LYSC_COTJA
ID LYSC_COTJA Reviewed; 147 AA.
AC P00701;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 2.
DT 03-AUG-2022, entry version 116.
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 Coturnix japonica (Japanese quail) (Coturnix coturnix japonica).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Perdicinae; Coturnix.
OX NCBI_TaxID=93934;
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.
RX PubMed=5358633;
RA Kaneda M., Kato I., Tominaga N., Titani K., Narita K.;
RT "The amino acid sequence of quail lysozyme.";
RL J. Biochem. 66:747-749(1969).
RN [3]
RP PROTEIN SEQUENCE OF 19-147, AND CATALYTIC ACTIVITY.
RC TISSUE=Egg white;
RA Thammasirirak S., Preecharram S., Phonkham P., Daduang S., Araki T.,
RA Svasti J.;
RT "Quail lysozyme II.";
RL Submitted (SEP-2006) to UniProtKB.
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF 19-147.
RA Houdusse A., Bentley G.A., Poljak R.J., Souchon H., Zhang Z.;
RL Submitted (JUN-1993) to the PDB data bank.
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; Evidence={ECO:0000269|Ref.3};
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; A91922; LZQJE.
DR PIR; JU0237; JU0237.
DR PDB; 2IHL; X-ray; 1.40 A; A=19-147.
DR PDBsum; 2IHL; -.
DR AlphaFoldDB; P00701; -.
DR SMR; P00701; -.
DR CAZy; GH22; Glycoside Hydrolase Family 22.
DR PRIDE; P00701; -.
DR ABCD; P00701; 1 sequenced antibody.
DR EvolutionaryTrace; P00701; -.
DR Proteomes; UP000694412; Unplaced.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0003796; F:lysozyme activity; IEA:UniProtKB-EC.
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 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:5358633, ECO:0000269|Ref.3"
FT CHAIN 19..147
FT /note="Lysozyme C"
FT /id="PRO_0000018496"
FT DOMAIN 19..147
FT /note="C-type lysozyme"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT ACT_SITE 53
FT ACT_SITE 70
FT DISULFID 24..145
FT DISULFID 48..133
FT DISULFID 82..98
FT DISULFID 94..112
FT CONFLICT 39
FT /note="Q -> LK (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT HELIX 23..32
FT /evidence="ECO:0007829|PDB:2IHL"
FT HELIX 43..54
FT /evidence="ECO:0007829|PDB:2IHL"
FT STRAND 61..63
FT /evidence="ECO:0007829|PDB:2IHL"
FT STRAND 69..71
FT /evidence="ECO:0007829|PDB:2IHL"
FT TURN 72..75
FT /evidence="ECO:0007829|PDB:2IHL"
FT TURN 78..80
FT /evidence="ECO:0007829|PDB:2IHL"
FT HELIX 98..102
FT /evidence="ECO:0007829|PDB:2IHL"
FT STRAND 103..105
FT /evidence="ECO:0007829|PDB:2IHL"
FT HELIX 107..116
FT /evidence="ECO:0007829|PDB:2IHL"
FT HELIX 122..125
FT /evidence="ECO:0007829|PDB:2IHL"
FT HELIX 127..132
FT /evidence="ECO:0007829|PDB:2IHL"
FT TURN 133..135
FT /evidence="ECO:0007829|PDB:2IHL"
FT HELIX 138..142
FT /evidence="ECO:0007829|PDB:2IHL"
SQ SEQUENCE 147 AA; 16278 MW; B1D03EDA0E85DED3 CRC64;
MRSLLVLVLC FLPLAALGKV YGRCELAAAM KRHGLDKYQG YSLGNWVCAA KFESNFNTQA
TNRNTDGSTD YGILQINSRW WCNDGRTPGS RNLCNIPCSA LLSSDITASV NCAKKIVSDV
HGMNAWVAWR NRCKGTDVNA WIRGCRL
