LYSC_MELGA
ID LYSC_MELGA Reviewed; 147 AA.
AC P00703;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1990, sequence version 2.
DT 03-AUG-2022, entry version 155.
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 Meleagris gallopavo (Wild turkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Meleagridinae; Meleagris.
OX NCBI_TaxID=9103;
RN [1]
RP PROTEIN SEQUENCE OF 1-18 (PRECURSOR PROTEIN).
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.
RC TISSUE=Egg white;
RX PubMed=5440837; DOI=10.1016/s0021-9258(18)63195-3;
RA Larue J.N., Speck J.C. Jr.;
RT "Turkey egg white lysozyme. Preparation of the crystalline enzyme and
RT investigation of the amino acid sequence.";
RL J. Biol. Chem. 245:1985-1991(1970).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS), AND DISULFIDE BONDS.
RX PubMed=886621; DOI=10.1016/0022-2836(77)90238-8;
RA Sarma R., Bott R.;
RT "Crystallographic study of turkey egg-white lysozyme and its complex with a
RT disaccharide.";
RL J. Mol. Biol. 113:555-565(1977).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
RX PubMed=1515108; DOI=10.1107/s0108768191012466;
RA Howell P.L., Almo S.C., Parsons M., Petsko G.A., Hajdu J.;
RT "Structure determination of turkey egg-white lysozyme using Laue
RT diffraction data.";
RL Acta Crystallogr. B 48:200-207(1992).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS).
RX PubMed=15299795; DOI=10.1107/s0907444994013612;
RA Howell P.L.;
RT "Structure of hexagonal turkey egg-white lysozyme at 1.65-A resolution.";
RL Acta Crystallogr. D 51:654-662(1995).
RN [6]
RP STRUCTURE BY NMR.
RX PubMed=8344294; DOI=10.1111/j.1432-1033.1993.tb18030.x;
RA Bartik K., Dobson C.M., Redfield C.;
RT "1H-NMR analysis of turkey egg-white lysozyme and comparison with hen egg-
RT white lysozyme.";
RL Eur. J. Biochem. 215:255-266(1993).
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; C92574; LZTK.
DR RefSeq; XP_003202118.1; XM_003202070.3.
DR PDB; 135L; X-ray; 1.30 A; A=19-147.
DR PDB; 1DZB; X-ray; 2.00 A; X/Y=19-147.
DR PDB; 1JEF; X-ray; 1.77 A; A=19-147.
DR PDB; 1JSE; X-ray; 1.12 A; A=19-147.
DR PDB; 1JTP; X-ray; 1.90 A; L/M=19-147.
DR PDB; 1LJN; X-ray; 1.19 A; A=19-147.
DR PDB; 1LZ2; X-ray; 2.80 A; A=19-147.
DR PDB; 1LZY; X-ray; 1.55 A; A=19-147.
DR PDB; 1TEW; X-ray; 1.65 A; A=19-147.
DR PDB; 1UAC; X-ray; 1.70 A; Y=19-147.
DR PDB; 1XFT; X-ray; 3.35 A; A=19-147.
DR PDB; 2LZ2; X-ray; 2.20 A; A=19-147.
DR PDB; 3LZ2; X-ray; 2.50 A; A=19-147.
DR PDBsum; 135L; -.
DR PDBsum; 1DZB; -.
DR PDBsum; 1JEF; -.
DR PDBsum; 1JSE; -.
DR PDBsum; 1JTP; -.
DR PDBsum; 1LJN; -.
DR PDBsum; 1LZ2; -.
DR PDBsum; 1LZY; -.
DR PDBsum; 1TEW; -.
DR PDBsum; 1UAC; -.
DR PDBsum; 1XFT; -.
DR PDBsum; 2LZ2; -.
DR PDBsum; 3LZ2; -.
DR AlphaFoldDB; P00703; -.
DR BMRB; P00703; -.
DR SMR; P00703; -.
DR CAZy; GH22; Glycoside Hydrolase Family 22.
DR ABCD; P00703; 7 sequenced antibodies.
