed:15364284};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:15364284}.
CC   -!- TISSUE SPECIFICITY: Hemolymph, labial palps, non-vesiculated cells of
CC       mantle connective tissue, cells of interlamellar junctions and
CC       epithelia surrounding the water tubes of the gills.
CC       {ECO:0000269|PubMed:17160350}.
CC   -!- MASS SPECTROMETRY: Mass=17771; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:15364284};
CC   -!- MASS SPECTROMETRY: Mass=17861; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:15364284};
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; AB206328; BAE47520.1; -; mRNA.
DR   AlphaFoldDB; P83673; -.
DR   SMR; P83673; -.
DR   CAZy; GH22; Glycoside Hydrolase Family 22.
DR   Proteomes; UP000694844; Genome assembly.
DR   GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR   GO; GO:0003796; F:lysozyme activity; IDA:UniProtKB.
DR   GO; GO:0050829; P:defense response to Gram-negative bacterium; IDA:UniProtKB.
DR   GO; GO:0050830; P:defense response to Gram-positive bacterium; IDA:UniProtKB.
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; cd16890; lyz_i; 1.
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   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..20
FT                   /evidence="ECO:0000269|PubMed:15364284"
FT   CHAIN           21..184
FT                   /note="Lysozyme 1"
FT                   /evidence="ECO:0000269|PubMed:15364284"
FT                   /id="PRO_0000084532"
FT   DOMAIN          69..184
FT                   /note="I-type lysozyme"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01257"
FT   ACT_SITE        84
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01257"
FT   ACT_SITE        95
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01257"
FT   BINDING         107..113
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q8IU26"
FT   BINDING         138
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q8IU26"
FT   BINDING         159..161
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q8IU26"
FT   DISULFID        76..152
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01257"
FT   DISULFID        81..87
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01257"
FT   DISULFID        92..101
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01257"
FT   DISULFID        114..134
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01257"
FT   DISULFID        124..130
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01257"
FT   DISULFID        148..166
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01257"
FT   CONFLICT        43
FT                   /note="Y -> T (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        75
FT                   /note="Q -> K (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        122
FT                   /note="Q -> K (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        128
FT                   /note="L -> I (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   184 AA;  19986 MW;  239FC8C991546523 CRC64;
     MNGLILFCAV VFATAVCTYG SDAPCLRAGG RCQHDSITCS GRYRTGLCSG GVRRRCCVPS
     SSNSGSFSTG MVSQQCLRCI CNVESGCRPI GCHWDVNSDS CGYFQIKRAY WIDCGSPGGD
     WQTCANNLAC SSRCVQAYMA RYHRRSGCSN SCESFARIHN GGPRGCRNSN TEGYWRRVQA
     QGCN
//