ID   LYS_BUFGA               Reviewed;         146 AA.
AC   P85045;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 1.
DT   03-AUG-2022, entry version 45.
DE   RecName: Full=Lysozyme C;
DE            EC=3.2.1.17;
DE   AltName: Full=1,4-beta-N-acetylmuramidase C;
DE   Flags: Precursor; Fragment;
OS   Bufo gargarizans andrewsi (Andrew's toad) (Bufo andrewsi).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Neobatrachia; Hyloidea; Bufonidae; Bufo.
OX   NCBI_TaxID=61428;
RN   [1] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 17-33, FUNCTION, CATALYTIC
RP   ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, AND TISSUE
RP   SPECIFICITY.
RC   TISSUE=Skin secretion {ECO:0000269|PubMed:16309969};
RX   PubMed=16309969; DOI=10.1016/j.cbpc.2005.10.001;
RA   Zhao Y., Jin Y., Lee W.-H., Zhang Y.;
RT   "Purification of a lysozyme from skin secretions of Bufo andrewsi.";
RL   Comp. Biochem. Physiol. 142C:46-52(2006).
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 antibacterial
CC       activity against the Gram-positive bacterium S.aureus and against the
CC       Gram-negative bacterium E.coli with a MIC of 1 uM and 8 uM
CC       respectively. No antifungal activity against C.albicans.
CC       {ECO:0000255|PROSITE-ProRule:PRU00680, ECO:0000269|PubMed:16309969}.
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:0000269|PubMed:16309969};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 6.0. {ECO:0000269|PubMed:16309969};
CC       Temperature dependence:
CC         Stable from 20 degrees Celsius to 70 degrees Celsius. Activity
CC         decreases sharply above 70 degrees Celsius.
CC         {ECO:0000269|PubMed:16309969};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:16309969}.
CC   -!- TISSUE SPECIFICITY: Expressed by the skin glands.
CC       {ECO:0000269|PubMed:16309969}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 22 family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00680}.
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DR   AlphaFoldDB; P85045; -.
DR   SMR; P85045; -.
DR   PRIDE; P85045; -.
DR   GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR   GO; GO:0003796; F:lysozyme activity; IDA:UniProtKB.
DR   GO; GO:0019835; P:cytolysis; IEA:UniProtKB-KW.
DR   GO; GO:0050829; P:defense response to Gram-negative bacterium; IDA:UniProtKB.
DR   GO; GO:0050830; P:defense response to Gram-positive bacterium; IDA:UniProtKB.
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   1: Evidence at protein level;
KW   Antibiotic; Antimicrobial; Bacteriolytic enzyme; Direct protein sequencing;
KW   Disulfide bond; Glycosidase; Hydrolase; Secreted; Signal.
FT   SIGNAL          <1..16
FT                   /evidence="ECO:0000269|PubMed:16309969"
FT   CHAIN           17..146
FT                   /note="Lysozyme C"
FT                   /evidence="ECO:0000269|PubMed:16309969"
FT                   /id="PRO_0000271190"
FT   DOMAIN          17..146
FT                   /note="C-type lysozyme"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT   ACT_SITE        51
FT                   /evidence="ECO:0000250|UniProtKB:P00702,
FT                   ECO:0000255|PROSITE-ProRule:PRU00680"
FT   ACT_SITE        69
FT                   /evidence="ECO:0000250|UniProtKB:P00702,
FT                   ECO:0000255|PROSITE-ProRule:PRU00680"
FT   DISULFID        22..144
FT                   /evidence="ECO:0000250|UniProtKB:P00702,
FT                   ECO:0000255|PROSITE-ProRule:PRU00680"
FT   DISULFID        46..132
FT                   /evidence="ECO:0000250|UniProtKB:P00702,
FT                   ECO:0000255|PROSITE-ProRule:PRU00680"
FT   DISULFID        81..97
FT                   /evidence="ECO:0000250|UniProtKB:P00702,
FT                   ECO:0000255|PROSITE-ProRule:PRU00680"
FT   DISULFID        93..111
FT                   /evidence="ECO:0000250|UniProtKB:P00702,
FT                   ECO:0000255|PROSITE-ProRule:PRU00680"
FT   NON_TER         1
FT                   /evidence="ECO:0000303|PubMed:16309969"
SQ   SEQUENCE   146 AA;  16608 MW;  126AA86ED3D01EBB CRC64;
     SGKYISWEDS CSYLQLQKYE RCELAKALKK GGLADFKGYS LENWICTAFH ESGYNTASTN
     YNPPDKSTDY GIFQINSRWW CNDYKTPRSK NTCNIDCKVL LGDDISPAIK CAKRVVSDPN
     GMGAWVAWKK YCKGKNLSQW TQGCKL