ID   LYSC1_ANAPL             Reviewed;         147 AA.
AC   P00705;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   27-MAR-2024, entry version 118.
DE   RecName: Full=Lysozyme C-1;
DE            EC=3.2.1.17;
DE   AltName: Full=1,4-beta-N-acetylmuramidase C;
DE   Flags: Precursor;
OS   Anas platyrhynchos (Mallard) (Anas boschas).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Anseriformes; Anatidae;
OC   Anatinae; Anas.
OX   NCBI_TaxID=8839;
RN   [1]
RP   PROTEIN SEQUENCE OF 1-18 (PRECURSOR PROTEIN).
RC   STRAIN=Pekin breed;
RX   PubMed=3511061; DOI=10.1016/s0021-9258(17)35936-7;
RA   Weisman L.S., Krummel B.M., Wilson A.C.;
RT   "Evolutionary shift in the site of cleavage of prelysozyme.";
RL   J. Biol. Chem. 261:2309-2313(1986).
RN   [2]
RP   PROTEIN SEQUENCE OF 19-147 (DL-1; DL-2 AND DL-3).
RC   STRAIN=Pekin breed;
RX   PubMed=7068576; DOI=10.1093/oxfordjournals.jbchem.a133729;
RA   Kondo K., Fujio H., Amano T.;
RT   "Chemical and immunological properties and amino acid sequences of three
RT   lysozymes from Peking-duck egg white.";
RL   J. Biochem. 91:571-587(1982).
RN   [3]
RP   PROTEIN SEQUENCE OF 19-147 (LYSOZYME II).
RX   PubMed=5138644; DOI=10.1111/j.1432-1033.1971.tb19650.x;
RA   Hermann J., Jolles J., Jolles P.;
RT   "Multiple forms of duck-egg white lysozyme. Primary structure of two duck
RT   lysozymes.";
RL   Eur. J. Biochem. 24:12-17(1971).
RN   [4]
RP   DISULFIDE BONDS.
RX   PubMed=4580844; DOI=10.1016/0003-9861(73)90631-0;
RA   Hermann J., Jolles J., Jolles P.;
RT   "The disulfide bridges of duck egg-white lysozyme II.";
RL   Arch. Biochem. Biophys. 158:355-358(1973).
RN   [5]
RP   CHARACTERIZATION OF VARIANTS DL-1; DL-2 AND DL-3C.
RC   STRAIN=Pekin breed;
RX   PubMed=5542021; DOI=10.1016/s0021-9258(18)62520-7;
RA   Prager E.M., Wilson A.C.;
RT   "Multiple lysozymes of duck egg white.";
RL   J. Biol. Chem. 246:523-530(1971).
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   -!- 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   -!- MISCELLANEOUS: The sequence of the DL-2 variant of lysozyme C from
CC       Pekin duck is shown. As only one lysozyme, or any combination of 2
CC       lysozymes, but never all 3, occurred in one egg, the existence of 3
CC       alleles at one locus has been suggested.
CC   -!- MISCELLANEOUS: The amino acid compositions of DL-1, DL-2, and DL-3 are
CC       identical with those of lysozymes A, B, and C, respectively. DL-1 and
CC       DL-2 are electrophoretically and immunologically indistinguishable from
CC       lysozymes A and B, respectively.
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   PIR; D92574; LZDK.
DR   PDB; 5V8G; X-ray; 1.20 A; A=19-145.
DR   PDB; 5V92; X-ray; 1.11 A; A/B=19-147.
DR   PDB; 5V94; X-ray; 1.65 A; A/B=19-147.
DR   PDB; 6D9I; X-ray; 1.15 A; A/B=19-147.
DR   PDBsum; 5V8G; -.
DR   PDBsum; 5V92; -.
DR   PDBsum; 5V94; -.
DR   PDBsum; 6D9I; -.
DR   AlphaFoldDB; P00705; -.
DR   SMR; P00705; -.
DR   CAZy; GH22; Glycoside Hydrolase Family 22.
DR   ABCD; P00705; 1 sequenced antibody.
DR   BRENDA; 3.2.1.17; 334.
DR   Proteomes; UP000694400; Unplaced.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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; 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   3D-structure; Antimicrobial; Bacteriolytic enzyme;
KW   Direct protein sequencing; Disulfide bond; Glycosidase; Hydrolase;
KW   Secreted; Signal.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000269|PubMed:5138644,
FT                   ECO:0000269|PubMed:7068576"
FT   CHAIN           19..147
FT                   /note="Lysozyme C-1"
FT                   /id="PRO_0000018494"
FT   DOMAIN          19..147
FT                   /note="C-type lysozyme"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT   ACT_SITE        53
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT   ACT_SITE        70
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT   DISULFID        24..145
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00680,
FT                   ECO:0000269|PubMed:4580844"
FT   DISULFID        48..133
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00680,
FT                   ECO:0000269|PubMed:4580844"
FT   DISULFID        82..98
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00680,
FT                   ECO:0000269|PubMed:4580844"
FT   DISULFID        94..112
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00680,
FT                   ECO:0000269|PubMed:4580844"
FT   VARIANT         43
FT                   /note="L -> I (in DL3)"
FT   VARIANT         55
FT                   /note="G -> S (in DL1 and lysozyme II)"
FT   VARIANT         75
FT                   /note="Q -> E (in lysozyme II)"
FT   VARIANT         89
FT                   /note="R -> G (in DL1 and lysozyme II)"
FT   VARIANT         97
FT                   /note="P -> R (in DL3)"
FT   HELIX           23..32
FT                   /evidence="ECO:0007829|PDB:5V92"
FT   HELIX           43..54
FT                   /evidence="ECO:0007829|PDB:5V92"
FT   STRAND          61..63
FT                   /evidence="ECO:0007829|PDB:5V92"
FT   STRAND          69..71
FT                   /evidence="ECO:0007829|PDB:5V92"
FT   TURN            72..75
FT                   /evidence="ECO:0007829|PDB:5V92"
FT   TURN            78..80
FT                   /evidence="ECO:0007829|PDB:5V92"
FT   HELIX           98..102
FT                   /evidence="ECO:0007829|PDB:5V92"
FT   STRAND          103..105
FT                   /evidence="ECO:0007829|PDB:6D9I"
FT   HELIX           107..119
FT                   /evidence="ECO:0007829|PDB:5V92"
FT   HELIX           122..125
FT                   /evidence="ECO:0007829|PDB:6D9I"
FT   HELIX           127..132
FT                   /evidence="ECO:0007829|PDB:5V92"
FT   TURN            133..135
FT                   /evidence="ECO:0007829|PDB:5V92"
FT   HELIX           138..142
FT                   /evidence="ECO:0007829|PDB:5V92"
SQ   SEQUENCE   147 AA;  16363 MW;  B0F2B6A9F7DA3978 CRC64;
     MKALLTLVFC LLPLAAQGKV YSRCELAAAM KRLGLDNYRG YSLGNWVCAA NYESGFNTQA
     TNRNTDGSTD YGILQINSRW WCDNGKTPRS KNACGIPCSV LLRSDITEAV RCAKRIVSDG
     DGMNAWVAWR NRCRGTDVSK WIRGCRL
//