LYSC1_HORSE
ID LYSC1_HORSE Reviewed; 129 AA.
AC P11376;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Lysozyme C, milk isozyme;
DE EC=3.2.1.17;
DE AltName: Full=1,4-beta-N-acetylmuramidase C;
GN Name=LYZ;
OS Equus caballus (Horse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus.
OX NCBI_TaxID=9796;
RN [1]
RP PROTEIN SEQUENCE.
RC TISSUE=Milk;
RX PubMed=4039138;
RA McKenzie H.A., Shaw D.C.;
RT "The amino acid sequence of equine milk lysozyme.";
RL Biochem. Int. 10:23-31(1985).
RN [2]
RP CALCIUM-BINDING DATA.
RC TISSUE=Milk;
RX PubMed=3666156; DOI=10.1016/0014-5793(87)80328-9;
RA Nitta K., Tsuge H., Sugai S., Shimazaki K.;
RT "The calcium-binding property of equine lysozyme.";
RL FEBS Lett. 223:405-408(1987).
RN [3]
RP PROTEIN SEQUENCE OF 1-35, AND CRYSTALLIZATION.
RC TISSUE=Milk;
RX PubMed=2394704; DOI=10.1016/s0021-9258(18)77198-6;
RA Zeng J., Rao K.R., Brew K., Fenna R.;
RT "Crystallization of a calcium-binding lysozyme from horse milk.";
RL J. Biol. Chem. 265:14886-14887(1990).
RN [4]
RP STRUCTURE BY NMR.
RC TISSUE=Milk;
RX PubMed=1646637; DOI=10.1016/0167-4838(91)90095-h;
RA Tsuge H., Koseki K., Miyano M., Shimazaki K., Chuman T., Matsumoto T.,
RA Noma M., Nitta K., Sugai S.;
RT "A structural study of calcium-binding equine lysozyme by two-dimensional
RT 1H-NMR.";
RL Biochim. Biophys. Acta 1078:77-84(1991).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
RC TISSUE=Milk;
RX PubMed=1569037; DOI=10.1093/oxfordjournals.jbchem.a123727;
RA Tsuge H., Ago H., Noma M., Nitta K., Sugai S., Miyano M.;
RT "Crystallographic studies of a calcium binding lysozyme from equine milk at
RT 2.5-A resolution.";
RL J. Biochem. 111:141-143(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 -!- 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; S07435; S07435.
DR PDB; 2EQL; X-ray; 2.50 A; A=1-129.
DR PDBsum; 2EQL; -.
DR AlphaFoldDB; P11376; -.
DR SMR; P11376; -.
DR STRING; 9796.ENSECAP00000008172; -.
DR Allergome; 12069; Equ c 6.
DR Allergome; 12070; Equ c 6.0101.
DR CAZy; GH22; Glycoside Hydrolase Family 22.
DR PaxDb; P11376; -.
DR PRIDE; P11376; -.
DR HOGENOM; CLU_111620_0_1_1; -.
DR InParanoid; P11376; -.
DR EvolutionaryTrace; P11376; -.
DR Proteomes; UP000002281; Unplaced.
DR GO; GO:0003796; F:lysozyme activity; IBA:GO_Central.
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; Reference proteome.
FT CHAIN 1..129
FT /note="Lysozyme C, milk isozyme"
FT /id="PRO_0000208851"
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:0000305|PubMed:3666156"
FT BINDING 85
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000305|PubMed:3666156"
FT BINDING 87
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000305|PubMed:3666156"
FT BINDING 90
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000305|PubMed:3666156"
FT BINDING 91
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000305|PubMed:3666156"
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..13
FT /evidence="ECO:0007829|PDB:2EQL"
FT TURN 14..19
FT /evidence="ECO:0007829|PDB:2EQL"
FT HELIX 20..22
FT /evidence="ECO:0007829|PDB:2EQL"
FT HELIX 25..36
FT /evidence="ECO:0007829|PDB:2EQL"
FT STRAND 37..39
FT /evidence="ECO:0007829|PDB:2EQL"
FT STRAND 43..45
FT /evidence="ECO:0007829|PDB:2EQL"
FT STRAND 52..54
FT /evidence="ECO:0007829|PDB:2EQL"
FT TURN 55..58
FT /evidence="ECO:0007829|PDB:2EQL"
FT HELIX 61..64
FT /evidence="ECO:0007829|PDB:2EQL"
FT STRAND 68..71
FT /evidence="ECO:0007829|PDB:2EQL"
FT HELIX 80..83
FT /evidence="ECO:0007829|PDB:2EQL"
FT STRAND 84..86
FT /evidence="ECO:0007829|PDB:2EQL"
FT HELIX 89..98
FT /evidence="ECO:0007829|PDB:2EQL"
FT HELIX 104..107
FT /evidence="ECO:0007829|PDB:2EQL"
FT HELIX 109..114
FT /evidence="ECO:0007829|PDB:2EQL"
FT TURN 115..117
FT /evidence="ECO:0007829|PDB:2EQL"
FT TURN 121..126
FT /evidence="ECO:0007829|PDB:2EQL"
SQ SEQUENCE 129 AA; 14653 MW; 87040531F4B60F46 CRC64;
KVFSKCELAH KLKAQEMDGF GGYSLANWVC MAEYESNFNT RAFNGKNANG SSDYGLFQLN
NKWWCKDNKR SSSNACNIMC SKLLDENIDD DISCAKRVVR DPKGMSAWKA WVKHCKDKDL
SEYLASCNL
