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Lysozyme C (EC 3.2.1.17) (1,4-beta-N-acetylmuramidase C)

 LYSC_ORTVE              Reviewed;         129 AA.
P00707;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
21-JUL-1986, sequence version 1.
15-MAR-2017, entry version 85.
RecName: Full=Lysozyme C;
EC=3.2.1.17;
AltName: Full=1,4-beta-N-acetylmuramidase C;
Name=LYZ;
Ortalis vetula (Plain chachalaca) (Penelope vetula).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Cracidae;
Ortalis.
NCBI_TaxID=8984;
[1]
PROTEIN SEQUENCE.
TISSUE=Egg white;
PubMed=940173; DOI=10.1007/BF01738883;
Jolles J., Schoentgen F., Jolles P., Prager E.M., Wilson A.C.;
"Amino acid sequence and immunological properties of chalchalaca egg
white lysozyme.";
J. Mol. Evol. 8:59-78(1976).
-!- FUNCTION: Lysozymes have primarily a bacteriolytic function; those
in tissues and body fluids are associated with the monocyte-
macrophage system and enhance the activity of immunoagents.
-!- CATALYTIC ACTIVITY: Hydrolysis of (1->4)-beta-linkages between N-
acetylmuramic acid and N-acetyl-D-glucosamine residues in a
peptidoglycan and between N-acetyl-D-glucosamine residues in
chitodextrins.
-!- SUBUNIT: Monomer.
-!- SUBCELLULAR LOCATION: Secreted.
-!- MISCELLANEOUS: Lysozyme C is capable of both hydrolysis and
transglycosylation; it shows also a slight esterase activity. It
acts rapidly on both peptide-substituted and unsubstituted
peptidoglycan, and slowly on chitin oligosaccharides.
-!- SIMILARITY: Belongs to the glycosyl hydrolase 22 family.
{ECO:0000255|PROSITE-ProRule:PRU00680}.
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PIR; A00862; LZOVE.
ProteinModelPortal; P00707; -.
SMR; P00707; -.
CAZy; GH22; Glycoside Hydrolase Family 22.
PRIDE; P00707; -.
HOVERGEN; HBG052297; -.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0003796; F:lysozyme activity; IEA:UniProtKB-EC.
GO; GO:0019835; P:cytolysis; IEA:UniProtKB-KW.
GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
GO; GO:0008152; P:metabolic process; IEA:UniProtKB-KW.
CDD; cd00119; LYZ1; 1.
InterPro; IPR001916; Glyco_hydro_22.
InterPro; IPR019799; Glyco_hydro_22_CS.
InterPro; IPR000974; Glyco_hydro_22_lys.
InterPro; IPR023346; Lysozyme-like_dom.
Pfam; PF00062; Lys; 1.
PRINTS; PR00137; LYSOZYME.
PRINTS; PR00135; LYZLACT.
SMART; SM00263; LYZ1; 1.
SUPFAM; SSF53955; SSF53955; 1.
PROSITE; PS00128; LACTALBUMIN_LYSOZYME_1; 1.
PROSITE; PS51348; LACTALBUMIN_LYSOZYME_2; 1.
1: Evidence at protein level;
Antimicrobial; Bacteriolytic enzyme; Direct protein sequencing;
Disulfide bond; Glycosidase; Hydrolase; Secreted.
CHAIN 1 129 Lysozyme C.
/FTId=PRO_0000208869.
ACT_SITE 35 35 {ECO:0000255|PROSITE-ProRule:PRU00680}.
ACT_SITE 52 52 {ECO:0000255|PROSITE-ProRule:PRU00680}.
DISULFID 6 127 {ECO:0000255|PROSITE-ProRule:PRU00680}.
DISULFID 30 115 {ECO:0000255|PROSITE-ProRule:PRU00680}.
DISULFID 64 80 {ECO:0000255|PROSITE-ProRule:PRU00680}.
DISULFID 76 94 {ECO:0000255|PROSITE-ProRule:PRU00680}.
SEQUENCE 129 AA; 14509 MW; 079C91A8C604E218 CRC64;
KIYKRCELAA AMKRYGLDNY RGYSLGNWVC AARYESNYNT QATNRNSNGS TDYGILQINS
RWWCNDGRTP GTKNLCHISC SALMGADIAP SVRCAKRIVS DGDGMNAWVA WRKHCKGTDV
STWIKDCKL


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