LYSC_TRASA
ID LYSC_TRASA Reviewed; 129 AA.
AC Q7LZI3;
DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 25-MAY-2022, entry version 65.
DE RecName: Full=Lysozyme C;
DE EC=3.2.1.17;
DE AltName: Full=1,4-beta-N-acetylmuramidase C;
GN Name=LYZ;
OS Tragopan satyra (Satyr tragopan) (Meleagris satyra).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Tragopan.
OX NCBI_TaxID=9070;
RN [1]
RP PROTEIN SEQUENCE.
RA Araki T., Kusao T., Torikata T.;
RT "Description of the amino acid sequence of satyr tragopan lysozyme.";
RL Submitted (JAN-2003) to the PIR 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. {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 -!- SUBUNIT: Monomer. {ECO:0000250}.
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; JC7908; JC7908.
DR AlphaFoldDB; Q7LZI3; -.
DR SMR; Q7LZI3; -.
DR PRIDE; Q7LZI3; -.
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 Antimicrobial; Bacteriolytic enzyme; Direct protein sequencing;
KW Disulfide bond; Glycosidase; Hydrolase; Secreted.
FT CHAIN 1..129
FT /note="Lysozyme C"
FT /id="PRO_0000208874"
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 52
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
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 129 AA; 14229 MW; CE05CFE0E944849B CRC64;
KVYGRCELAA AMKRLGLDNY RGYSLGNWVC AAKFESNFNT HATNRNTDGS TDYGILQINS
RWWCNDGRTP GSRNLCNIPC SALLSSDITA SVNCAKKIVS GGSGMNAWVA WRNRCKGTDV
QAWIRGCRL
