ID   LYSC_AXIAX              Reviewed;         129 AA.
AC   P12066;
DT   01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1989, sequence version 1.
DT   03-MAY-2023, entry version 103.
DE   RecName: Full=Lysozyme C-1/C-2;
DE            EC=3.2.1.17;
DE   AltName: Full=1,4-beta-N-acetylmuramidase C;
OS   Axis axis (Axis deer) (Chital).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Cervidae;
OC   Cervinae; Axis.
OX   NCBI_TaxID=30531;
RN   [1]
RP   PROTEIN SEQUENCE.
RC   TISSUE=Stomach;
RX   PubMed=2504928; DOI=10.1007/bf02602933;
RA   Jolles J., Jolles P., Bowman B.H., Prager E.M., Stewart C.-B., Wilson A.C.;
RT   "Episodic evolution in the stomach lysozymes of ruminants.";
RL   J. Mol. Evol. 28:528-535(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOZYMES 1 AND 2).
RX   PubMed=2318875; DOI=10.1016/s0021-9258(19)34066-9;
RA   Irwin D.M., Wilson A.C.;
RT   "Concerted evolution of ruminant stomach lysozymes. Characterization of
RT   lysozyme cDNA clones from sheep and deer.";
RL   J. Biol. Chem. 265:4944-4952(1990).
CC   -!- FUNCTION: Lysozymes have primarily a bacteriolytic function; those in
CC       tissues and body fluids are associated with the monocyte-macrophage
CC       system and enhance the activity of immunoagents.
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;
CC   -!- SUBUNIT: Monomer.
CC   -!- MISCELLANEOUS: Lysozyme C is capable of both hydrolysis and
CC       transglycosylation; it shows also a slight esterase activity. It acts
CC       rapidly on both peptide-substituted and unsubstituted peptidoglycan,
CC       and slowly on chitin oligosaccharides.
CC   -!- MISCELLANEOUS: The sequence of isozyme 1 is shown.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 22 family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00680}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; M32499; AAA30344.1; -; mRNA.
DR   EMBL; M32500; AAA30345.1; -; mRNA.
DR   PIR; G35558; G35558.
DR   PIR; H35558; H35558.
DR   AlphaFoldDB; P12066; -.
DR   SMR; P12066; -.
DR   CAZy; GH22; Glycoside Hydrolase Family 22.
DR   GO; GO:0003796; F:lysozyme activity; IEA:UniProtKB-EC.
DR   GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR   GO; GO:0007586; P:digestion; IEA:UniProtKB-KW.
DR   GO; GO:0031640; P:killing of cells of another organism; IEA:UniProtKB-KW.
DR   GO; GO:0008152; P:metabolic process; IEA:UniProtKB-KW.
DR   CDD; cd16897; LYZ_C; 1.
DR   Gene3D; 1.10.530.10; -; 1.
DR   InterPro; IPR001916; Glyco_hydro_22.
DR   InterPro; IPR019799; Glyco_hydro_22_CS.
DR   InterPro; IPR000974; Glyco_hydro_22_lys.
DR   InterPro; IPR023346; Lysozyme-like_dom_sf.
DR   PANTHER; PTHR11407; LYSOZYME C; 1.
DR   PANTHER; PTHR11407:SF28; LYSOZYME C; 1.
DR   Pfam; PF00062; Lys; 1.
DR   PRINTS; PR00137; LYSOZYME.
DR   PRINTS; PR00135; LYZLACT.
DR   SMART; SM00263; LYZ1; 1.
DR   SUPFAM; SSF53955; Lysozyme-like; 1.
DR   PROSITE; PS00128; GLYCOSYL_HYDROL_F22_1; 1.
DR   PROSITE; PS51348; GLYCOSYL_HYDROL_F22_2; 1.
PE   1: Evidence at protein level;
KW   Antimicrobial; Bacteriolytic enzyme; Digestion; Direct protein sequencing;
KW   Disulfide bond; Glycosidase; Hydrolase.
FT   CHAIN           1..129
FT                   /note="Lysozyme C-1/C-2"
FT                   /id="PRO_0000208843"
FT   DOMAIN          1..129
FT                   /note="C-type lysozyme"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT   ACT_SITE        35
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT   ACT_SITE        53
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT   DISULFID        6..127
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT   DISULFID        30..115
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT   DISULFID        65..81
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT   DISULFID        77..95
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT   VARIANT         66
FT                   /note="D -> N (in isozyme 2)"
FT   VARIANT         88
FT                   /note="N -> D (in isozyme 2)"
FT   VARIANT         90
FT                   /note="D -> A (in isozyme 2)"
FT   VARIANT         94
FT                   /note="T -> A (in isozyme 2)"
FT   VARIANT         117
FT                   /note="G -> H (in isozyme 2)"
SQ   SEQUENCE   129 AA;  14446 MW;  A0AA48E69C2EB383 CRC64;
     KVFERCELAR TLKELGLDGY KGVSLANWLC LTKWESSYNT KATNYNPGSE STDYGIFQIN
     SKWWCDDGKT PNAVDGCHVA CSELMENNID KAVTCAKQIV REQGITAWVA WKSHCRGHDV
     SSYVEGCTL
//