LYS1_CRAVI
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-AUG-2022, entry version 59.
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 PRIDE; P83673; -.
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:0019835; P:cytolysis; IEA:UniProtKB-KW.
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: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..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
