ID DROS_DROME Reviewed; 64 AA. AC P36193; Q53ZZ5; Q867T5; Q86BV9; Q9V749; DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot. DT 05-OCT-2010, sequence version 2. DT 27-MAR-2024, entry version 148. DE RecName: Full=Drosocin antimicrobial peptides {ECO:0000305}; DE Contains: DE RecName: Full=Drosocin {ECO:0000303|PubMed:8325867}; DE Contains: DE RecName: Full=Buletin {ECO:0000303|PubMed:35730150}; DE AltName: Full=DIM 7 {ECO:0000303|PubMed:9736738}; DE AltName: Full=IM7 {ECO:0000303|PubMed:35730150}; DE Flags: Precursor; GN Name=Dro; ORFNames=CG10816; 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], PROTEIN SEQUENCE OF 22-40, FUNCTION, RP INDUCTION BY BACTERIAL INFECTION, PROTEOLYTIC CLEAVAGE, VARIANT ALA-52, AND RP GLYCOSYLATION AT THR-32. RC STRAIN=Oregon-R; RX PubMed=8325867; DOI=10.1016/s0021-9258(18)82417-6; RA Bulet P., Dimarcq J.-L., Hetru C., Lagueux M., Charlet M., Hegy G., RA van Dorsselaer A., Hoffmann J.A.; RT "A novel inducible antibacterial peptide of Drosophila carries an O- RT glycosylated substitution."; RL J. Biol. Chem. 268:14893-14897(1993). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, RP INDUCTION BY BACTERIAL INFECTION AND LPS, AND VARIANT ALA-52. RC STRAIN=Oregon-R; RX PubMed=8944755; DOI=10.1111/j.1432-1033.1996.00699.x; RA Charlet M., Lagueux M., Reichhart J.-M., Hoffmann D., Braun A., Meister M.; RT "Cloning of the gene encoding the antibacterial peptide drosocin involved RT in Drosophila immunity. Expression studies during the immune response."; RL Eur. J. Biochem. 241:699-706(1996). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ALA-52 AND VAL-64. RC STRAIN=10B, 10C, 10D, 10F, 10G, 10H, 2CPA1, 2CPA103, 2CPA105, 2CPA118, RC 2CPA12, 2CPA122, 2CPA129, 2CPA14, 2CPA43, 2CPA46, 2CPA51, 2CPA7, 8B, RC 8C, 8D, 8E, 8F, 8G, 9A, 9B, 9C, 9D, 9E, 9F, 9G, and 9H; RX PubMed=12716986; DOI=10.1093/molbev/msg109; RA Lazzaro B.P., Clark A.G.; RT "Molecular population genetics of inducible antibacterial peptide genes in RT Drosophila melanogaster."; RL Mol. Biol. Evol. 20:914-923(2003). RN [4] 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 [5] 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 [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=Berkeley; TISSUE=Head; 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 [7] RP SEQUENCE REVISION. RA Carlson J.W., Booth B., Frise E., Park S., Wan K.H., Yu C., Celniker S.E.; RL Submitted (MAY-2009) to the EMBL/GenBank/DDBJ databases. RN [8] RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INDUCTION BY BACTERIA, RP GLYCOSYLATION AT SER-28, AND MASS SPECTROMETRY. RC STRAIN=Oregon-R {ECO:0000303|PubMed:9736738}; RC TISSUE=Hemolymph {ECO:0000303|PubMed:9736738}; RX PubMed=9736738; DOI=10.1073/pnas.95.19.11342; RA Uttenweiler-Joseph S., Moniatte M., Lagueux M., van Dorsselaer A., RA Hoffmann J.A., Bulet P.; RT "Differential display of peptides induced during the immune response of RT Drosophila: a matrix-assisted laser desorption ionization time-of-flight RT mass spectrometry study."; RL Proc. Natl. Acad. Sci. U.S.A. 95:11342-11347(1998). RN [9] RP IDENTIFICATION OF BULETIN, FUNCTION, SUBCELLULAR LOCATION, TISSUE RP SPECIFICITY, INDUCTION BY BACTERIAL INFECTION, PROTEOLYTIC CLEAVAGE, AND RP MASS SPECTROMETRY. RX PubMed=35730150; DOI=10.1098/rspb.2022.0773; RA Hanson M.A., Kondo S., Lemaitre