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   25-MAY-2022, entry version 91.
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) (Phasianus hoazin).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Opisthocomiformes; Opisthocomidae;
OC   Opisthocomus.
OX   NCBI_TaxID=30419;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Stomach;
RX   PubMed=7815930; DOI=10.1093/oxfordjournals.molbev.a040173;
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 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 {ECO:0000250}.
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   EMBL; L36032; AAA73935.1; -; mRNA.
DR   PIR; A55241; A55241.
DR   PDB; 6T5S; X-ray; 1.50 A; A=20-145.
DR   PDB; 6T6C; X-ray; 1.25 A; A=21-145.
DR   PDBsum; 6T5S; -.
DR   PDBsum; 6T6C; -.
DR   AlphaFoldDB; Q91159; -.
DR   SMR; Q91159; -.
DR   CAZy; GH22; Glycoside Hydrolase Family 22.
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; Disulfide bond;
KW   Glycosidase; Hydrolase; Secreted; Signal.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..145
FT                   /note="Lysozyme C"
FT                   /id="PRO_0000018498"
FT   DOMAIN          20..145
FT                   /note="C-type lysozyme"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT   ACT_SITE        54
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT   ACT_SITE        70
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT   DISULFID        25..145
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT   DISULFID        49..133
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT   DISULFID        82..98
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT   DISULFID        94..112
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT   VARIANT         23
FT                   /note="P -> S (in 50% of the molecules)"
FT   HELIX           24..33
FT                   /evidence="ECO:0007829|PDB:6T6C"
FT   HELIX           39..41
FT                   /evidence="ECO:0007829|PDB:6T6C"
FT   HELIX           44..54
FT                   /evidence="ECO:0007829|PDB:6T6C"
FT   TURN            55..57
FT                   /evidence="ECO:0007829|PDB:6T6C"
FT   STRAND          62..64
FT                   /evidence="ECO:0007829|PDB:6T6C"
FT   STRAND          69..71
FT                   /evidence="ECO:0007829|PDB:6T6C"
FT   TURN            72..75
FT                   /evidence="ECO:0007829|PDB:6T6C"
FT   TURN            78..80
FT                   /evidence="ECO:0007829|PDB:6T6C"
FT   HELIX           98..102
FT                   /evidence="ECO:0007829|PDB:6T6C"
FT   HELIX           107..120
FT                   /evidence="ECO:0007829|PDB:6T6C"
FT   HELIX           127..132
FT                   /evidence="ECO:0007829|PDB:6T6C"
FT   TURN            133..135
FT                   /evidence="ECO:0007829|PDB:6T6C"
FT   HELIX           139..142
FT                   /evidence="ECO:0007829|PDB:6T6C"
SQ   SEQUENCE   145 AA;  16268 MW;  FCDA921A2CAE7E94 CRC64;
     MLFFGFLLAF LSAVPGTEGE IIPRCELVKI LREHGFEGFE GTTIADWICL VQHESDYNTE
     AYNNNGPSRD YGIFQINSKY WCNDGKTSGA VDGCHISCSE LMTNDLEDDI KCAKKIARDA
     HGLTPWYGWK NHCEGRDLSS YVKGC