LYSC2_ONCMY
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 03-AUG-2022, entry version 123.
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; ENSOMYP00000007146; ENSOMYG00000003648.
DR Ensembl; ENSOMYT00000007974; ENSOMYP00000007157; ENSOMYG00000065270.
DR Ensembl; ENSOMYT00000007994; ENSOMYP00000007177; ENSOMYG00000003648.
DR GeneID; 100136768; -.
DR KEGG; omy:100136768; -.
DR CTD; 17105; -.
DR GeneTree; ENSGT00940000153832; -.
DR OrthoDB; 1551203at2759; -.
DR EvolutionaryTrace; P11941; -.
DR GO; GO:0005615; C:extracellular space; IDA:AgBase.
DR GO; GO:0003796; F:lysozyme activity; IDA:AgBase.
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 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
