LYSC_DRONO
ID LYSC_DRONO Reviewed; 147 AA.
AC G3XDT7;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 03-AUG-2022, entry version 31.
DE RecName: Full=Lysozyme C {ECO:0000312|EMBL:BAL03622.1};
DE EC=3.2.1.17 {ECO:0000250|UniProtKB:P00698};
DE AltName: Full=1,4-beta-N-acetylmuramidase C {ECO:0000250|UniProtKB:P00698};
DE Flags: Precursor;
OS Dromaius novaehollandiae (Emu).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Palaeognathae; Casuariiformes; Dromaiidae; Dromaius.
OX NCBI_TaxID=8790;
RN [1] {ECO:0000305, ECO:0000312|EMBL:BAL03622.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RC TISSUE=Muscle {ECO:0000269|PubMed:22044478}, and
RC Oviduct {ECO:0000312|EMBL:BAL03622.1};
RX PubMed=22044478; DOI=10.1016/j.gene.2011.10.021;
RA Maehashi K., Matano M., Irisawa T., Uchino M., Kashiwagi Y., Watanabe T.;
RT "Molecular characterization of goose- and chicken-type lysozymes in emu
RT (Dromaius novaehollandiae): evidence for extremely low lysozyme levels in
RT emu egg white.";
RL Gene 492:244-249(2012).
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. Has bacteriolytic
CC activity against M.luteus. {ECO:0000255|PROSITE-ProRule:PRU00680,
CC ECO:0000269|PubMed:22044478}.
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; Evidence={ECO:0000250|UniProtKB:P00698};
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:P00698}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P00698}.
CC -!- TISSUE SPECIFICITY: Expressed in liver and ovary. Not expressed in bone
CC marrow, lung, spleen, intestine or oviduct.
CC {ECO:0000269|PubMed:22044478}.
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 (By similarity).
CC {ECO:0000250|UniProtKB:P00698}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 22 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00680}.
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DR EMBL; AB513676; BAL03621.1; -; Genomic_DNA.
DR EMBL; AB513854; BAL03622.1; -; mRNA.
DR AlphaFoldDB; G3XDT7; -.
DR SMR; G3XDT7; -.
DR CAZy; GH22; Glycoside Hydrolase Family 22.
DR Ensembl; ENSDNVT00000022564; ENSDNVP00000018735; ENSDNVG00000013082.
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 2: Evidence at transcript level;
KW Antimicrobial; Bacteriolytic enzyme; Disulfide bond; Glycosidase;
KW Hydrolase; Secreted; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..147
FT /note="Lysozyme C"
FT /evidence="ECO:0000255"
FT /id="PRO_5000795993"
FT DOMAIN 19..147
FT /note="C-type lysozyme"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT ACT_SITE 53
FT /evidence="ECO:0000250|UniProtKB:P00698,
FT ECO:0000255|PROSITE-ProRule:PRU00680"
FT ACT_SITE 70
FT /evidence="ECO:0000250|UniProtKB:P00698,
FT ECO:0000255|PROSITE-ProRule:PRU00680"
FT BINDING 119
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00698"
FT DISULFID 24..145
FT /evidence="ECO:0000250|UniProtKB:P00698,
FT ECO:0000255|PROSITE-ProRule:PRU00680"
FT DISULFID 48..133
FT /evidence="ECO:0000250|UniProtKB:P00698,
FT ECO:0000255|PROSITE-ProRule:PRU00680"
FT DISULFID 82..98
FT /evidence="ECO:0000250|UniProtKB:P00698,
FT ECO:0000255|PROSITE-ProRule:PRU00680"
FT DISULFID 94..112
FT /evidence="ECO:0000250|UniProtKB:P00698,
FT ECO:0000255|PROSITE-ProRule:PRU00680"
SQ SEQUENCE 147 AA; 16443 MW; F771E0B42235C110 CRC64;
MKFFLILGFC LLPLIAQGKV FQRCELAAAM KKHGLSNYRG YSLGHWVCAA KYESNFNTAA
INRNRDGSSD YGILQINSRW WCNDGRTSGA KNLCKISCSA LLSSDITASV NCAKRVVSDK
NGMNAWVAWR NHCKGRDVSQ WIRGCRV
