LYSC1_ANAPL
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 25-MAY-2022, entry version 114.
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}.
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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 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 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
