LYSC_EQUAS
ID LYSC_EQUAS Reviewed; 129 AA.
AC P11375;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Lysozyme C;
DE EC=3.2.1.17;
DE AltName: Full=1,4-beta-N-acetylmuramidase C;
GN Name=LYZ;
OS Equus asinus (Donkey) (Equus africanus asinus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus.
OX NCBI_TaxID=9793;
RN [1]
RP PROTEIN SEQUENCE.
RX PubMed=3242541; DOI=10.1515/bchm3.1988.369.2.1109;
RA Godovac-Zimmermann J., Conti A., Napolitano L.;
RT "The primary structure of donkey (Equus asinus) lysozyme contains the
RT Ca(II) binding site of alpha-lactalbumin.";
RL Biol. Chem. Hoppe-Seyler 369:1109-1115(1988).
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; Evidence={ECO:0000305};
CC Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000305};
CC -!- SUBUNIT: Monomer.
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; S01661; S01661.
DR PDB; 5XUW; X-ray; 1.76 A; A/B=1-129.
DR PDBsum; 5XUW; -.
DR AlphaFoldDB; P11375; -.
DR SMR; P11375; -.
DR Allergome; 12071; Equ as 6.
DR CAZy; GH22; Glycoside Hydrolase Family 22.
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; IPR030057; LYZL1/LYZL2.
DR PANTHER; PTHR11407; PTHR11407; 1.
DR PANTHER; PTHR11407:SF62; PTHR11407:SF62; 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; Calcium;
KW Direct protein sequencing; Disulfide bond; Glycosidase; Hydrolase;
KW Metal-binding; Milk protein.
FT CHAIN 1..129
FT /note="Lysozyme C"
FT /id="PRO_0000208849"
FT DOMAIN 1..129
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 53
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:P81708"
FT BINDING 85
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P81708"
FT BINDING 87
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P81708"
FT BINDING 90
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P81708"
FT BINDING 91
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P81708"
FT DISULFID 6..127
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT DISULFID 30..115
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT DISULFID 65..80
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT DISULFID 76..94
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT HELIX 5..14
FT /evidence="ECO:0007829|PDB:5XUW"
FT HELIX 20..22
FT /evidence="ECO:0007829|PDB:5XUW"
FT HELIX 25..36
FT /evidence="ECO:0007829|PDB:5XUW"
FT STRAND 43..46
FT /evidence="ECO:0007829|PDB:5XUW"
FT STRAND 48..50
FT /evidence="ECO:0007829|PDB:5XUW"
FT TURN 55..58
FT /evidence="ECO:0007829|PDB:5XUW"
FT TURN 61..64
FT /evidence="ECO:0007829|PDB:5XUW"
FT HELIX 80..83
FT /evidence="ECO:0007829|PDB:5XUW"
FT STRAND 84..86
FT /evidence="ECO:0007829|PDB:5XUW"
FT HELIX 89..100
FT /evidence="ECO:0007829|PDB:5XUW"
FT HELIX 104..107
FT /evidence="ECO:0007829|PDB:5XUW"
FT HELIX 109..114
FT /evidence="ECO:0007829|PDB:5XUW"
FT TURN 115..117
FT /evidence="ECO:0007829|PDB:5XUW"
FT TURN 121..124
FT /evidence="ECO:0007829|PDB:5XUW"
FT HELIX 125..127
FT /evidence="ECO:0007829|PDB:5XUW"
SQ SEQUENCE 129 AA; 14688 MW; 094D0850B41A40F5 CRC64;
KVFSKCELAH KLKAQEMDGF GGYSLANWVC MAEYESNFNT RAFNGKNANG SYDYGLFQLN
SKWWCKDNKR SSSNACNIMC SKLLDDNIDD DISCAKRVVR DPKGMSAWKA WVKHCKDKDL
SEYLASCNL
