ID   LYS_ANTMY               Reviewed;         120 AA.
AC   Q7SID7;
DT   16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2003, sequence version 1.
DT   27-MAR-2024, entry version 63.
DE   RecName: Full=Lysozyme;
DE            EC=3.2.1.17;
DE   AltName: Full=1,4-beta-N-acetylmuramidase;
OS   Antheraea mylitta (Tasar silkworm).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Bombycoidea;
OC   Saturniidae; Saturniinae; Saturniini; Antheraea.
OX   NCBI_TaxID=34739;
RN   [1] {ECO:0000305, ECO:0000312|PDB:1IIZ}
RP   PROTEIN SEQUENCE OF 1-32, AND X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
RX   PubMed=11522783; DOI=10.1074/jbc.m104674200;
RA   Jain D., Nair D.T., Swaminathan G.J., Abraham E.G., Nagaraju J.,
RA   Salunke D.M.;
RT   "Structure of the induced antibacterial protein from tasar silkworm,
RT   Antheraea mylitta. Implications to molecular evolution.";
RL   J. Biol. Chem. 276:41377-41382(2001).
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. {ECO:0000305}.
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. {ECO:0000269|PubMed:11522783}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 22 family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00680}.
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DR   PDB; 1IIZ; X-ray; 2.40 A; A=1-120.
DR   PDBsum; 1IIZ; -.
DR   AlphaFoldDB; Q7SID7; -.
DR   SMR; Q7SID7; -.
DR   CAZy; GH22; Glycoside Hydrolase Family 22.
DR   EvolutionaryTrace; Q7SID7; -.
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:0031640; P:killing of cells of another organism; IEA:UniProtKB-KW.
DR   GO; GO:0008152; P:metabolic process; IEA:UniProtKB-KW.
DR   CDD; cd16899; LYZ_C_invert; 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:SF63; 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   3D-structure; Antimicrobial; Bacteriolytic enzyme;
KW   Direct protein sequencing; Disulfide bond; Glycosidase; Hydrolase.
FT   CHAIN           1..120
FT                   /note="Lysozyme"
FT                   /id="PRO_0000235825"
FT   DOMAIN          1..120
FT                   /note="C-type lysozyme"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT   ACT_SITE        32
FT                   /evidence="ECO:0000250|UniProtKB:P00698,
FT                   ECO:0000255|PROSITE-ProRule:PRU00680"
FT   ACT_SITE        50
FT                   /evidence="ECO:0000250|UniProtKB:P00698,
FT                   ECO:0000255|PROSITE-ProRule:PRU00680"
FT   DISULFID        6..120
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00680,
FT                   ECO:0000269|PubMed:11522783"
FT   DISULFID        27..110
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00680,
FT                   ECO:0000269|PubMed:11522783"
FT   DISULFID        62..76
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00680,
FT                   ECO:0000269|PubMed:11522783"
FT   DISULFID        72..90
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00680,
FT                   ECO:0000269|PubMed:11522783"
FT   HELIX           5..14
FT                   /evidence="ECO:0007829|PDB:1IIZ"
FT   HELIX           19..21
FT                   /evidence="ECO:0007829|PDB:1IIZ"
FT   HELIX           22..32
FT                   /evidence="ECO:0007829|PDB:1IIZ"
FT   TURN            33..35
FT                   /evidence="ECO:0007829|PDB:1IIZ"
FT   STRAND          36..38
FT                   /evidence="ECO:0007829|PDB:1IIZ"
FT   STRAND          45..47
FT                   /evidence="ECO:0007829|PDB:1IIZ"
FT   TURN            52..55
FT                   /evidence="ECO:0007829|PDB:1IIZ"
FT   TURN            58..61
FT                   /evidence="ECO:0007829|PDB:1IIZ"
FT   STRAND          62..67
FT                   /evidence="ECO:0007829|PDB:1IIZ"
FT   HELIX           76..80
FT                   /evidence="ECO:0007829|PDB:1IIZ"
FT   STRAND          81..83
FT                   /evidence="ECO:0007829|PDB:1IIZ"
FT   HELIX           85..98
FT                   /evidence="ECO:0007829|PDB:1IIZ"
FT   TURN            99..102
FT                   /evidence="ECO:0007829|PDB:1IIZ"
FT   HELIX           104..109
FT                   /evidence="ECO:0007829|PDB:1IIZ"
FT   STRAND          110..112
FT                   /evidence="ECO:0007829|PDB:1IIZ"
SQ   SEQUENCE   120 AA;  13741 MW;  5705F78312527AE7 CRC64;
     KRFTRCGLVN ELRKQGFDEN LMRDWVCLVE NESARYTDKI ANVNKNGSRD YGLFQINDKY
     WCSKGSTPGK DCNVTCSQLL TDDITVASTC AKKIYKRTKF DAWSGWDNHC NHSNPDISSC
//