ID   LYSC_OPIHO              Reviewed;         145 AA.
AC   Q91159;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   16-JUN-2009, entry version 54.
DE   RecName: Full=Lysozyme C;
DE            EC=3.2.1.17;
DE   AltName: Full=1,4-beta-N-acetylmuramidase C;
DE   Flags: Precursor;
GN   Name=LYZ;
OS   Opisthocomus hoazin (Hoatzin).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archosauria; Dinosauria; Saurischia; Theropoda; Coelurosauria; Aves;
OC   Neognathae; Opisthocomiformes; Opisthocomidae; Opisthocomus.
OX   NCBI_TaxID=30419;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Stomach;
RX   MEDLINE=95115540; PubMed=7815930;
RA   Kornegay J.R., Schilling J.W., Wilson A.C.;
RT   "Molecular adaptation of a leaf-eating bird: stomach lysozyme of the
RT   hoatzin.";
RL   Mol. Biol. Evol. 11:921-928(1994).
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.
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.
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; L36032; AAA73935.1; -; mRNA.
DR   PIR; A55241; A55241.
DR   HSSP; P37156; 1JUG.
DR   CAZy; GH22; Glycoside Hydrolase Family 22.
DR   HOVERGEN; Q91159; -.
DR   BRENDA; 3.2.1.17; 290509.
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; 1.
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     19       Potential.
FT   CHAIN        20    145       Lysozyme C.
FT                                /FTId=PRO_0000018498.
FT   ACT_SITE     53     53       By similarity.
FT   ACT_SITE     70     70       By similarity.
FT   DISULFID     25    145       By similarity.
FT   DISULFID     49    133       By similarity.
FT   DISULFID     82     98       By similarity.
FT   DISULFID     94    112       By similarity.
FT   VARIANT      23     23       P -> S (in 50% of the molecules).
SQ   SEQUENCE   145 AA;  16268 MW;  FCDA921A2CAE7E94 CRC64;
     MLFFGFLLAF LSAVPGTEGE IIPRCELVKI LREHGFEGFE GTTIADWICL VQHESDYNTE
     AYNNNGPSRD YGIFQINSKY WCNDGKTSGA VDGCHISCSE LMTNDLEDDI KCAKKIARDA
     HGLTPWYGWK NHCEGRDLSS YVKGC
//