ID   LYSC2_ONCMY             Reviewed;         144 AA.
AC   P11941; P83333; Q9DDK3;
DT   01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 2.
DT   27-MAR-2024, entry version 128.
DE   RecName: Full=Lysozyme C II;
DE            EC=3.2.1.17;
DE   AltName: Full=1,4-beta-N-acetylmuramidase C;
DE   AltName: Full=Lysozyme type II;
DE   Flags: Precursor;
OS   Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC   Salmonidae; Salmoninae; Oncorhynchus.
OX   NCBI_TaxID=8022;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Liver;
RX   PubMed=1901095; DOI=10.1007/bf02515392;
RA   Dautingny A., Prager E.M., Pham-Dinh D., Jolles J., Pakdel F., Grinde B.,
RA   Jolles P.;
RT   "cDNA and amino acid sequences of rainbow trout (Oncorhynchus mykiss)
RT   lysozymes and their implications for the evolution of lysozyme and
RT   lactalbumin.";
RL   J. Mol. Evol. 32:187-198(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Kamploop; TISSUE=Kidney;
RX   PubMed=12887175; DOI=10.1081/abio-120020181;
RA   Mitra A., Foster-Frey J., Wells K.D., Rexroad C.E. III, Wall R.J.;
RT   "Molecular characterization of lysozyme type II gene from rainbow trout
RT   (Oncorhynchus mykiss): an evidence of a duplicate gene.";
RL   Anim. Biotechnol. 14:7-12(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Kidney;
RA   Mitra A., Wells K.D., Rexroad C.E. III, Wall R.J.;
RT   "A new genetic variant of lysozyme from rainbow trout.";
RL   Submitted (NOV-2000) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   PROTEIN SEQUENCE OF 16-50.
RX   PubMed=3360007; DOI=10.1111/j.1432-1033.1988.tb13994.x;
RA   Grinde B., Jolles J., Jolles P.;
RT   "Purification and characterization of two lysozymes from rainbow trout
RT   (Salmo gairdneri).";
RL   Eur. J. Biochem. 173:269-273(1988).
RN   [5]
RP   PROTEIN SEQUENCE OF 16-30, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
RP   PROPERTIES, AND MASS SPECTROMETRY.
RC   TISSUE=Skin mucus;
RX   PubMed=15142536; DOI=10.1016/j.cbpc.2004.02.004;
RA   Fernandes J.M.O., Kemp G.D., Smith V.J.;
RT   "Two novel muramidases from skin mucosa of rainbow trout (Oncorhynchus
RT   mykiss).";
RL   Comp. Biochem. Physiol. 138B:53-64(2004).
RN   [6]
RP   X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
RX   PubMed=15299303; DOI=10.1107/s0907444994010929;
RA   Karlsen S., Eliassen B.E., Hansen L.K., Larsen R.L., Riise B.W.,
RA   Smalaas A.O., Hough E., Grinde B.;
RT   "Refined crystal structure of lysozyme from the rainbow trout (Oncorhynchus
RT   mykiss).";
RL   Acta Crystallogr. D 51:354-367(1995).
RN   [7]
RP   X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
RX   PubMed=10089395; DOI=10.1107/s0907444998006623;
RA   Vollan V.B., Hough E., Karlsen S.;
RT   "Structural studies on the binding of 4-methylumbelliferone glycosides of
RT   chitin to rainbow trout lysozyme.";
RL   Acta Crystallogr. D 55:60-66(1999).
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 P.citreus. Has no
CC       antibacterial activity against the Gram negative bacteria E.coli and
CC       Y.ruckeri. Does not have hemolytic activity against trout erythrocytes.
CC       {ECO:0000255|PROSITE-ProRule:PRU00680, ECO:0000269|PubMed:15142536}.
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:15142536};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 4.5-5.5. No activity above pH 8.8.
CC         {ECO:0000269|PubMed:15142536};
CC       Temperature dependence:
CC         Optimum temperature is 33-49 degrees Celsius. Retains 25% of its
CC         maximal activity after heating 10 minutes at 80 degrees Celsius.
CC         {ECO:0000269|PubMed:15142536};
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- MASS SPECTROMETRY: Mass=14252; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:15142536};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 22 family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00680}.
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DR   EMBL; X59491; CAA42084.1; -; mRNA.
DR   EMBL; AF322106; AAG45933.1; -; Genomic_DNA.
DR   EMBL; AF452171; AAL48290.1; -; Genomic_DNA.
DR   EMBL; AF321519; AAG34564.1; -; mRNA.
DR   PIR; I51047; I51047.
DR   RefSeq; NP_001118188.1; NM_001124716.1.
DR   PDB; 1BB6; X-ray; 2.00 A; A=16-144.
DR   PDB; 1BB7; X-ray; 2.00 A; A=16-144.
DR   PDB; 1LMC; X-ray; 2.00 A; A=16-144.
DR   PDB; 1LMN; X-ray; 1.80 A; A=16-144.
DR   PDB; 1LMO; X-ray; 1.80 A; A=16-144.
DR   PDB; 1LMP; X-ray; 2.00 A; A=16-144.
DR   PDB; 1LMQ; X-ray; 1.60 A; A=16-144.
