ID A0A4W5PCA8_9TELE Unreviewed; 178 AA.
AC A0A4W5PCA8;
DT 18-SEP-2019, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2019, sequence version 1.
DT 28-JAN-2026, entry version 24.
DE RecName: Full=Lysozyme g {ECO:0000256|ARBA:ARBA00016485, ECO:0000256|PIRNR:PIRNR001065};
DE EC=3.2.1.17 {ECO:0000256|ARBA:ARBA00012732, ECO:0000256|PIRNR:PIRNR001065};
OS Hucho hucho (huchen).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Hucho.
OX NCBI_TaxID=62062 {ECO:0000313|Ensembl:ENSHHUP00000061047.1, ECO:0000313|Proteomes:UP000314982};
RN [1] {ECO:0000313|Proteomes:UP000314982}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Macqueen D.J., Gundappa M.K.;
RT "Genome assembly of Danube salmon.";
RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSHHUP00000061047.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [3] {ECO:0000313|Ensembl:ENSHHUP00000061047.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2025) to UniProtKB.
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:0000256|ARBA:ARBA00000632,
CC ECO:0000256|PIRNR:PIRNR001065};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 23 family.
CC {ECO:0000256|ARBA:ARBA00008902, ECO:0000256|PIRNR:PIRNR001065}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR AlphaFoldDB; A0A4W5PCA8; -.
DR Ensembl; ENSHHUT00000063121.1; ENSHHUP00000061047.1; ENSHHUG00000035795.1.
DR GeneTree; ENSGT00390000017614; -.
DR Proteomes; UP000314982; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:TreeGrafter.
DR GO; GO:0003796; F:lysozyme activity; IEA:UniProtKB-UniRule.
DR GO; GO:0050830; P:defense response to Gram-positive bacterium; IEA:TreeGrafter.
DR GO; GO:0031640; P:killing of cells of another organism; IEA:UniProtKB-KW.
DR GO; GO:0009253; P:peptidoglycan catabolic process; IEA:InterPro.
DR CDD; cd01021; GEWL; 1.
DR Gene3D; 1.10.530.10; -; 1.
DR InterPro; IPR002152; Glyco_hydro_23.
DR InterPro; IPR023346; Lysozyme-like_dom_sf.
DR InterPro; IPR008258; Transglycosylase_SLT_dom_1.
DR PANTHER; PTHR31698; LYSOZYME G FAMILY MEMBER; 1.
DR PANTHER; PTHR31698:SF8; LYSOZYME G-RELATED; 1.
DR Pfam; PF01464; SLT; 1.
DR PIRSF; PIRSF001065; Lysozyme_g; 1.
DR PRINTS; PR00749; LYSOZYMEG.
DR SUPFAM; SSF53955; Lysozyme-like; 1.
PE 3: Inferred from homology;
KW Antimicrobial {ECO:0000256|ARBA:ARBA00022529};
KW Bacteriolytic enzyme {ECO:0000256|ARBA:ARBA00022638};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|PIRNR:PIRNR001065};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PIRNR:PIRNR001065};
KW Reference proteome {ECO:0000313|Proteomes:UP000314982};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..178
FT /note="Lysozyme g"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5021418689"
FT DOMAIN 46..154
FT /note="Transglycosylase SLT"
FT /evidence="ECO:0000259|Pfam:PF01464"
FT ACT_SITE 66
FT /evidence="ECO:0000256|PIRSR:PIRSR001065-1"
FT ACT_SITE 79
FT /evidence="ECO:0000256|PIRSR:PIRSR001065-1"
SQ SEQUENCE 178 AA; 19215 MW; ADDC462BB6E3569D CRC64;
VGFENANRMV ITFLFFFAIN HQGVSASHEM AERDLPYVDK YKGRITSAGQ KHGVDPAVLG
GIISRESRGG TGLVNSSGDN GNAHGLMQVD KRCHSPKGAC GSQEHIDQGA QILVGSYSDV
EKKYPHWTKE QKLKGALAAY NMGAGSISSY EQVDAKTTGG DYSNDVAARA QYFKKHGY
//
