LYS2_CRAVI
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 03-AUG-2022, entry version 45.
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 OrthoDB; 1343143at2759; -.
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: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 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: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