B.; RT "Drosophila immunity: the Drosocin gene encodes two host defence peptides RT with pathogen-specific roles."; RL Proc. R. Soc. B 289:20220773-20220773(2022). RN [10] RP FUNCTION, SUBUNIT, GLYCOSYLATION AT THR-32, AND MUTAGENESIS OF GLY-22; RP PRO-24; PRO-26; TYR-27; SER-28; PRO-29; THR-32; SER-33; HIS-34; PRO-35; RP ARG-36; ILE-38 AND ARG-39. RX PubMed=36997647; DOI=10.1038/s41589-023-01300-x; RA Mangano K., Klepacki D., Ohanmu I., Baliga C., Huang W., Brakel A., RA Krizsan A., Polikanov Y.S., Hoffmann R., Vazquez-Laslop N., Mankin A.S.; RT "Inhibition of translation termination by the antimicrobial peptide RT Drosocin."; RL Nat. Chem. Biol. 0:0-0(2023). RN [11] RP STRUCTURE BY NMR, AND GLYCOSYLATION AT THR-32. RX PubMed=9888811; DOI=10.1021/bi981956d; RA McManus A.M., Otvos L. Jr., Hoffmann R., Craik D.J.; RT "Conformational studies by NMR of the antimicrobial peptide, drosocin, and RT its non-glycosylated derivative: effects of glycosylation on solution RT conformation."; RL Biochemistry 38:705-714(1999). RN [12] {ECO:0000312|PDB:8AKN, ECO:0000312|PDB:8AM9, ECO:0000312|PDB:8ANA} RP STRUCTURE BY ELECTRON MICROSCOPY (2.0 ANGSTROMS) OF 22-40 IN COMPLEX WITH RP E.COLI RIBOSOME COMPLEX AND E.COLI PRFA, FUNCTION, INTERACTION WITH E.COLI RP RIBOSOME COMPLEX AND E.COLI PRFA, GLYCOSYLATION AT THR-32, AND MUTAGENESIS RP OF 28-SER--SER-33; SER-36 AND ARG-39. RX PubMed=36997646; DOI=10.1038/s41589-023-01293-7; RA Koller T.O., Morici M., Berger M., Safdari H.A., Lele D.S., Beckert B., RA Kaur K.J., Wilson D.N.; RT "Structural basis for translation inhibition by the glycosylated drosocin RT peptide."; RL Nat. Chem. Biol. 0:0-0(2023). CC -!- FUNCTION: [Drosocin]: Antibacterial peptide with strong anti-Gram- CC negative bacteria activity (PubMed:8325867). Significantly contributes CC to antibacterial activity against Enterobacter cloacae but not CC Providencia burhodogranariea (PubMed:35730150). Inhibitor of bacterial CC translation machinery that targets translation termination in a CC prfA- or prfB-dependent manner (PubMed:36997646). Binds within the CC nascent peptide exit tunnel of the bacterial large ribosomal subunit, CC potentially interfering with nascent chain translocation that occurs CC post-peptide bond formation (PubMed:36997646, PubMed:36997647). Binds CC prfA/RF1 (and potentially prfB/RF2), trapping it on the ribosome after CC release of the nascent polypeptide chain and preventing further CC translation (PubMed:36997646). The resulting depletion of peptide chain CC release factors further disrupts bacterial translation by preventing CC ribosomal peptide chain release and inducing stop codon readthrough CC (PubMed:36997647). Entry into target Escherichia coli cells requires CC the bacterial peptide antibiotic transporter sbmA (PubMed:36997646). CC {ECO:0000269|PubMed:35730150, ECO:0000269|PubMed:36997646, CC ECO:0000269|PubMed:36997647, ECO:0000269|PubMed:8325867}. CC -!- FUNCTION: [Buletin]: Peptide with significant antibacterial activity CC against Providencia burhodogranariea but not Enterobacter cloacae. CC {ECO:0000269|PubMed:35730150}. CC -!