ID   LYS2_CRAVI              Reviewed;         135 AA.
AC   Q1XG90;
DT   20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   02-MAY-2006, sequence version 1.
DT   13-SEP-2023, entry version 49.
DE   RecName: Full=Lysozyme 2;
DE            EC=3.2.1.17 {ECO:0000269|PubMed:17160350};
DE   AltName: Full=1,4-beta-N-acetylmuramidase 2;
DE   AltName: Full=Invertebrate-type lysozyme 2 {ECO:0000305};
DE   AltName: Full=cv-lysozyme 2;
DE   Flags: Precursor;
GN   Name=lysoz2 {ECO:0000312|EMBL:BAE93114.1};
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, ECO:0000312|EMBL:BAE93114.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 19-105 AND 116-135,
RP   FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP   PROPERTIES, TISSUE SPECIFICITY, AND MASS SPECTROMETRY.
RC   TISSUE=Digestive gland {ECO:0000312|EMBL:BAE93114.1};
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: The main role of this lysozyme is in digestion. Has
CC       antibacterial activity against the Gram-positive bacterium P.cerevisiae
CC       and the Gram-negative bacteria E.coli and V.vulnificus. Shows some
CC       chitinase activity but no isopeptidase activity.
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:17160350};
CC   -!- ACTIVITY REGULATION: Activity decreased by 80% by addition of 0.01 M
CC       calcium, zinc or magnesium. Activity only decreased by 17% by addition
CC       of ammonium, and by 2% by addition of sodium.
CC       {ECO:0000269|PubMed:17160350}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Retains more than 90% of its maximum activity between pH 5.4 and 6.4
CC         in the ionic strength range of I=0.005-0.01. In buffers of I=0.005
CC         more than 75% of maximum activity is retained between pH 5.3 and 7.5.
CC         In buffers of I=0.02 more than 75% of maximum activity is retained
CC         between pH 5.3 and 6.5. {ECO:0000269|PubMed:17160350};
CC       Temperature dependence:
CC         Optimum temperature is 55 degrees Celsius. No decrease in activity
CC         was detected after incubation at 30 degrees Celsius for 30 minutes.
CC         No activity could be detected after incubation at 90 degrees Celsius
CC         for 30 minutes or 100 degrees Celsius for 10 minutes.
CC         {ECO:0000269|PubMed:17160350};
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed in the epithelia of the basophil cells in
CC       the digestive tubules, but not in the epithelial cells lining the
CC       digestive ducts and stomach. Expressed at a much lower level in the
CC       style sac-midgut tissues. No expression detected in mantle, gills,
CC       labial palps or hemocytes. {ECO:0000269|PubMed:17160350}.
CC   -!- MASS SPECTROMETRY: Mass=12984.6; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:17160350};
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; AB252064; BAE93114.1; -; mRNA.
DR   AlphaFoldDB; Q1XG90; -.
DR   SMR; Q1XG90; -.
DR   CAZy; GH22; Glycoside Hydrolase Family 22.
DR   EnsemblMetazoa; XM_022488230.1; XP_022343938.1; LOC111137008.
DR   OrthoDB; 3019454at2759; -.
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:0051838; P:cytolysis by host of symbiont cells; IDA:UniProtKB.
DR   GO; GO:0042742; P:defense response to bacterium; 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   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:17160350"
FT   CHAIN           19..135
FT                   /note="Lysozyme 2"
FT                   /evidence="ECO:0000269|PubMed:17160350"
FT                   /id="PRO_0000280510"
FT   DOMAIN          19..135
FT                   /note="I-type lysozyme"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01257"
FT   ACT_SITE        32
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01257"
FT   ACT_SITE        43
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01257"
FT   BINDING         55..61
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q8IU26"
FT   BINDING         86
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q8IU26"
FT   BINDING         107..109
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q8IU26"
FT   DISULFID        24..100
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01257"
FT   DISULFID        29..35
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01257"
FT   DISULFID        40..49
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01257"
FT   DISULFID        62..82
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01257"
FT   DISULFID        72..78
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01257"
FT   DISULFID        96..114
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01257"
SQ   SEQUENCE   135 AA;  14950 MW;  20465553F0D0D1BB CRC64;
     MNFLILFCVV ASASVVYSSI SDQCLRCICE VESGCRAIGC HWDVYSNSCG YFQIKQGYWT
     DCGSPGHSME SCADNYNCAS GCVRSYMDHY IKYNGCADTC ESYARMHNGG PNGCKSSHHH
     ATDNYWRLVQ AKGCS
//