ID A0A060A0J8_XENLA Unreviewed; 153 AA.
AC A0A060A0J8;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 24-JAN-2024, entry version 46.
DE RecName: Full=lysozyme {ECO:0000256|ARBA:ARBA00012732};
DE EC=3.2.1.17 {ECO:0000256|ARBA:ARBA00012732};
GN Name=lyz.L {ECO:0000313|RefSeq:XP_018107197.1,
GN ECO:0000313|Xenbase:XB-GENE-6252020};
GN Synonyms=lyz {ECO:0000313|EMBL:AIA57285.1};
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355 {ECO:0000313|EMBL:AIA57285.1};
RN [1] {ECO:0000313|EMBL:AIA57285.1}
RP NUCLEOTIDE SEQUENCE.
RA Zhao D., Ma L., Yang L., Zhang S.;
RT "Molecular cloning, expression and bioactivity analysis of lysozyme in
RT South African clawed frog, Xenopus laevis.";
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|RefSeq:XP_018107197.1}
RP IDENTIFICATION.
RC STRAIN=J_2021 {ECO:0000313|RefSeq:XP_018107197.1};
RC TISSUE=Erythrocytes {ECO:0000313|RefSeq:XP_018107197.1};
RG RefSeq;
RL Submitted (SEP-2023) 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 -!- SIMILARITY: Belongs to the glycosyl hydrolase 22 family.
CC {ECO:0000256|RuleBase:RU004440}.
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DR EMBL; KJ591621; AIA57285.1; -; mRNA.
DR RefSeq; XP_018107197.1; XM_018251708.1.
DR RefSeq; XP_018107197.1; XM_018251708.2.
DR STRING; 8355.A0A060A0J8; -.
DR PaxDb; 8355-A0A060A0J8; -.
DR GeneID; 443604; -.
DR KEGG; xla:443604; -.
DR CTD; 443604; -.
DR Xenbase; XB-GENE-6252020; lyz.L.
DR OMA; GWRNHCQ; -.
DR OrthoDB; 4825544at2759; -.
DR Proteomes; UP000186698; Chromosome 3L.
DR Bgee; 443604; Expressed in spleen and 15 other cell types or tissues.
DR GO; GO:0003796; F:lysozyme activity; IEA:UniProtKB-EC.
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 2: Evidence at transcript level;
KW Antimicrobial {ECO:0000256|ARBA:ARBA00022529};
KW Bacteriolytic enzyme {ECO:0000256|ARBA:ARBA00022638};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000186698};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..153
FT /note="lysozyme"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5010899096"
FT DOMAIN 96..114
FT /note="Glycosyl hydrolases family 22 (GH22)"
FT /evidence="ECO:0000259|PROSITE:PS00128"
SQ SEQUENCE 153 AA; 17570 MW; 4EED629353AA7134 CRC64;
MNSAVLILVG IFIFPATNGK LFERCELAGT MKKMGLDGYR GYSLPNWVCT AFFESSFYTD
RTNFNRGDNS TDYGILQINS RWWCNDDKTP RSHNACNINC RDLLSDDITQ SVICAKRVVR
DPQGMEAWVG WRNHCKGRDL SQWIKDCKLD ILL
//