ID A0A034W495_BACDO Unreviewed; 153 AA.
AC A0A034W495;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 28-JAN-2026, entry version 37.
DE RecName: Full=lysozyme {ECO:0000256|ARBA:ARBA00012732};
DE EC=3.2.1.17 {ECO:0000256|ARBA:ARBA00012732};
GN Name=LYS {ECO:0000313|EMBL:JAC48950.1};
GN Synonyms=LOC105233408 {ECO:0000313|RefSeq:XP_011213791.1};
OS Bactrocera dorsalis (Oriental fruit fly) (Dacus dorsalis).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Tephritoidea;
OC Tephritidae; Bactrocera; Bactrocera.
OX NCBI_TaxID=27457 {ECO:0000313|EMBL:JAC48950.1};
RN [1] {ECO:0000313|EMBL:JAC48950.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Punador {ECO:0000313|EMBL:JAC48950.1};
RX PubMed=25348373; DOI=10.1186/1471-2164-15-942;
RA Geib S.M., Calla B., Hall B., Hou S., Manoukis N.C.;
RT "Characterizing the developmental transcriptome of the oriental fruit fly,
RT Bactrocera dorsalis (Diptera: Tephritidae) through comparative genomic
RT analysis with Drosophila melanogaster utilizing modENCODE datasets.";
RL BMC Genomics 15:942-942(2014).
RN [2] {ECO:0000313|RefSeq:XP_011213791.1}
RP IDENTIFICATION.
RC STRAIN=Punador {ECO:0000313|RefSeq:XP_011213791.1};
RG RefSeq;
RL Submitted (APR-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};
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DR EMBL; GAKP01010002; JAC48950.1; -; Transcribed_RNA.
DR RefSeq; XP_011213791.1; XM_011215489.2.
DR AlphaFoldDB; A0A034W495; -.
DR GeneID; 105233408; -.
DR KEGG; bdr:105233408; -.
DR OMA; YDFAAIH; -.
DR OrthoDB; 6337871at2759; -.
DR Proteomes; UP001652620; Chromosome 3.
DR GO; GO:0003796; F:lysozyme activity; IEA:UniProtKB-EC.
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 CDD; cd16890; lyz_i; 1.
DR FunFam; 1.10.530.10:FF:000019; lysozyme; 1.
DR Gene3D; 1.10.530.10; -; 1.
DR InterPro; IPR008597; Invert_lysozyme.
DR PANTHER; PTHR11195; DESTABILASE-RELATED; 1.
DR PANTHER; PTHR11195:SF22; LYSOZYME; 1.
DR Pfam; PF05497; Destabilase; 1.
DR PROSITE; PS51909; LYSOZYME_I; 1.
PE 4: Predicted;
KW Antimicrobial {ECO:0000256|ARBA:ARBA00022529};
KW Bacteriolytic enzyme {ECO:0000256|ARBA:ARBA00022638};
KW Disulfide bond {ECO:0000256|PIRSR:PIRSR608597-3};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP001652620};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..153
FT /note="lysozyme"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5044537735"
FT DISULFID 34..118
FT /evidence="ECO:0000256|PIRSR:PIRSR608597-3"
FT DISULFID 39..45
FT /evidence="ECO:0000256|PIRSR:PIRSR608597-3"
FT DISULFID 88..94
FT /evidence="ECO:0000256|PIRSR:PIRSR608597-3"
SQ SEQUENCE 153 AA; 16609 MW; 539096F5CBEB20AA CRC64;
MANTYYGKYL IAALLCVGFA MLINAQEKPV TDICLGCICE AISGCNRTAT CTGGVCGLFR
ITWPYWSDGG KLTLNGESPD SETAYPNCVN DPYCAANTIQ NYMTKYAQDC NGDNQVDCFD
YAAIHKLGGY GCKGELGYNY QTTLSNCLNL FQG
//