- SUBUNIT: [Drosocin]: Associates with the bacterial 50S ribosomal CC complex, occupying the nascent peptide exit tunnel (PubMed:36997646). CC Interacts with bacterial 23S rRNA; this interaction is direct CC (PubMed:36997646, PubMed:36997647). Interacts with bacterial rplV/50S CC ribosomal protein L22; this interaction is direct (PubMed:36997646, CC PubMed:36997647). Interacts with bacterial prfA/peptide chain release CC factor RF1; while associated with the bacterial 50S ribosomal complex, CC this interaction is direct and traps RF1 on the ribosome, inhibiting CC further translation (PubMed:36997646, PubMed:36997647). CC {ECO:0000269|PubMed:36997646, ECO:0000269|PubMed:36997647}. CC -!- SUBCELLULAR LOCATION: [Drosocin]: Secreted CC {ECO:0000269|PubMed:35730150, ECO:0000269|PubMed:9736738}. CC -!- SUBCELLULAR LOCATION: [Buletin]: Secreted {ECO:0000269|PubMed:35730150, CC ECO:0000269|PubMed:9736738}. CC -!- TISSUE SPECIFICITY: Constitutively expressed in the calyx and oviduct CC of the genital tract of fertilised egg-laying females, but not virgin CC females (PubMed:8944755). Not expressed in male genital tract CC (PubMed:8944755). Inducibly expressed in the fat body (PubMed:8944755). CC {ECO:0000269|PubMed:8944755}. CC -!- TISSUE SPECIFICITY: [Drosocin]: Hemolymph (at protein level). CC {ECO:0000269|PubMed:35730150, ECO:0000269|PubMed:9736738}. CC -!- TISSUE SPECIFICITY: [Buletin]: Hemolymph (at protein level). CC {ECO:0000269|PubMed:35730150, ECO:0000269|PubMed:9736738}. CC -!- DEVELOPMENTAL STAGE: Expressed in larvae and in adults. CC {ECO:0000269|PubMed:8944755}. CC -!- INDUCTION: By bacterial infection and LPS (PubMed:8944755). In 3rd CC instar larvae and both male and female adults expression is detectable CC between 1 and 16 hours after immune challenge, peaking at 6 hours CC (PubMed:8944755). {ECO:0000269|PubMed:8944755}. CC -!- INDUCTION: [Drosocin]: By bacterial infection (at protein level) CC (PubMed:8325867, PubMed:9736738, PubMed:35730150). Detectable in CC hemolymph from 6 hours after immune challenge, levels of expression CC increase for first 24 hours and persist for the following two weeks (at CC protein level) (PubMed:9736738). {ECO:0000269|PubMed:35730150, CC ECO:0000269|PubMed:8325867, ECO:0000269|PubMed:9736738}. CC -!- INDUCTION: [Buletin]: By bacterial infection (at protein level) CC (PubMed:9736738, PubMed:35730150). Detectable in hemolymph from 6 hours CC after immune challenge, levels of expression increase for first 24 CC hours and decrease to undetectable levels in the following 2 to 3 weeks CC (at protein level) (PubMed:9736738). {ECO:0000269|PubMed:35730150, CC ECO:0000269|PubMed:9736738}. CC -!- PTM: Proteolytically cleaved at a pair of basic residues corresponding CC to the RXK/RR optimal cleavage site for furin proteases to produce two CC distinct antibacterial peptides. {ECO:0000269|PubMed:8325867, CC ECO:0000303|PubMed:35730150}. CC -!- PTM: [Drosocin]: O-glycosylated (PubMed:8325867, PubMed:9888811, CC PubMed:9736738). O-glycosylation may be required for efficient uptake CC by target bacterial cells (PubMed:36997646). Monosaccharide CC modification of Thr-32 provides better antibacterial activity than CC disaccharide modification or no modification (PubMed:36997646). O- CC glycosylation of Thr-32 is not essential for antimicrobial activity but CC enhances this activity by mediating interactions with the 23S rRNA and CC increasing the efficiency of translation inhibition (PubMed:8325867, CC PubMed:36997646, PubMed:36997647). {ECO:0000269|PubMed:36997646, CC ECO:0000269|PubMed:36997647, ECO:0000269|PubMed:8325867, CC ECO:0000269|PubMed:9736738, ECO:0000269|PubMed:9888811}. CC -!