LYSC_COLLI
ID LYSC_COLLI Reviewed; 127 AA.
AC P00708;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Lysozyme C;
DE EC=3.2.1.17;
DE AltName: Full=1,4-beta-N-acetylmuramidase C;
GN Name=LYZ;
OS Columba livia (Rock dove).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Columbiformes; Columbidae; Columba.
OX NCBI_TaxID=8932;
RN [1]
RP PROTEIN SEQUENCE.
RC TISSUE=Egg white;
RX PubMed=4091856;
RA Rodriguez R., Menendez-Arias L., Gonzalez de Buitrago G., Gavilanes J.G.;
RT "Amino acid sequence of pigeon egg-white lysozyme.";
RL Biochem. Int. 11:841-843(1985).
RN [2]
RP CALCIUM-BINDING DATA.
RX PubMed=3214551; DOI=10.1515/bchm3.1988.369.2.671;
RA Nitta K., Tsuge H., Shimazaki K., Sugai S.;
RT "Calcium-binding lysozymes.";
RL Biol. Chem. Hoppe-Seyler 369:671-675(1988).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
RX PubMed=1607355; DOI=10.1093/oxfordjournals.jbchem.a123703;
RA Yao M., Tanaka I., Hikichi K., Nitta K.;
RT "Crystallization and preliminary X-ray structure analysis of pigeon egg-
RT white lysozyme.";
RL J. Biochem. 111:1-3(1992).
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 -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Note=Binds 1 Ca(2+) ion per subunit.;
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; A00863; LZPY.
DR AlphaFoldDB; P00708; -.
DR SMR; P00708; -.
DR STRING; 8932.XP_005505385.1; -.
DR CAZy; GH22; Glycoside Hydrolase Family 22.
DR eggNOG; ENOG502S4CB; Eukaryota.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0003796; F:lysozyme activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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 Antimicrobial; Bacteriolytic enzyme; Calcium; Direct protein sequencing;
KW Disulfide bond; Glycosidase; Hydrolase; Metal-binding; Secreted.
FT CHAIN 1..127
FT /note="Lysozyme C"
FT /id="PRO_0000208862"
FT DOMAIN 1..127
FT /note="C-type lysozyme"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT ACT_SITE 35
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT ACT_SITE 52
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT BINDING 82
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P11376"
FT BINDING 85
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P11376,
FT ECO:0000305|PubMed:1607355"
FT BINDING 87
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P11376"
FT BINDING 90
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P11376,
FT ECO:0000305|PubMed:1607355"
FT BINDING 91
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P11376,
FT ECO:0000305|PubMed:1607355"
FT DISULFID 6..127
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT DISULFID 30..115
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT DISULFID 64..80
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT DISULFID 76..94
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
SQ SEQUENCE 127 AA; 14452 MW; 96D3BAFDFD934DD8 CRC64;
KDIPRCELVK ILRRHGFEGF VGKTVANWVC LVKHESGYRT TAFNNNGPNS RDYGIFQINS
KYWCNDGKTR GSKNACNINC SKLRDDNIAD DIQCAKKIAR EARGLTPWVA WKKYCQGKDL
SSYVRGC