DR Ensembl; ENSMGAT00000011853; ENSMGAP00000010985; ENSMGAG00000010559.
DR GeneID; 100547044; -.
DR KEGG; mgp:100547044; -.
DR CTD; 4069; -.
DR GeneTree; ENSGT00940000153832; -.
DR HOGENOM; CLU_111620_0_1_1; -.
DR InParanoid; P00703; -.
DR OMA; CAKYIRQ; -.
DR OrthoDB; 1551203at2759; -.
DR TreeFam; TF324882; -.
DR EvolutionaryTrace; P00703; -.
DR Proteomes; UP000001645; Chromosome 1.
DR Bgee; ENSMGAG00000010559; Expressed in bursa of Fabricius and 12 other tissues.
DR GO; GO:0005737; C:cytoplasm; IDA:CAFA.
DR GO; GO:0005615; C:extracellular space; IEA:Ensembl.
DR GO; GO:0005539; F:glycosaminoglycan binding; IDA:CAFA.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0003796; F:lysozyme activity; IDA:CAFA.
DR GO; GO:0016998; P:cell wall macromolecule catabolic process; IDA:CAFA.
DR GO; GO:0019835; P:cytolysis; IEA:UniProtKB-KW.
DR GO; GO:0050830; P:defense response to Gram-positive bacterium; IEA:Ensembl.
DR GO; GO:0031640; P:killing of cells of another organism; IEA:Ensembl.
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 Reference proteome; Secreted; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000269|PubMed:5440837"
FT CHAIN 19..147
FT /note="Lysozyme C"
FT /id="PRO_0000018497"
FT DOMAIN 19..147
FT /note="C-type lysozyme"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT DISULFID 24..145
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00680,
FT ECO:0000269|PubMed:886621"
FT DISULFID 48..133
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00680,
FT ECO:0000269|PubMed:886621"
FT DISULFID 82..98
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00680,
FT ECO:0000269|PubMed:886621"
FT DISULFID 94..112
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00680,
FT ECO:0000269|PubMed:886621"
FT HELIX 23..32
FT /evidence="ECO:0007829|PDB:1JSE"
FT HELIX 38..40
FT /evidence="ECO:0007829|PDB:1TEW"
FT HELIX 43..54
FT /evidence="ECO:0007829|PDB:1JSE"
FT STRAND 55..59
FT /evidence="ECO:0007829|PDB:2LZ2"
FT STRAND 61..63
FT /evidence="ECO:0007829|PDB:1JSE"
FT STRAND 69..71
FT /evidence="ECO:0007829|PDB:1JSE"
FT TURN 72..75
FT /evidence="ECO:0007829|PDB:1JSE"
FT TURN 78..81
FT /evidence="ECO:0007829|PDB:1JSE"
FT STRAND 85..87
FT /evidence="ECO:0007829|PDB:1JSE"
FT HELIX 98..102
FT /evidence="ECO:0007829|PDB:1JSE"
FT STRAND 103..105
FT /evidence="ECO:0007829|PDB:1JSE"
FT HELIX 107..117
FT /evidence="ECO:0007829|PDB:1JSE"
FT STRAND 119..121
FT /evidence="ECO:0007829|PDB:1JTP"
FT HELIX 122..125
FT /evidence="ECO:0007829|PDB:1JSE"
FT HELIX 127..132
FT /evidence="ECO:0007829|PDB:1JSE"
FT TURN 133..135
FT /evidence="ECO:0007829|PDB:1JSE"
FT HELIX 138..142
FT /evidence="ECO:0007829|PDB:1JSE"
SQ SEQUENCE 147 AA; 16135 MW; 77C54CD70834583F CRC64;
MRSLLILVLC FLPLAALGKV YGRCELAAAM KRLGLDNYRG YSLGNWVCAA KFESNFNTHA
TNRNTDGSTD YGILQINSRW WCNDGRTPGS KNLCNIPCSA LLSSDITASV NCAKKIASGG
NGMNAWVAWR NRCKGTDVHA WIRGCRL