- MASS SPECTROMETRY: [Drosocin]: Mass=2401.9; Method=MALDI; Note=With CC monosaccharide on Thr-32.; Evidence={ECO:0000269|PubMed:35730150, CC ECO:0000269|PubMed:9736738}; CC -!- MASS SPECTROMETRY: [Drosocin]: Mass=2564.4; Method=MALDI; Note=With CC disaccharide on Ser-28 and Thr-32.; CC Evidence={ECO:0000269|PubMed:35730150, ECO:0000269|PubMed:9736738}; CC -!- MASS SPECTROMETRY: [Buletin]: Mass=2308.1; Method=MALDI; CC Evidence={ECO:0000269|PubMed:35730150, ECO:0000269|PubMed:9736738}; CC -!- MISCELLANEOUS: Unlike many antimicrobial peptides that kill bacteria CC using a lytic mechanism, proline-rich antimicrobial peptides can enter CC the bacterial cell to target intracellular processes. {ECO:0000305}. CC -!- MISCELLANEOUS: 'Buletin' is named after Philippe Bulet, whose dedicated CC efforts in the 1980s-1990s characterized many of the Drosophila CC antimicrobial peptides, including Drosocin. CC {ECO:0000303|PubMed:35730150}. CC -!- SIMILARITY: Belongs to the drosocin family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAM29584.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; 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; Z21942; CAA79936.1; -; Genomic_DNA. DR EMBL; X98416; CAA67062.1; -; Genomic_DNA. DR EMBL; AY224606; AAO72465.1; -; Genomic_DNA. DR EMBL; AY224607; AAO72466.1; -; Genomic_DNA. DR EMBL; AY224608; AAO72467.1; -; Genomic_DNA. DR EMBL; AY224609; AAO72468.1; -; Genomic_DNA. DR EMBL; AY224610; AAO72469.1; -; Genomic_DNA. DR EMBL; AY224611; AAO72470.1; -; Genomic_DNA. DR EMBL; AY224612; AAO72471.1; -; Genomic_DNA. DR EMBL; AY224613; AAO72472.1; -; Genomic_DNA. DR EMBL; AY224614; AAO72473.1; -; Genomic_DNA. DR EMBL; AY224615; AAO72474.1; -; Genomic_DNA. DR EMBL; AY224616; AAO72475.1; -; Genomic_DNA. DR EMBL; AY224617; AAO72476.1; -; Genomic_DNA. DR EMBL; AY224643; AAO72502.1; -; Genomic_DNA. DR EMBL; AY224644; AAO72503.1; -; Genomic_DNA. DR EMBL; AY224645; AAO72504.1; -; Genomic_DNA. DR EMBL; AY224646; AAO72505.1; -; Genomic_DNA. DR EMBL; AY224647; AAO72506.1; -; Genomic_DNA. DR EMBL; AY224648; AAO72507.1; -; Genomic_DNA. DR EMBL; AY224649; AAO72508.1; -; Genomic_DNA. DR EMBL; AY224650; AAO72509.1; -; Genomic_DNA. DR EMBL; AY224651; AAO72510.1; -; Genomic_DNA. DR EMBL; AY224652; AAO72511.1; -; Genomic_DNA. DR EMBL; AY224653; AAO72512.1; -; Genomic_DNA. DR EMBL; AY224654; AAO72513.1; -; Genomic_DNA. DR EMBL; AY224655; AAO72514.1; -; Genomic_DNA. DR EMBL; AY224656; AAO72515.1; -; Genomic_DNA. DR EMBL; AY224657; AAO72516.1; -; Genomic_DNA. DR EMBL; AY224658; AAO72517.1; -; Genomic_DNA. DR EMBL; AY224659; AAO72518.1; -; Genomic_DNA. DR EMBL; AY224660; AAO72519.1; -; Genomic_DNA. DR EMBL; AY224661; AAO72520.1; -; Genomic_DNA. DR EMBL; AY224662; AAO72521.1; -; Genomic_DNA. DR EMBL; AE013599; AAF58216.1; -; Genomic_DNA. DR EMBL; AY113579; AAM29584.2; ALT_INIT; mRNA. DR PIR; S35984; A47103. DR RefSeq; NP_001246324.1; NM_001259395.2. DR RefSeq; NP_523744.1; NM_079020.5. DR PDB; 4EZR; X-ray; 1.90 A; B=33-40. DR PDB; 6Z2P; X-ray; 2.16 A; C=22-40. DR PDB; 6Z2Q; X-ray; 2.35 A; D=22-40. DR PDB; 8AKN; EM; 2.30 A; A=22-40. DR PDB; 8AM9; EM; 2.80 A; A=22-40. DR PDB; 8ANA; EM; 2.00 A; A=22-40. DR PDBsum; 4EZR; -. DR PDBsum; 6Z2P; -. DR PDBsum; 6Z2Q; -. DR PDBsum; 