LYSC1_CANLF
ID LYSC1_CANLF Reviewed; 129 AA.
AC P81708;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Lysozyme C, milk isozyme;
DE EC=3.2.1.17;
DE AltName: Full=1,4-beta-N-acetylmuramidase C;
OS Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP PROTEIN SEQUENCE.
RC TISSUE=Milk;
RX PubMed=8080284; DOI=10.1006/abbi.1994.1399;
RA Grobler J.A., Rao K.R., Pervaiz S., Brew K.;
RT "Sequences of two highly divergent canine type c lysozymes: implications
RT for the evolutionary origins of the lysozyme/alpha-lactalbumin
RT superfamily.";
RL Arch. Biochem. Biophys. 313:360-366(1994).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS), AND DISULFIDE BONDS.
RX PubMed=10727216; DOI=10.1021/bi991525a;
RA Koshiba T., Yao M., Kobashigawa Y., Demura M., Nakagawa A., Tanaka I.,
RA Kuwajima K., Nitta K.;
RT "Structure and thermodynamics of the extraordinarily stable molten globule
RT state of canine milk lysozyme.";
RL Biochemistry 39:3248-3257(2000).
RN [3] {ECO:0007744|PDB:1EL1}
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH CALCIUM.
RA Koshiba T., Yao M., Tanaka I., Nitta K.;
RT "Calcium Induced Conformational Changes of Canine Milk Lysozyme Revealed by
RT Structural and Thermodynamical Evidences.";
RL Submitted (MAR-2000) to the PDB data bank.
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS), CALCIUM-BINDING REGION, AND
RP DISULFIDE BONDS.
RX PubMed=20080106; DOI=10.1016/j.jmb.2010.01.021;
RA Nakamura T., Makabe K., Tomoyori K., Maki K., Mukaiyama A., Kuwajima K.;
RT "Different folding pathways taken by highly homologous proteins, goat
RT alpha-lactalbumin and canine milk lysozyme.";
RL J. Mol. Biol. 396:1361-1378(2010).
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. {ECO:0000255|PROSITE-
CC ProRule:PRU00680}.
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. {ECO:0000269|Ref.3};
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
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 (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 22 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00680}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR PIR; S48641; S48641.
DR PDB; 1EL1; X-ray; 1.90 A; A/B=1-129.
DR PDB; 1I56; NMR; -; A=1-129.
DR PDB; 1QQY; X-ray; 1.85 A; A=1-129.
DR PDB; 2CWI; X-ray; 1.94 A; A/B=1-129.
DR PDB; 2Z2E; X-ray; 2.01 A; A/B=1-129.
DR PDBsum; 1EL1; -.
DR PDBsum; 1I56; -.
DR PDBsum; 1QQY; -.
DR PDBsum; 2CWI; -.
DR PDBsum; 2Z2E; -.
DR AlphaFoldDB; P81708; -.
DR BMRB; P81708; -.
DR SMR; P81708; -.
DR STRING; 9615.ENSCAFP00000013141; -.
DR CAZy; GH22; Glycoside Hydrolase Family 22.
DR PaxDb; P81708; -.
DR eggNOG; ENOG502S1S1; Eukaryota.
DR EvolutionaryTrace; P81708; -.
DR Proteomes; UP000002254; 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; Milk protein; Reference proteome.
FT CHAIN 1..129
FT /note="Lysozyme C, milk isozyme"
FT /id="PRO_0000208845"
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:0007744|PDB:1EL1"
FT BINDING 85
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0007744|PDB:1EL1"
FT BINDING 87
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0007744|PDB:1EL1"
FT BINDING 90
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0007744|PDB:1EL1"
FT BINDING 91
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0007744|PDB:1EL1"
FT DISULFID 6..127
FT DISULFID 30..115
FT DISULFID 65..80
FT DISULFID 76..94
FT HELIX 5..14
FT /evidence="ECO:0007829|PDB:1QQY"
FT HELIX 25..36
FT /evidence="ECO:0007829|PDB:1QQY"
FT STRAND 43..46
FT /evidence="ECO:0007829|PDB:1QQY"
FT STRAND 48..50
FT /evidence="ECO:0007829|PDB:1QQY"
FT STRAND 52..54
FT /evidence="ECO:0007829|PDB:2Z2E"
FT TURN 55..58
FT /evidence="ECO:0007829|PDB:1QQY"
FT TURN 61..64
FT /evidence="ECO:0007829|PDB:1QQY"
FT STRAND 68..70
FT /evidence="ECO:0007829|PDB:1EL1"
FT HELIX 80..84
FT /evidence="ECO:0007829|PDB:1QQY"
FT HELIX 89..98
FT /evidence="ECO:0007829|PDB:1QQY"
FT STRAND 101..103
FT /evidence="ECO:0007829|PDB:1I56"
FT HELIX 104..107
FT /evidence="ECO:0007829|PDB:1QQY"
FT HELIX 109..114
FT /evidence="ECO:0007829|PDB:1QQY"
FT TURN 115..117
FT /evidence="ECO:0007829|PDB:1QQY"
FT TURN 121..126
FT /evidence="ECO:0007829|PDB:1QQY"
SQ SEQUENCE 129 AA; 14471 MW; 64CD8C3F9C80359A CRC64;
KIFSKCELAR KLKSMGMDGF HGYSLANWVC MAEYESNFNT QAFNGRNSNG SSDYGIFQLN
SKWWCKSNSH SSANACNIMC SKFLDDNIDD DIACAKRVVK DPNGMSAWVA WVKHCKGKDL
SKYLASCNL
