LYSX_DROME
ID LYSX_DROME Reviewed; 142 AA.
AC P37161; A4V9W9; A4V9X0; A4V9X1; A4V9X2; Q9W0K1;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 2.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Lysozyme X;
DE EC=3.2.1.17;
DE AltName: Full=1,4-beta-N-acetylmuramidase X;
DE Flags: Precursor;
GN Name=LysX; ORFNames=CG9120;
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], AND VARIANTS THR-6; LEU-78 AND GLY-94.
RC STRAIN=G02, G130, G140, and G28;
RX PubMed=17465907; DOI=10.1111/j.1420-9101.2007.01305.x;
RA Jiggins F.M., Kim K.W.;
RT "A screen for immunity genes evolving under positive selection in
RT Drosophila.";
RL J. Evol. Biol. 20:965-970(2007).
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).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 62-142.
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).
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 May be involved in the clearance of bacteria from the larval gut before
CC metamorphosis.
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: Rises dramatically in the late third instar, then
CC decreases gradually during the pupal stages. Low expression is found in
CC adults.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 22 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00680}.
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DR EMBL; AM412869; CAL85492.1; -; Genomic_DNA.
DR EMBL; AM412870; CAL85493.1; -; Genomic_DNA.
DR EMBL; AM412871; CAL85494.1; -; Genomic_DNA.
DR EMBL; AM412872; CAL85495.1; -; Genomic_DNA.
DR EMBL; AE014296; AAF47445.1; -; Genomic_DNA.
DR EMBL; AY119081; AAM50941.1; -; mRNA.
DR EMBL; Z22224; CAA80226.1; -; mRNA.
DR PIR; S41580; S41580.
DR RefSeq; NP_523881.1; NM_079157.2.
DR AlphaFoldDB; P37161; -.
DR SMR; P37161; -.
DR BioGRID; 63669; 1.
DR DIP; DIP-24095N; -.
DR STRING; 7227.FBpp0072533; -.
DR CAZy; GH22; Glycoside Hydrolase Family 22.
DR PaxDb; P37161; -.
DR DNASU; 38122; -.
DR EnsemblMetazoa; FBtr0072637; FBpp0072533; FBgn0004431.
DR GeneID; 38122; -.
DR KEGG; dme:Dmel_CG9120; -.
DR CTD; 38122; -.
DR FlyBase; FBgn0004431; LysX.
DR VEuPathDB; VectorBase:FBgn0004431; -.
DR eggNOG; ENOG502S1S1; Eukaryota.
DR GeneTree; ENSGT00940000166760; -.
DR HOGENOM; CLU_111620_2_1_1; -.
DR InParanoid; P37161; -.
DR OMA; GCGVSCK; -.
DR OrthoDB; 1551203at2759; -.
DR PhylomeDB; P37161; -.
DR Reactome; R-DME-5653890; Lactose synthesis.
DR BioGRID-ORCS; 38122; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 38122; -.
DR PRO; PR:P37161; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0004431; Expressed in adult midgut (Drosophila) and 13 other tissues.
DR ExpressionAtlas; P37161; baseline and differential.
DR Genevisible; P37161; DM.
DR GO; GO:0005615; C:extracellular space; ISS:FlyBase.
DR GO; GO:0003796; F:lysozyme activity; ISS:FlyBase.
DR GO; GO:0019835; P:cytolysis; IEA:UniProtKB-KW.
DR GO; GO:0050829; P:defense response to Gram-negative bacterium; ISS:FlyBase.
DR GO; GO:0008152; P:metabolic process; IEA:UniProtKB-KW.
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; Bacteriolytic enzyme; Disulfide bond; Glycosidase;
KW Hydrolase; Reference proteome; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..142
FT /note="Lysozyme X"
FT /id="PRO_0000018516"
FT DOMAIN 20..142
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..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"
FT VARIANT 6
FT /note="G -> T (in strain: G140)"
FT /evidence="ECO:0000269|PubMed:17465907"
FT VARIANT 78
FT /note="M -> L (in strain: Canton-S, G02, G130 and G140)"
FT /evidence="ECO:0000269|PubMed:17465907"
FT VARIANT 94
FT /note="D -> G (in strain: G130 and G140)"
FT /evidence="ECO:0000269|PubMed:17465907"
SQ SEQUENCE 142 AA; 15591 MW; 2A48035364B995BC CRC64;
MRALLGICVL ALVTPAVLGR TMDRCSLARE MANMGVSRDQ LSKWACIAEH ESSYRTGVVG
PPNTDGSNDY GIFQINDMYW CQPSSGKFSH NGCDVSCNAL LTDDIKSSVR CALKVLGQQG
WSAWSTWHYC SGYLPPIDDC FV
