ID   LYS1A_LUCSE             Reviewed;         141 AA.
AC   D9J142;
DT   12-SEP-2018, integrated into UniProtKB/Swiss-Prot.
DT   05-OCT-2010, sequence version 1.
DT   25-MAY-2022, entry version 33.
DE   RecName: Full=Inactive lysozyme 1A {ECO:0000305};
DE   Flags: Precursor;
OS   Lucilia sericata (Green bottle fly) (Phaenicia sericata).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Oestroidea;
OC   Calliphoridae; Luciliinae; Lucilia.
OX   NCBI_TaxID=13632 {ECO:0000312|EMBL:ADI87386.1};
RN   [1] {ECO:0000312|EMBL:ADI87386.1}
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Larva {ECO:0000303|PubMed:20542901};
RX   PubMed=20542901; DOI=10.1093/jac/dkq165;
RA   Andersen A.S., Sandvang D., Schnorr K.M., Kruse T., Neve S., Joergensen B.,
RA   Karlsmark T., Krogfelt K.A.;
RT   "A novel approach to the antimicrobial activity of maggot debridement
RT   therapy.";
RL   J. Antimicrob. Chemother. 65:1646-1654(2010).
RN   [2] {ECO:0000305}
RP   FUNCTION, AND TISSUE SPECIFICITY.
RX   PubMed=25098233; DOI=10.1111/imb.12122;
RA   Valachova I., Takac P., Majtan J.;
RT   "Midgut lysozymes of Lucilia sericata - new antimicrobials involved in
RT   maggot debridement therapy.";
RL   Insect Mol. Biol. 23:779-787(2014).
CC   -!- FUNCTION: Shows antibacterial activity against Gram-positive bacterium
CC       M.luteus but shows no activity against Gram-negative bacterium E.coli
CC       (PubMed:25098233). Likely to play a role in the eradication of ingested
CC       pathogens during their passage through the intestine (Probable).
CC       {ECO:0000269|PubMed:25098233, ECO:0000305|PubMed:25098233}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Expressed only in the midgut where it is restricted
CC       to the first half in all larval stages (PubMed:25098233). Expression
CC       initiates at the base of the caeca, proceeds throughout the first half
CC       of the midgut and gradually stops at the middle of the midgut
CC       (PubMed:25098233). {ECO:0000269|PubMed:25098233}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 22 family. {ECO:0000255,
CC       ECO:0000255|PROSITE-ProRule:PRU00680, ECO:0000255|RuleBase:RU004440}.
CC   -!- CAUTION: Although it belongs to the glycosyl hydrolase 22 family, Gly-
CC       51 is present instead of the conserved Glu which is an active site
CC       residue. It is therefore expected that this protein lacks hydrolase
CC       activity. {ECO:0000305}.
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DR   EMBL; HM243538; ADI87386.1; -; mRNA.
DR   AlphaFoldDB; D9J142; -.
DR   SMR; D9J142; -.
DR   CAZy; GH22; Glycoside Hydrolase Family 22.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0003796; F:lysozyme activity; IEA:InterPro.
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; PTHR11407; 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   2: Evidence at transcript level;
KW   Antimicrobial; Disulfide bond; Glycoprotein; Secreted; Signal.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..141
FT                   /note="Inactive lysozyme 1A"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_5003125784"
FT   DOMAIN          20..141
FT                   /note="C-type lysozyme"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT   CARBOHYD        65
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        104
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   DISULFID        25..140
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT   DISULFID        46..130
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT   DISULFID        81..97
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT   DISULFID        93..111
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
SQ   SEQUENCE   141 AA;  15782 MW;  5F919D9B0BA4D63E CRC64;
     MKFFIVLLAA LALFTPAFGK TFTRCSLAKE VYALGVPKSE LPQWTCIAEH GSSYRTNVVG
     PTNSNGSNDY GIFQINNYYW CQPANGRFSY NECKLSCNDL LTDNISNSVK CARKIKSQQG
     WTAWSTWKYC SGSLPSINDC F