ID   LYSC_PSEPE              Reviewed;          49 AA.
AC   P21776;
DT   01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1991, sequence version 1.
DT   25-MAY-2022, entry version 87.
DE   RecName: Full=Lysozyme C;
DE            EC=3.2.1.17;
DE   AltName: Full=1,4-beta-N-acetylmuramidase C;
DE   Flags: Fragment;
GN   Name=LYZ;
OS   Pseudocheirus peregrinus (Common ring-tailed possum).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Metatheria; Diprotodontia; Pseudocheiridae; Pseudocheirus.
OX   NCBI_TaxID=9333;
RN   [1]
RP   PROTEIN SEQUENCE.
RC   TISSUE=Milk;
RX   PubMed=2605916; DOI=10.1016/0305-0491(89)90164-8;
RA   Nicholas K.R., Loughnan M., Messer M., Munks S., Griffiths M., Shaw D.;
RT   "Isolation, partial sequence and asynchronous appearance during lactation
RT   of lysozyme and alpha-lactalbumin in the milk of a marsupial, the common
RT   ringtail possum (Pseudocheirus peregrinus).";
RL   Comp. Biochem. Physiol. 94B:775-778(1989).
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;
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; PL0163; PL0163.
DR   AlphaFoldDB; P21776; -.
DR   SMR; P21776; -.
DR   CAZy; GH22; Glycoside Hydrolase Family 22.
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; 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   SUPFAM; SSF53955; SSF53955; 1.
DR   PROSITE; PS51348; GLYCOSYL_HYDROL_F22_2; 1.
PE   1: Evidence at protein level;
KW   Antimicrobial; Bacteriolytic enzyme; Direct protein sequencing;
KW   Glycosidase; Hydrolase; Milk protein; Secreted.
FT   CHAIN           1..>49
FT                   /note="Lysozyme C"
FT                   /id="PRO_0000208854"
FT   DOMAIN          1..>49
FT                   /note="C-type lysozyme"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT   ACT_SITE        35
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT   NON_TER         49
SQ   SEQUENCE   49 AA;  5570 MW;  8F044234322D6C2A CRC64;
     SKMKKCEFAK IAKEQHMDGY HGVSLADWVC LVNNESDFNT KAINRNKGI