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Database: UniProt
Entry: LYSB_DROME
LinkDB: LYSB_DROME
Original site: LYSB_DROME 
ID   LYSB_DROME              Reviewed;         140 AA.
AC   Q08694; P37158; Q9W0J8;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   21-FEB-2001, sequence version 2.
DT   24-JAN-2024, entry version 167.
DE   RecName: Full=Lysozyme B;
DE            EC=3.2.1.17;
DE   AltName: Full=1,4-beta-N-acetylmuramidase B;
DE   Flags: Precursor;
GN   Name=LysB; ORFNames=CG1179;
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).
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.
CC   -!- DEVELOPMENTAL STAGE: Maximal expression is found during the third
CC       larval instar, it drops to become undetectable in the late pupal stage.
CC       The expression in adults is similar to that of first and second larval
CC       instars.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 22 family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00680}.
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DR   EMBL; Z22225; CAA80227.1; -; Genomic_DNA.
DR   EMBL; AE014296; AAF47448.1; -; Genomic_DNA.
DR   PIR; S41574; S41574.
DR   RefSeq; NP_001261245.1; NM_001274316.1.
DR   RefSeq; NP_523882.1; NM_079158.3.
DR   AlphaFoldDB; Q08694; -.
DR   SMR; Q08694; -.
DR   BioGRID; 63671; 2.
DR   DIP; DIP-20169N; -.
DR   STRING; 7227.FBpp0307718; -.
DR   CAZy; GH22; Glycoside Hydrolase Family 22.
DR   PaxDb; 7227-FBpp0072524; -.
DR   DNASU; 38125; -.
DR   EnsemblMetazoa; FBtr0072628; FBpp0072524; FBgn0004425.
DR   EnsemblMetazoa; FBtr0336738; FBpp0307718; FBgn0004425.
DR   GeneID; 38125; -.
DR   KEGG; dme:Dmel_CG1179; -.
DR   AGR; FB:FBgn0004425; -.
DR   CTD; 38125; -.
DR   FlyBase; FBgn0004425; LysB.
DR   VEuPathDB; VectorBase:FBgn0004425; -.
DR   eggNOG; ENOG502S1S1; Eukaryota.
DR   GeneTree; ENSGT00940000166760; -.
DR   HOGENOM; CLU_111620_2_1_1; -.
DR   InParanoid; Q08694; -.
DR   OMA; RCQLART; -.
DR   OrthoDB; 5361006at2759; -.
DR   PhylomeDB; Q08694; -.
DR   Reactome; R-DME-5653890; Lactose synthesis.
DR   BioGRID-ORCS; 38125; 0 hits in 3 CRISPR screens.
DR   GenomeRNAi; 38125; -.
DR   PRO; PR:Q08694; -.
DR   Proteomes; UP000000803; Chromosome 3L.
DR   Bgee; FBgn0004425; Expressed in midgut and 14 other cell types or tissues.
DR   ExpressionAtlas; Q08694; 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.
PE   2: Evidence at transcript level;
KW   Antimicrobial; Bacteriolytic enzyme; Disulfide bond; Glycosidase;
KW   Hydrolase; Reference proteome; Signal.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000250"
FT   CHAIN           19..140
FT                   /note="Lysozyme B"
FT                   /id="PRO_0000018510"
FT   DOMAIN          19..140
FT                   /note="C-type lysozyme"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT   ACT_SITE        50
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT   ACT_SITE        68
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT   DISULFID        24..139
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT   DISULFID        45..129
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT   DISULFID        80..96
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT   DISULFID        92..110
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT   CONFLICT        12..13
FT                   /note="LA -> SG (in Ref. 1; CAA80227)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   140 AA;  15612 MW;  70AFA5321857F093 CRC64;
     MKAFIVLVAL ALAAPALGRT MDRCSLAREM SNLGVPRDQL ARWACIAEHE SSYRTGVVGP
     ENYNGSNDYG IFQINDYYWC APPSGRFSYN ECGLSCNALL TDDITHSVRC AQKVLSQQGW
     SAWSTWHYCS GWLPSIDDCF
//
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