ID   LYSC_FUGRU              Reviewed;         143 AA.
AC   P61944;
DT   07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT   07-JUN-2004, sequence version 1.
DT   16-JUN-2009, entry version 38.
DE   RecName: Full=Lysozyme C;
DE            EC=3.2.1.17;
DE   AltName: Full=1,4-beta-N-acetylmuramidase C;
DE   Flags: Precursor;
OS   Fugu rubripes (Japanese pufferfish) (Takifugu rubripes).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei;
OC   Acanthomorpha; Acanthopterygii; Percomorpha; Tetraodontiformes;
OC   Tetradontoidea; Tetraodontidae; Takifugu.
OX   NCBI_TaxID=31033;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Liver;
RA   Miyadai T., Ootani M., Iwata K.;
RT   "Molecular cloning, expression of chicken- and goose-type lysozyme
RT   gene of torafugu (Takifugu rubripes).";
RL   Submitted (NOV-2003) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Lysozymes have primarily a bacteriolytic function; those
CC       in tissues and body fluids are associated with the monocyte-
CC       macrophage system and enhance the activity of immunoagents (By
CC       similarity).
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   -!- SUBUNIT: Monomer (By similarity).
CC   -!- MISCELLANEOUS: Lysozyme C is capable of both hydrolysis and
CC       transglycosylation; it shows also a slight esterase activity. It
CC       acts rapidly on both peptide-substituted and unsubstituted
CC       peptidoglycan, and slowly on chitin oligosaccharides.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 22 family.
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DR   EMBL; AB126243; BAD02933.1; -; mRNA.
DR   RefSeq; NP_001027914.1; -.
DR   UniGene; Tru.1982; -.
DR   SMR; P61944; 16-143.
DR   CAZy; GH22; Glycoside Hydrolase Family 22.
DR   GeneID; 445925; -.
DR   HOVERGEN; P61944; -.
DR   BRENDA; 3.2.1.17; 281122.
DR   GO; GO:0003796; F:lysozyme activity; IEA:EC.
DR   GO; GO:0016998; P:cell wall macromolecule catabolic process; IEA:InterPro.
DR   GO; GO:0019835; P:cytolysis; IEA:UniProtKB-KW.
DR   GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR   InterPro; IPR001916; Glyco_hydro_22.
DR   InterPro; IPR019799; Glyco_hydro_22_CS.
DR   InterPro; IPR000974; Glyco_hydro_22_lys.
DR   Pfam; PF00062; Lys; 1.
DR   PRINTS; PR00137; LYSOZYME.
DR   PRINTS; PR00135; LYZLACT.
DR   SMART; SM00263; LYZ1; 1.
DR   PROSITE; PS00128; LACTALBUMIN_LYSOZYME_1; FALSE_NEG.
DR   PROSITE; PS51348; LACTALBUMIN_LYSOZYME_2; 1.
PE   2: Evidence at transcript level;
KW   Antimicrobial; Bacteriolytic enzyme; Disulfide bond; Glycosidase;
KW   Hydrolase; Signal.
FT   SIGNAL        1     15       Potential.
FT   CHAIN        16    143       Lysozyme C.
FT                                /FTId=PRO_0000018500.
FT   ACT_SITE     50     50       By similarity.
FT   ACT_SITE     67     67       By similarity.
FT   DISULFID     21    141       By similarity.
FT   DISULFID     45    129       By similarity.
FT   DISULFID     79     94       By similarity.
FT   DISULFID     90    108       By similarity.
SQ   SEQUENCE   143 AA;  16198 MW;  72A5DC9C3F44C139 CRC64;
     MKIPVFLLLL ALANAKVFQR CEWARVLKAR GMDGYRGISL ADWVCLSKWE SQYNTNAINH
     NTDGSTDYGI FQINSRWWCN DDRIPTRNAC NIKCSALQTD DVTVAINCAK RVVSDPQGIR
     AWVAWNRHCQ NRDLSAYIAG CGL
//