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   16-JUN-2009, entry version 16.
DE   RecName: Full=Lysozyme 2;
DE            EC=3.2.1.17;
DE   AltName: Full=1,4-beta-N-acetylmuramidase 2;
DE   AltName: Full=cv-lysozyme 2;
DE   Flags: Precursor;
GN   Name=lysoz2;
OS   Crassostrea virginica (Eastern oyster).
OC   Eukaryota; Metazoa; Mollusca; Bivalvia; Pteriomorphia; Ostreoida;
OC   Ostreoidea; Ostreidae; Crassostrea.
OX   NCBI_TaxID=6565;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 19-105 AND 116-135,
RP   FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, BIOPHYSICOCHEMICAL
RP   PROPERTIES, TISSUE SPECIFICITY, AND MASS SPECTROMETRY.
RC   TISSUE=Digestive gland;
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)
RT   indicates 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
CC       P.cerevisiae and the Gram-negative bacteria E.coli and
CC       V.vulnificus. Shows some chitinase activity but no isopeptidase
CC       activity.
CC   -!- CATALYTIC ACTIVITY: Hydrolysis of (1->4)-beta-linkages between N-
CC       acetylmuramic acid and N-acetyl-D-glucosamine residues in a
CC       peptidoglycan and between N-acetyl-D-glucosamine residues in
CC       chitodextrins.
CC   -!- ENZYME REGULATION: Activity decreased by 80% by addition of 0.01 M
CC       calcium, zinc or magnesium. Activity only decreased by 17% by
CC       addition of ammonium, and by 2% by addition of sodium.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Retains more than 90% of its maximum activity between pH 5.4 and
CC         6.4 in the ionic strength range of I=0.005-0.01. In buffers of
CC         I=0.005 more than 75% of maximum activity is retained between pH
CC         5.3 and 7.5. In buffers of I=0.02 more than 75% of maximum
CC         activity is retained between pH 5.3 and 6.5;
CC       Temperature dependence:
CC         Optimum temperature is 55 degrees Celsius. No decrease in
CC         activity was detected after incubation at 30 degrees Celsius for
CC         30 minutes. No activity could be detected after incubation at 90
CC         degrees Celsius for 30 minutes or 100 degrees Celsius for 10
CC         minutes;
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed in the epithelia of the basophil
CC       cells in the digestive tubules, but not in the epithelial cells
CC       lining the digestive ducts and stomach. Expressed at a much lower
CC       level in the style sac-midgut tissues. No expression detected in
CC       mantle, gills, labial palps or hemocytes.
CC   -!- MASS SPECTROMETRY: Mass=12984.6; Method=MALDI; Range=19-135;
CC       Source=PubMed:17160350;
CC   -!- SIMILARITY: Belongs to the lysozyme type I family.
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DR   EMBL; AB252064; BAE93114.1; -; mRNA.
DR   CAZy; GH22; Glycoside Hydrolase Family 22.
DR   BRENDA; 3.2.1.17; 141032.
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; 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   InterPro; IPR008597; Destabilase.
DR   PANTHER; PTHR11195; Destabilase; 1.
DR   Pfam; PF05497; Destabilase; 1.
PE   1: Evidence at protein level;
KW   Antibiotic; Antimicrobial; Bacteriolytic enzyme;
KW   Direct protein sequencing; Glycosidase; Hydrolase; Secreted; Signal.
FT   SIGNAL        1     18
FT   CHAIN        19    135       Lysozyme 2.
FT                                /FTId=PRO_0000280510.
SQ   SEQUENCE   135 AA;  14950 MW;  20465553F0D0D1BB CRC64;
     MNFLILFCVV ASASVVYSSI SDQCLRCICE VESGCRAIGC HWDVYSNSCG YFQIKQGYWT
     DCGSPGHSME SCADNYNCAS GCVRSYMDHY IKYNGCADTC ESYARMHNGG PNGCKSSHHH
     ATDNYWRLVQ AKGCS
//