DR   PDBsum; 1BB6; -.
DR   PDBsum; 1BB7; -.
DR   PDBsum; 1LMC; -.
DR   PDBsum; 1LMN; -.
DR   PDBsum; 1LMO; -.
DR   PDBsum; 1LMP; -.
DR   PDBsum; 1LMQ; -.
DR   AlphaFoldDB; P11941; -.
DR   SMR; P11941; -.
DR   CAZy; GH22; Glycoside Hydrolase Family 22.
DR   Ensembl; ENSOMYT00000007960.2; ENSOMYP00000007146.1; ENSOMYG00000003648.2.
DR   Ensembl; ENSOMYT00000007974.2; ENSOMYP00000007157.1; ENSOMYG00000065270.1.
DR   Ensembl; ENSOMYT00000007994.2; ENSOMYP00000007177.2; ENSOMYG00000003648.2.
DR   GeneID; 100136768; -.
DR   KEGG; omy:100136768; -.
DR   CTD; 17105; -.
DR   GeneTree; ENSGT00940000153832; -.
DR   OrthoDB; 5344399at2759; -.
DR   EvolutionaryTrace; P11941; -.
DR   Proteomes; UP000694395; Chromosome 5.
DR   GO; GO:0005615; C:extracellular space; IDA:AgBase.
DR   GO; GO:0003796; F:lysozyme activity; IDA:AgBase.
DR   GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR   GO; GO:0031640; P:killing of cells of another organism; IEA:UniProtKB-KW.
DR   GO; GO:0008152; P:metabolic process; IEA:UniProtKB-KW.
DR   CDD; cd16897; LYZ_C; 1.
DR   Gene3D; 1.10.530.10; -; 1.
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   PANTHER; PTHR11407; LYSOZYME C; 1.
DR   PANTHER; PTHR11407:SF28; LYSOZYME C; 1.
DR   Pfam; PF00062; Lys; 1.
DR   PRINTS; PR00137; LYSOZYME.
DR   PRINTS; PR00135; LYZLACT.
DR   SMART; SM00263; LYZ1; 1.
DR   SUPFAM; SSF53955; Lysozyme-like; 1.
DR   PROSITE; PS00128; GLYCOSYL_HYDROL_F22_1; 1.
DR   PROSITE; PS51348; GLYCOSYL_HYDROL_F22_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Antibiotic; Antimicrobial; Bacteriolytic enzyme;
KW   Direct protein sequencing; Disulfide bond; Glycosidase; Hydrolase;
KW   Secreted; Signal.
FT   SIGNAL          1..15
FT                   /evidence="ECO:0000269|PubMed:15142536,
FT                   ECO:0000269|PubMed:3360007"
FT   CHAIN           16..144
FT                   /note="Lysozyme C II"
FT                   /id="PRO_0000018501"
FT   DOMAIN          16..144
FT                   /note="C-type lysozyme"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT   ACT_SITE        50
FT   ACT_SITE        67
FT   DISULFID        21..142
FT   DISULFID        45..130
FT   DISULFID        79..95
FT   DISULFID        91..109
FT   CONFLICT        94
FT                   /note="R -> H (in Ref. 3; AAG34564)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        101
FT                   /note="A -> D (in Ref. 3; AAG34564)"
FT                   /evidence="ECO:0000305"
FT   HELIX           20..29
FT                   /evidence="ECO:0007829|PDB:1LMQ"
FT   HELIX           40..51
FT                   /evidence="ECO:0007829|PDB:1LMQ"
FT   STRAND          58..60
FT                   /evidence="ECO:0007829|PDB:1LMQ"
FT   STRAND          66..68
FT                   /evidence="ECO:0007829|PDB:1LMQ"
FT   TURN            69..72
FT                   /evidence="ECO:0007829|PDB:1LMQ"
FT   TURN            75..77
FT                   /evidence="ECO:0007829|PDB:1LMQ"
FT   HELIX           95..98
FT                   /evidence="ECO:0007829|PDB:1LMQ"
FT   STRAND          99..102
FT                   /evidence="ECO:0007829|PDB:1LMQ"
FT   HELIX           104..113
FT                   /evidence="ECO:0007829|PDB:1LMQ"
FT   HELIX           119..122
FT                   /evidence="ECO:0007829|PDB:1LMQ"
FT   HELIX           124..129
FT                   /evidence="ECO:0007829|PDB:1LMQ"
FT   TURN            130..132
FT                   /evidence="ECO:0007829|PDB:1LMQ"
FT   HELIX           136..138
FT                   /evidence="ECO:0007829|PDB:1LMQ"
FT   TURN            139..141
FT                   /evidence="ECO:0007829|PDB:1LMQ"
SQ   SEQUENCE   144 AA;  15737 MW;  BF945ADCDCC2D668 CRC64;
     MRAVVVLLLV AVASAKVYDR CELARALKAS GMDGYAGNSL PNWVCLSKWE SSYNTQATNR
     NTDGSTDYGI FQINSRYWCD DGRTPGAKNV CGIRCSQLLT ADLTVAIRCA KRVVLDPNGI
     GAWVAWRLHC QNQDLRSYVA GCGV
//