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Lysozyme (EC 3.2.1.17) (1,4-beta-N-acetylmuramidase) (Invertebrate-type lysozyme)

 LYS_OSTED               Reviewed;         137 AA.
Q6L6Q5;
20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
05-JUL-2004, sequence version 1.
05-DEC-2018, entry version 42.
RecName: Full=Lysozyme;
EC=3.2.1.17 {ECO:0000250|UniProtKB:Q8IU26};
AltName: Full=1,4-beta-N-acetylmuramidase;
AltName: Full=Invertebrate-type lysozyme {ECO:0000305};
Flags: Precursor;
Name=lysoz;
Ostrea edulis (Native oyster) (European flat oyster).
Eukaryota; Metazoa; Lophotrochozoa; Mollusca; Bivalvia; Pteriomorphia;
Ostreoida; Ostreoidea; Ostreidae; Ostrea.
NCBI_TaxID=37623;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=16996284; DOI=10.1016/j.cbpb.2006.08.003;
Matsumoto T., Nakamura A.M., Takahashi K.G.;
"Cloning of cDNAs and hybridization analysis of lysozymes from two
oyster species, Crassostrea gigas and Ostrea edulis.";
Comp. Biochem. Physiol. 145B:325-330(2006).
-!- FUNCTION: Has bacteriolytic activity (By similarity). May play a
role in digestion and in the host defense mechanisms against
invading microbes (PubMed:16996284).
{ECO:0000250|UniProtKB:Q8IU26, ECO:0000303|PubMed:16996284}.
-!- CATALYTIC ACTIVITY:
Reaction=Hydrolysis of (1->4)-beta-linkages between N-
acetylmuramic acid and N-acetyl-D-glucosamine residues in a
peptidoglycan and between N-acetyl-D-glucosamine residues in
chitodextrins.; EC=3.2.1.17;
Evidence={ECO:0000250|UniProtKB:Q8IU26};
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P83673}.
-!- SIMILARITY: Belongs to the lysozyme type I family. {ECO:0000305}.
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EMBL; AB179776; BAD19060.1; -; mRNA.
ProteinModelPortal; Q6L6Q5; -.
SMR; Q6L6Q5; -.
CAZy; GH22; Glycoside Hydrolase Family 22.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0003796; F:lysozyme activity; IEA:UniProtKB-EC.
GO; GO:0019835; P:cytolysis; IEA:UniProtKB-KW.
GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
GO; GO:0008152; P:metabolic process; IEA:UniProtKB-KW.
InterPro; IPR008597; Invert_lysozyme.
InterPro; IPR023346; Lysozyme-like_dom_sf.
PANTHER; PTHR11195; PTHR11195; 1.
Pfam; PF05497; Destabilase; 1.
SUPFAM; SSF53955; SSF53955; 1.
2: Evidence at transcript level;
Antibiotic; Antimicrobial; Bacteriolytic enzyme; Disulfide bond;
Glycosidase; Hydrolase; Secreted; Signal.
SIGNAL 1 20 {ECO:0000255}.
CHAIN 21 137 Lysozyme.
/FTId=PRO_0000280512.
REGION 57 63 Substrate binding.
{ECO:0000250|UniProtKB:Q8IU26}.
REGION 109 111 Substrate binding.
{ECO:0000250|UniProtKB:Q8IU26}.
ACT_SITE 33 33 Proton donor.
{ECO:0000250|UniProtKB:Q8IU26}.
ACT_SITE 45 45 Nucleophile.
{ECO:0000250|UniProtKB:Q8IU26}.
BINDING 88 88 Substrate.
{ECO:0000250|UniProtKB:Q8IU26}.
DISULFID 25 102 {ECO:0000250|UniProtKB:Q8IU26}.
DISULFID 28 133 {ECO:0000250|UniProtKB:Q8IU26}.
DISULFID 30 37 {ECO:0000250|UniProtKB:Q8IU26}.
DISULFID 42 51 {ECO:0000250|UniProtKB:Q8IU26}.
DISULFID 64 84 {ECO:0000250|UniProtKB:Q8IU26}.
DISULFID 74 80 {ECO:0000250|UniProtKB:Q8IU26}.
DISULFID 98 116 {ECO:0000250|UniProtKB:Q8IU26}.
SEQUENCE 137 AA; 14918 MW; 5E267529DE695722 CRC64;
MSAVLVLALV LLSLTCVTDA ISDACLTCIC KQESYGCTQI GCRMDGRSLS CGYFQIKKSY
WIDCGRLGSS WEACADDYNC AVRCVRAYMK KYIGKSGCTA NCKNYARLHN GGPKGCTKPS
TLTYWNAVKN QGCSINS


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