LYSC_PYGNE
ID LYSC_PYGNE Reviewed; 148 AA.
AC P79847;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 25-MAY-2022, entry version 84.
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; Synonyms=LZM;
OS Pygathrix nemaeus (Red-shanked douc langur).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Colobinae; Pygathrix.
OX NCBI_TaxID=54133;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Blood;
RX PubMed=8990116; DOI=10.1038/385151a0;
RA Messier W., Stewart C.B.;
RT "Episodic adaptive evolution of primate lysozymes.";
RL Nature 385:151-154(1997).
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 {ECO:0000250}.
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 EMBL; U76944; AAB41217.1; -; Genomic_DNA.
DR EMBL; U76941; AAB41217.1; JOINED; Genomic_DNA.
DR EMBL; U76942; AAB41217.1; JOINED; Genomic_DNA.
DR EMBL; U76943; AAB41217.1; JOINED; Genomic_DNA.
DR AlphaFoldDB; P79847; -.
DR SMR; P79847; -.
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; 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 3: Inferred from homology;
KW Antimicrobial; Bacteriolytic enzyme; Disulfide bond; Glycosidase;
KW Hydrolase; Secreted; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000250"
FT CHAIN 19..148
FT /note="Lysozyme C"
FT /id="PRO_0000018483"
FT DOMAIN 19..148
FT /note="C-type lysozyme"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT ACT_SITE 53
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT ACT_SITE 71
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT DISULFID 24..146
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT DISULFID 48..134
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT DISULFID 83..99
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT DISULFID 95..113
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
SQ SEQUENCE 148 AA; 16217 MW; D2D0D48A499370B6 CRC64;
MKALIILGLV LLSVTVQGKI FERCELARTL KKLGLDGYKG VSLANWVCLA KWESGYNTEA
TNYNPGDEST DYGIFQINSR YWCNNGKTPG AVDACHISCS ALLQNNIADA VACAKRVVSD
PQGVRAWVAW RNHCQNKDVS QYVKGCGV
