LYS2_LUCSE
ID LYS2_LUCSE Reviewed; 142 AA.
AC C0HLB7;
DT 12-SEP-2018, integrated into UniProtKB/Swiss-Prot.
DT 12-SEP-2018, sequence version 1.
DT 25-MAY-2022, entry version 11.
DE RecName: Full=Lysozyme 2 {ECO:0000303|PubMed:25098233};
DE EC=3.2.1.17 {ECO:0000255|PROSITE-ProRule:PRU00680};
DE AltName: Full=1,4-beta-N-acetylmuramidase C {ECO:0000255|PROSITE-ProRule:PRU00680};
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;
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA], AND INDUCTION.
RC TISSUE=Larva {ECO:0000303|PubMed:19076250};
RX PubMed=19076250; DOI=10.1111/j.1365-2583.2008.00856.x;
RA Altincicek B., Vilcinskas A.;
RT "Septic injury-inducible genes in medicinal maggots of the green blow fly
RT Lucilia sericata.";
RL Insect Mol. Biol. 18:119-125(2009).
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: Lysozymes have primarily a bacteriolytic function (Probable).
CC Shows antibacterial activity against Gram-positive bacterium M.luteus
CC 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 -!- 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:0000255|PROSITE-ProRule:PRU00680};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed only in the midgut where it is
CC concentrated around the middle in all larval stages.
CC {ECO:0000269|PubMed:25098233}.
CC -!- INDUCTION: By septic injury caused by dorsolateral puncturing with a
CC needle contaminated with lipopolysaccharide (LPS) solution.
CC {ECO:0000269|PubMed:19076250}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 22 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00680}.
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 EMBL; FG360533; -; NOT_ANNOTATED_CDS; mRNA.
DR AlphaFoldDB; C0HLB7; -.
DR SMR; C0HLB7; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0003796; F:lysozyme activity; IEA:UniProtKB-EC.
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; 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; PS51348; GLYCOSYL_HYDROL_F22_2; 1.
PE 2: Evidence at transcript level;
KW Antimicrobial; Bacteriolytic enzyme; Disulfide bond; Glycoprotein;
KW Glycosidase; Hydrolase; Secreted; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..142
FT /note="Lysozyme 2"
FT /evidence="ECO:0000255"
FT /id="PRO_0000445034"
FT DOMAIN 21..142
FT /note="C-type lysozyme"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT ACT_SITE 52
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT ACT_SITE 70
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT CARBOHYD 66
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 26..141
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT DISULFID 47..131
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT DISULFID 82..98
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT DISULFID 94..112
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
SQ SEQUENCE 142 AA; 15956 MW; D37B4937B3532976 CRC64;
MLKLTLTILA AVLLVTPAFG KVYTRCSLAR EMHTLGVPKN QLARWTCIAE HESAYNTKAV
GSMNSNGSRD YGIFQINNYY WCSPPSGAFS YNECKIKCAD FLVDSIEPAV KCAQLVLRQQ
GWSAWSTWKY CDHTLPSIDD CF
