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   16-JUN-2009, entry version 77.
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; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha;
OC   Ephydroidea; Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7227;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Canton-S;
RX   MEDLINE=94211204; 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
RT   family 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   MEDLINE=20196006; 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.,
RA   Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D.,
RA   Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G.,
RA   Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D.,
RA   Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M.,
RA   Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S.,
RA   Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P.,
RA   Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I.,
RA   Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P.,
RA   de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M.,
RA   Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P.,
RA   Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W.,
RA   Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K.,
RA   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.,
RA   Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C.,
RA   Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A.,
RA   Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z.,
RA   Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X.,
RA   Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D.,
RA   Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A.,
RA   Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L.,
RA   Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M.,
RA   Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G.,
RA   Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H.,
RA   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.,
RA   Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X.,
RA   Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J.,
RA   Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A.,
RA   Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L.,
RA   Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X.,
RA   Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
RT   "The genome sequence of Drosophila melanogaster.";
RL   Science 287:2185-2195(2000).
RN   [3]
RP   GENOME REANNOTATION.
RX   MEDLINE=22426069; PubMed=12537572;
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.,
RA   Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M.,
RA   Lewis S.E.;
RT   "Annotation of the Drosophila melanogaster euchromatic genome: a
RT   systematic 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
CC       food.
CC   -!- CATALYTIC ACTIVITY: Hydrolysis of (1->4)-beta-linkages between N-
CC       acetylmuramic acid and N-acetyl-D-glucosamine residues in a
CC       peptidoglycan and between N-acetyl-D-glucosamine residues in
CC       chitodextrins.
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
CC       stage. The expression in adults is similar to that of first and
CC       second larval instars.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 22 family.
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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_523882.1; -.
DR   UniGene; Dm.23958; -.
DR   HSSP; P00695; 1LZ5.
DR   SMR; Q08694; 19-140.
DR   DIP; DIP:20169N; -.
DR   IntAct; Q08694; 2.
DR   CAZy; GH22; Glycoside Hydrolase Family 22.
DR   Ensembl; FBgn0004425; Drosophila melanogaster.
DR   GeneID; 38125; -.
DR   KEGG; dme:Dmel_CG1179; -.
DR   FlyBase; FBgn0004425; LysB.
DR   HOGENOM; Q08694; -.
DR   OMA; Q08694; DTSALNK.
DR   BioCyc; DMEL-XXX-02:DMEL-XXX-02-014578-MON; -.
DR   BRENDA; 3.2.1.17; 48.
DR   NextBio; 807090; -.
DR   GermOnline; CG1179; Drosophila melanogaster.
DR   GO; GO:0003796; F:lysozyme activity; IEA:EC.
DR   GO; GO:0016998; P:cell wall macromolecule catabolic process; IEA:InterPro.
DR   GO; GO:0019835; P:cytolysis; IEA:UniProtKB-KW.
DR   GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR   InterPro; IPR001916; Glyco_hydro_22.
DR   InterPro; IPR019799; Glyco_hydro_22_CS.
DR   InterPro; IPR000974; Glyco_hydro_22_lys.
DR   Pfam; PF00062; Lys; 1.
DR   PRINTS; PR00137; LYSOZYME.
DR   PRINTS; PR00135; LYZLACT.
DR   SMART; SM00263; LYZ1; 1.
DR   PROSITE; PS00128; LACTALBUMIN_LYSOZYME_1; 1.
DR   PROSITE; PS51348; LACTALBUMIN_LYSOZYME_2; 1.
PE   2: Evidence at transcript level;
KW   Antimicrobial; Bacteriolytic enzyme; Complete proteome;
KW   Disulfide bond; Glycosidase; Hydrolase; Signal.
FT   SIGNAL        1     18       By similarity.
FT   CHAIN        19    140       Lysozyme B.
FT                                /FTId=PRO_0000018510.
FT   ACT_SITE     50     50       By similarity.
FT   ACT_SITE     68     68       By similarity.
FT   DISULFID     24    139       By similarity.
FT   DISULFID     45    129       By similarity.
FT   DISULFID     80     96       By similarity.
FT   DISULFID     92    110       By similarity.
FT   CONFLICT     12     13       LA -> SG (in Ref. 1; CAA80227).
SQ   SEQUENCE   140 AA;  15612 MW;  70AFA5321857F093 CRC64;
     MKAFIVLVAL ALAAPALGRT MDRCSLAREM SNLGVPRDQL ARWACIAEHE SSYRTGVVGP
     ENYNGSNDYG IFQINDYYWC APPSGRFSYN ECGLSCNALL TDDITHSVRC AQKVLSQQGW
     SAWSTWHYCS GWLPSIDDCF
//