ID   LYSS_DROME              Reviewed;         140 AA.
AC   P37160; Q9W0J3;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2000, sequence version 2.
DT   27-MAR-2024, entry version 156.
DE   RecName: Full=Lysozyme S;
DE            EC=3.2.1.17;
DE   AltName: Full=1,4-beta-N-acetylmuramidase S;
DE   Flags: Precursor;
GN   Name=LysS; ORFNames=CG1165;
OS   Drosophila melanogaster (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7227;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Canton-S;
RX   PubMed=8159165; DOI=10.1007/bf00391008;
RA   Daffre S., Kylsten P., Samakovlis C., Hultmark D.;
RT   "The lysozyme locus in Drosophila melanogaster: an expanded gene family
RT   adapted for expression in the digestive tract.";
RL   Mol. Gen. Genet. 242:152-162(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley;
RX   PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA   Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA   Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA   George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA   Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA   Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA   Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA   An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA   Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA   Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA   Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA   Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA   Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA   Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA   Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA   Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA   Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA   Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA   Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA   Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA   Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA   Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA   McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA   Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA   Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA   Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA   Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA   Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA   Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA   Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA   Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA   Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA   Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA   Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA   Venter J.C.;
RT   "The genome sequence of Drosophila melanogaster.";
RL   Science 287:2185-2195(2000).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=Berkeley;
RX   PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA   Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA   Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA   Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA   Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA   Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA   Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT   "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT   review.";
RL   Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Berkeley; TISSUE=Larva, and Pupae;
RX   PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA   Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA   Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA   Celniker S.E.;
RT   "A Drosophila full-length cDNA resource.";
RL   Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
CC   -!- FUNCTION: Unlikely to play an active role in the humoral immune
CC       defense. May have a function in the digestion of bacteria in the food.
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;
CC   -!- TISSUE SPECIFICITY: Found in the midgut, especially the epithelium of
CC       the gastric caeca.
CC   -!- DEVELOPMENTAL STAGE: Expressed only during the larval stage, the
CC       highest level is reached during the third larval instar.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 22 family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00680}.
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DR   EMBL; Z22228; CAA80230.1; -; Genomic_DNA.
DR   EMBL; AE014296; AAF47453.1; -; Genomic_DNA.
DR   EMBL; AY119049; AAM50909.1; -; mRNA.
DR   PIR; S41579; S41579.
DR   RefSeq; NP_476829.1; NM_057481.4.
DR   AlphaFoldDB; P37160; -.
DR   SMR; P37160; -.
DR   STRING; 7227.FBpp0072527; -.
DR   CAZy; GH22; Glycoside Hydrolase Family 22.
DR   PaxDb; 7227-FBpp0072527; -.
DR   DNASU; 38130; -.
DR   EnsemblMetazoa; FBtr0072631; FBpp0072527; FBgn0004430.
DR   GeneID; 38130; -.
DR   KEGG; dme:Dmel_CG1165; -.
DR   AGR; FB:FBgn0004430; -.
DR   CTD; 38130; -.
DR   FlyBase; FBgn0004430; LysS.
DR   VEuPathDB; VectorBase:FBgn0004430; -.
DR   eggNOG; ENOG502S1S1; Eukaryota.
DR   GeneTree; ENSGT00940000166760; -.
DR   HOGENOM; CLU_111620_2_1_1; -.
DR   InParanoid; P37160; -.
DR   OMA; TPYLDGC; -.
DR   PhylomeDB; P37160; -.
DR   Reactome; R-DME-5653890; Lactose synthesis.
DR   BioGRID-ORCS; 38130; 0 hits in 3 CRISPR screens.
DR   GenomeRNAi; 38130; -.
DR   PRO; PR:P37160; -.
DR   Proteomes; UP000000803; Chromosome 3L.
DR   Bgee; FBgn0004430; Expressed in adult Malpighian tubule (Drosophila) and 11 other cell types or tissues.
DR   ExpressionAtlas; P37160; baseline and differential.
DR   GO; GO:0005615; C:extracellular space; ISS:FlyBase.
DR   GO; GO:0003796; F:lysozyme activity; ISS:FlyBase.
DR   GO; GO:0050829; P:defense response to Gram-negative bacterium; ISS:FlyBase.
DR   GO; GO:0031640; P:killing of cells of another organism; IEA:UniProtKB-KW.
DR   GO; GO:0008152; P:metabolic process; IEA:UniProtKB-KW.
DR   CDD; cd16899; LYZ_C_invert; 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:SF36; GEO02684P1-RELATED; 1.
DR   PANTHER; PTHR11407; 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.
DR   Genevisible; P37160; DM.
PE   2: Evidence at transcript level;
KW   Antimicrobial; Bacteriolytic enzyme; Disulfide bond; Glycosidase;
KW   Hydrolase; Reference proteome; Signal.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..140
FT                   /note="Lysozyme S"
FT                   /id="PRO_0000018515"
FT   DOMAIN          20..140
FT                   /note="C-type lysozyme"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT   ACT_SITE        51
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT   ACT_SITE        69
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT   DISULFID        25..139
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT   DISULFID        46..129
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT   DISULFID        81..96
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT   DISULFID        92..110
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT   CONFLICT        11..16
FT                   /note="AIAAPA -> PLPLC (in Ref. 1; CAA80230)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   140 AA;  15652 MW;  ACD139CC656EF8FC CRC64;
     MKAFFALVLL AIAAPALAGR TLDRCSLARE MADLGVPRDQ LDKWTCIAQH ESDYRTWVVG
     PANSDGSNDY GIFQINDLYW CQADGRFSYN ECGLSCNALL TDDITNSVRC AQKVLSQQGW
     SAWAVWHYCS GWLPSIDECF
//