8AKN; -. DR PDBsum; 8AM9; -. DR PDBsum; 8ANA; -. DR AlphaFoldDB; P36193; -. DR SMR; P36193; -. DR STRING; 7227.FBpp0301076; -. DR GlyCosmos; P36193; 2 sites, No reported glycans. DR GlyGen; P36193; 2 sites. DR iPTMnet; P36193; -. DR PaxDb; 7227-FBpp0301076; -. DR DNASU; 36635; -. DR EnsemblMetazoa; FBtr0087436; FBpp0086566; FBgn0010388. DR EnsemblMetazoa; FBtr0309055; FBpp0301076; FBgn0010388. DR GeneID; 36635; -. DR KEGG; dme:Dmel_CG10816; -. DR AGR; FB:FBgn0010388; -. DR CTD; 36635; -. DR FlyBase; FBgn0010388; Dro. DR VEuPathDB; VectorBase:FBgn0010388; -. DR HOGENOM; CLU_2869984_0_0_1; -. DR InParanoid; P36193; -. DR OMA; MLLACIW; -. DR OrthoDB; 3537773at2759; -. DR PhylomeDB; P36193; -. DR BioGRID-ORCS; 36635; 0 hits in 1 CRISPR screen. DR GenomeRNAi; 36635; -. DR PRO; PR:P36193; -. DR Proteomes; UP000000803; Chromosome 2R. DR Bgee; FBgn0010388; Expressed in seminal fluid secreting gland and 15 other cell types or tissues. DR ExpressionAtlas; P36193; baseline and differential. DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB. DR GO; GO:0019731; P:antibacterial humoral response; IEP:FlyBase. DR GO; GO:0006952; P:defense response; IDA:FlyBase. DR GO; GO:0042742; P:defense response to bacterium; TAS:FlyBase. DR GO; GO:0050829; P:defense response to Gram-negative bacterium; IDA:UniProtKB. DR GO; GO:0050830; P:defense response to Gram-positive bacterium; IDA:FlyBase. DR GO; GO:0002213; P:defense response to insect; IEP:FlyBase. DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW. DR GO; GO:0006964; P:positive regulation of biosynthetic process of antibacterial peptides active against Gram-negative bacteria; IDA:UniProtKB. DR GO; GO:0009617; P:response to bacterium; IDA:FlyBase. DR Genevisible; P36193; DM. PE 1: Evidence at protein level; KW 3D-structure; Antibiotic; Antimicrobial; KW Cleavage on pair of basic residues; Direct protein sequencing; KW Glycoprotein; Immunity; Innate immunity; Reference proteome; Secreted; KW Signal. FT SIGNAL 1..19 FT /evidence="ECO:0000255" FT PROPEP 20..21 FT /evidence="ECO:0000269|PubMed:8325867" FT /id="PRO_0000004958" FT PEPTIDE 22..40 FT /note="Drosocin" FT /evidence="ECO:0000269|PubMed:35730150" FT /id="PRO_0000004959" FT PEPTIDE 43..64 FT /note="Buletin" FT /evidence="ECO:0000269|PubMed:35730150" FT /id="PRO_0000458865" FT REGION 32..40 FT /note="Critical for inhibition of translation, possibly due FT to its role in mediating interactions with bacterial 23S FT rRNA and peptide chain release factors" FT /evidence="ECO:0000269|PubMed:36997647" FT SITE 23 FT /note="Critical for inhibition of translation, possibly due FT to its role in mediating the interaction with bacterial 23S FT rRNA" FT /evidence="ECO:0000269|PubMed:36997647" FT SITE 25 FT /note="Critical for inhibition of translation, possibly due FT to its role in mediating the interaction with bacterial 23S FT rRNA" FT /evidence="ECO:0000269|PubMed:36997647" FT SITE 30 FT /note="Critical for inhibition of translation, possibly due FT to its role in mediating the interaction with bacterial 23S FT rRNA and rplV/50S ribosomal protein L22" FT /evidence="ECO:0000269|PubMed:36997646, FT ECO:0000269|PubMed:36997647" FT CARBOHYD 28 FT /note="O-linked (GalNAc...) serine" FT /evidence="ECO:0000269|PubMed:9736738" FT CARBOHYD 32 FT /note="O-linked (GalNAc...) threonine" FT /evidence="ECO:0000269|PubMed:36997646, FT ECO:0000269|PubMed:8325867, ECO:0000269|PubMed:9736738, FT ECO:0000269|PubMed:9888811, ECO:0000312|PDB:8AKN, FT ECO:0000312|PDB:8AM9, ECO:0000312|PDB:8ANA" FT VARIANT 52 FT /note="T -> A (in strain: 2CPA1, 2CPA12, 2CPA51, 2CPA105, FT 2CPA118, 2CPA122, 8B, 8D, 8E, 8F, 8G, 9A, 9B, 9C, 9D, 9E, FT 9F, 9G, 9H, 10B, 10F, 10G, 10H and Oregon-R; required for FT antibacterial activity against Providencia FT burhodogranariea)" FT /evidence="ECO:0000269|PubMed:12716986, FT ECO:0000269|PubMed:35730150, ECO:0000269|PubMed:8325867, FT ECO:0000269|PubMed:8944755" FT VARIANT 64 FT /note="A -> V (in strain: 2CPA51)" FT /evidence="ECO:0000269|PubMed:12716986" FT MUTAGEN 22 FT /note="G->A,K,T: No significant impact on translation FT inhibition efficiency." FT /evidence="ECO:0000269|PubMed:36997647" FT MUTAGEN 24 FT /note="P->K: No significant impact on translation FT inhibition efficiency." FT /evidence="ECO:0000269|PubMed:36997647" FT MUTAGEN 26 FT /note="P->D,N: No significant impact on translation FT inhibition efficiency." FT /evidence="ECO:0000269|PubMed:36997647" FT MUTAGEN 27 FT /note="Y->A,P,Q,R,S: No significant impact on translation FT inhibition efficiency." FT /evidence="ECO:0000269|PubMed:36997647" FT MUTAGEN 28..33 FT /note="SPRPTS->PPRPPP: Significant loss of antimicrobial FT activity." FT /evidence="ECO:0000269|PubMed:36997646" FT MUTAGEN 28 FT /note="S->T: Enhanced translation inhibition efficiency." FT /evidence="ECO:0000269|PubMed:36997647" FT MUTAGEN 29 FT /note="P->H: No significant impact on translation FT inhibition efficiency." FT /evidence="ECO:0000269|PubMed:36997647" FT MUTAGEN 32 FT /note="T->P,R: Significantly enhanced translation FT inhibition efficiency." FT /evidence="ECO:0000269|PubMed:36997647" FT MUTAGEN 33 FT /note="S->G,P: Enhanced translation inhibition efficiency." FT /evidence="ECO:0000269|PubMed:36997647" FT MUTAGEN 34 FT /note="H->F: Enhanced translation inhibition efficiency." FT /evidence="ECO:0000269|PubMed:36997647" FT MUTAGEN 35 FT /note="P->M: Significantly enhanced translation inhibition FT efficiency." FT /evidence="ECO:0000269|PubMed:36997647" FT MUTAGEN 36 FT /note="R->A: Significant loss of translation inhibition FT activity, possibly due to disruption of interaction with FT bacterial 23S rRNA." FT /evidence="ECO:0000269|PubMed:36997646, FT ECO:0000269|PubMed:36997647" FT MUTAGEN 38 FT /note="I->M: Enhanced translation inhibition efficiency." FT /evidence="ECO:0000269|PubMed:36997647" FT MUTAGEN 39 FT /note="R->A: Complete loss of ability to inhibit FT translation, possibly due to disruption of interactions FT with prfA/RF1." FT /evidence="ECO:0000269|PubMed:36997646, FT ECO:0000269|PubMed:36997647" FT MUTAGEN 39 FT /note="R->K: No loss of translation inhibition activity." FT /evidence="ECO:0000269|PubMed:36997646" FT CONFLICT 17 FT /note="G -> A (in Ref. 1; CAA79936, 2; CAA67062 and 3; FT AAO72465/AAO72466/AAO72467/AAO72468/AAO72469/AAO72470/AAO72471/AAO72472/AAO72473/AAO72474/AAO72475/AAO72476/AAO72502/AAO72503/AAO72504/AAO72505/AAO72506/AAO72507/AAO72508/AAO72509/AAO72510/AAO72511/AAO72512/AAO72513/AAO72514/AAO72515/AAO72516/AAO72517/AAO72518/AAO72519/AAO72520/AAO72521)" FT /evidence="ECO:0000305" SQ SEQUENCE 64 AA; 7085 MW; D715F5BA52FDAD17 CRC64; MKFTIVFLLL ACVFAMGVAT PGKPRPYSPR PTSHPRPIRV RREALAIEDH LTQAAIRPPP ILPA //