ID   LYSC1_TACAC             Reviewed;         125 AA.
AC   P37156;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 1.
DT   25-MAY-2022, entry version 99.
DE   RecName: Full=Lysozyme C I;
DE            EC=3.2.1.17;
DE   AltName: Full=1,4-beta-N-acetylmuramidase C;
OS   Tachyglossus aculeatus aculeatus (Southeast Australian short-beaked
OS   echidna).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Monotremata; Tachyglossidae; Tachyglossus.
OX   NCBI_TaxID=49271;
RN   [1]
RP   PROTEIN SEQUENCE.
RC   TISSUE=Milk;
RX   PubMed=1768265;
RA   Teahan C.G., McKenzie H.A., Shaw D.C., Griffiths M.;
RT   "The isolation and amino acid sequences of echidna (Tachyglossus aculeatus)
RT   milk lysozyme I and II.";
RL   Biochem. Int. 24:85-95(1991).
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
RX   PubMed=15299900; DOI=10.1107/s0907444996015831;
RA   Guss J.M., Messer M., Costello M., Hardy K., Kumar V.;
RT   "Structure of the calcium-binding Echidna milk lysozyme at 1.9-A
RT   resolution.";
RL   Acta Crystallogr. D 53:355-363(1997).
RN   [3]
RP   ERRATUM OF PUBMED:15299900.
RX   DOI=10.1107/S0907444997099162;
RA   Guss J.M., Messer M., Costello M., Hardy K., Kumar V.;
RL   Acta Crystallogr. D 53:805-805(1997).
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   -!- SUBCELLULAR LOCATION: Secreted.
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   -!- SIMILARITY: Belongs to the glycosyl hydrolase 22 family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00680}.
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DR   PIR; A45660; A45660.
DR   PDB; 1JUG; X-ray; 1.90 A; A=1-125.
DR   PDBsum; 1JUG; -.
DR   AlphaFoldDB; P37156; -.
DR   SMR; P37156; -.
DR   CAZy; GH22; Glycoside Hydrolase Family 22.
DR   EvolutionaryTrace; P37156; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0003796; F:lysozyme activity; IEA:UniProtKB-EC.
DR   GO; GO:0019835; P:cytolysis; IEA:UniProtKB-KW.
DR   GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR   GO; GO:0008152; P:metabolic process; IEA:UniProtKB-KW.
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   InterPro; IPR030056; Lysozyme_C.
DR   PANTHER; PTHR11407; PTHR11407; 1.
DR   PANTHER; PTHR11407:SF28; PTHR11407:SF28; 1.
DR   Pfam; PF00062; Lys; 1.
DR   PRINTS; PR00137; LYSOZYME.
DR   PRINTS; PR00135; LYZLACT.
DR   SMART; SM00263; LYZ1; 1.
DR   SUPFAM; SSF53955; SSF53955; 1.
DR   PROSITE; PS00128; GLYCOSYL_HYDROL_F22_1; 1.
DR   PROSITE; PS51348; GLYCOSYL_HYDROL_F22_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Antimicrobial; Bacteriolytic enzyme;
KW   Direct protein sequencing; Disulfide bond; Glycosidase; Hydrolase;
KW   Milk protein; Secreted.
FT   CHAIN           1..125
FT                   /note="Lysozyme C I"
FT                   /id="PRO_0000208857"
FT   DOMAIN          1..125
FT                   /note="C-type lysozyme"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT   ACT_SITE        35
FT   ACT_SITE        52
FT   DISULFID        9..125
FT   DISULFID        30..115
FT   DISULFID        64..80
FT   DISULFID        76..94
FT   HELIX           5..14
FT                   /evidence="ECO:0007829|PDB:1JUG"
FT   HELIX           25..36
FT                   /evidence="ECO:0007829|PDB:1JUG"
FT   STRAND          43..45
FT                   /evidence="ECO:0007829|PDB:1JUG"
FT   STRAND          51..53
FT                   /evidence="ECO:0007829|PDB:1JUG"
FT   TURN            54..57
FT                   /evidence="ECO:0007829|PDB:1JUG"
FT   TURN            60..63
FT                   /evidence="ECO:0007829|PDB:1JUG"
FT   HELIX           80..83
FT                   /evidence="ECO:0007829|PDB:1JUG"
FT   STRAND          84..86
FT                   /evidence="ECO:0007829|PDB:1JUG"
FT   HELIX           89..102
FT                   /evidence="ECO:0007829|PDB:1JUG"
FT   HELIX           109..114
FT                   /evidence="ECO:0007829|PDB:1JUG"
FT   TURN            115..117
FT                   /evidence="ECO:0007829|PDB:1JUG"
FT   HELIX           121..123
FT                   /evidence="ECO:0007829|PDB:1JUG"
SQ   SEQUENCE   125 AA;  13994 MW;  18D8A1DBA3724073 CRC64;
     KILKKQELCK NLVAQGMNGY QHITLPNWVC TAFHESSYNT RATNHNTDGS TDYGILQINS
     RYWCHDGKTP GSKNACNISC SKLLDDDITD DLKCAKKIAG EAKGLTPWVA WKSKCRGHDL
     SKFKC