ID LYSC_CHEMY Reviewed; 130 AA.
AC P84492;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 29-MAR-2005, sequence version 1.
DT 03-MAY-2023, entry version 58.
DE RecName: Full=Lysozyme C;
DE EC=3.2.1.17;
DE AltName: Full=1,4-beta-N-acetylmuramidase C;
GN Name=LYZ;
OS Chelonia mydas (Green sea-turtle) (Chelonia agassizi).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Testudinata; Testudines; Cryptodira; Durocryptodira;
OC Americhelydia; Chelonioidea; Cheloniidae; Chelonia.
OX NCBI_TaxID=8469;
RN [1]
RP PROTEIN SEQUENCE.
RA Araki T., Chijiiwa Y., Okabayashi K., Kawase M., Kamesaki M., Torikata T.;
RL Submitted (MAR-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; JC7918; JC7918.
DR AlphaFoldDB; P84492; -.
DR SMR; P84492; -.
DR eggNOG; ENOG502RZU4; Eukaryota.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0003796; F:lysozyme activity; IEA:UniProtKB-EC.
DR GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR GO; GO:0031640; P:killing of cells of another organism; IEA:UniProtKB-KW.
DR GO; GO:0008152; P:metabolic process; IEA:UniProtKB-KW.
DR CDD; cd16897; LYZ_C; 1.
DR Gene3D; 1.10.530.10; -; 1.
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 PANTHER; PTHR11407; LYSOZYME C; 1.
DR PANTHER; PTHR11407:SF28; LYSOZYME C; 1.
DR Pfam; PF00062; Lys; 1.
DR PRINTS; PR00137; LYSOZYME.
DR PRINTS; PR00135; LYZLACT.
DR SMART; SM00263; LYZ1; 1.
DR SUPFAM; SSF53955; Lysozyme-like; 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..130
FT /note="Lysozyme C"
FT /id="PRO_0000247815"
FT DOMAIN 1..130
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 DISULFID 6..128
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT DISULFID 30..116
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT DISULFID 65..81
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT DISULFID 77..95
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
SQ SEQUENCE 130 AA; 14704 MW; 4CBB271A77565168 CRC64;
KTYERCELAR AMKRLGLDGY WGYSLGHWVC AAKYESNFNT GATNYNPGDQ STDYGILQIN
SRWWCNDGKT PRTKNACKIQ CRELLTADIT ASVNCAKRVV RDPNGMGAWV AWTKNCKGRD
VSPWIRDCGL
//
