ID   PGPLB_DROME             Reviewed;         232 AA.
AC   Q8INK6; Q9VGN3;
DT   10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   24-JAN-2024, entry version 149.
DE   RecName: Full=Peptidoglycan-recognition protein LB;
DE            EC=3.5.1.28;
DE   Flags: Precursor;
GN   Name=PGRP-LB; ORFNames=CG14704;
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 [MRNA] (ISOFORM A), TISSUE SPECIFICITY, DEVELOPMENTAL
RP   STAGE, AND INDUCTION.
RX   PubMed=11106397; DOI=10.1073/pnas.97.25.13772;
RA   Werner T., Liu G., Kang D., Ekengren S., Steiner H., Hultmark D.;
RT   "A family of peptidoglycan recognition proteins in the fruit fly Drosophila
RT   melanogaster.";
RL   Proc. Natl. Acad. Sci. U.S.A. 97:13772-13777(2000).
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, AND ALTERNATIVE SPLICING.
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] (ISOFORM A).
RC   STRAIN=Berkeley; TISSUE=Embryo;
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 [LARGE SCALE MRNA] (ISOFORM C).
RC   STRAIN=Berkeley; TISSUE=Embryo;
RA   Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Pacleb J.M.,
RA   Park S., Wan K.H., Yu C., Rubin G.M., Celniker S.E.;
RL   Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   INDUCTION.
RX   PubMed=12032070; DOI=10.1093/emboj/21.11.2568;
RA   De Gregorio E., Spellman P.T., Tzou P., Rubin G.M., Lemaitre B.;
RT   "The Toll and Imd pathways are the major regulators of the immune response
RT   in Drosophila.";
RL   EMBO J. 21:2568-2579(2002).
RN   [7]
RP   X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 1-215 (ISOFORM A) IN COMPLEX WITH
RP   ZINC, FUNCTION, SUBUNIT, DISULFIDE BOND, AND MUTAGENESIS OF THR-175.
RX   PubMed=12845326; DOI=10.1038/ni952;
RA   Kim M.-S., Byun M., Oh B.-H.;
RT   "Crystal structure of peptidoglycan recognition protein LB from Drosophila
RT   melanogaster.";
RL   Nat. Immunol. 4:787-793(2003).
CC   -!- FUNCTION: N-acetylmuramyl-L-alanine amidase involved in innate immunity
CC       by degrading bacterial peptidoglycans (PGN). Probably plays a scavenger
CC       role by digesting biologically active PGN into biologically inactive
CC       fragments. Has no direct bacteriolytic activity.
CC       {ECO:0000269|PubMed:12845326}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolyzes the link between N-acetylmuramoyl residues and L-
CC         amino acid residues in certain cell-wall glycopeptides.; EC=3.5.1.28;
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000269|PubMed:12845326};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:12845326};
CC   -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:12845326}.
CC   -!- SUBCELLULAR LOCATION: [Isoform C]: Secreted {ECO:0000305}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=C;
CC         IsoId=Q8INK6-1; Sequence=Displayed;
CC       Name=A; Synonyms=B;
CC         IsoId=Q8INK6-2; Sequence=VSP_013593;
CC   -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:11106397}.
CC   -!- DEVELOPMENTAL STAGE: Expressed from old embryos. Expressed in larvae
CC       and adults. {ECO:0000269|PubMed:11106397}.
CC   -!- INDUCTION: Strongly up-regulated by PGN from B.subtilis. Regulated by
CC       the imd/Relish pathway. {ECO:0000269|PubMed:11106397,
CC       ECO:0000269|PubMed:12032070}.
CC   -!- MISCELLANEOUS: [Isoform A]: Does not contain a signal sequence.
CC       {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the N-acetylmuramoyl-L-alanine amidase 2 family.
CC       {ECO:0000305}.
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DR   EMBL; AF207537; AAG23731.1; -; mRNA.
DR   EMBL; AF207538; AAG23732.1; -; mRNA.
DR   EMBL; AE014297; AAF54643.1; -; Genomic_DNA.
DR   EMBL; AE014297; AAN13505.1; -; Genomic_DNA.
DR   EMBL; AY060759; AAL28307.1; -; mRNA.
DR   EMBL; BT011455; AAR99113.1; -; mRNA.
DR   RefSeq; NP_001247053.1; NM_001260124.2. [Q8INK6-2]
DR   RefSeq; NP_001247054.1; NM_001260125.2. [Q8INK6-2]
DR   RefSeq; NP_650079.1; NM_141822.3. [Q8INK6-2]
DR   RefSeq; NP_731575.1; NM_169392.2. [Q8INK6-1]
DR   RefSeq; NP_731576.1; NM_169393.3. [Q8INK6-2]
DR   PDB; 1OHT; X-ray; 2.00 A; A=18-232.
DR   PDB; 7NSX; X-ray; 1.90 A; AAA=18-232.
DR   PDB; 7NSY; X-ray; 1.40 A; AAA/BBB=18-232.
DR   PDB; 7NSZ; X-ray; 1.30 A; AAA=18-232.
DR   PDB; 7NT0; X-ray; 1.80 A; AAA/BBB=18-232.
DR   PDBsum; 1OHT; -.
DR   PDBsum; 7NSX; -.
DR   PDBsum; 7NSY; -.
DR   PDBsum; 7NSZ; -.
DR   PDBsum; 7NT0; -.
DR   AlphaFoldDB; Q8INK6; -.
DR   SMR; Q8INK6; -.
DR   BioGRID; 66511; 5.
DR   IntAct; Q8INK6; 3.
DR   STRING; 7227.FBpp0297234; -.
DR   GlyCosmos; Q8INK6; 1 site, No reported glycans.
DR   GlyGen; Q8INK6; 1 site.
DR   PaxDb; 7227-FBpp0297234; -.
DR   DNASU; 41379; -.
DR   EnsemblMetazoa; FBtr0082396; FBpp0081872; FBgn0037906. [Q8INK6-1]
DR   EnsemblMetazoa; FBtr0082397; FBpp0081873; FBgn0037906. [Q8INK6-2]
DR   EnsemblMetazoa; FBtr0082398; FBpp0081874; FBgn0037906. [Q8INK6-2]
DR   EnsemblMetazoa; FBtr0306098; FBpp0297235; FBgn0037906. [Q8INK6-2]
DR   EnsemblMetazoa; FBtr0306099; FBpp0297236; FBgn0037906. [Q8INK6-2]
DR   GeneID; 41379; -.
DR   KEGG; dme:Dmel_CG14704; -.
DR   AGR; FB:FBgn0037906; -.
DR   CTD; 41379; -.
DR   FlyBase; FBgn0037906; PGRP-LB.
DR   VEuPathDB; VectorBase:FBgn0037906; -.
DR   eggNOG; ENOG502QR3D; Eukaryota.
DR   InParanoid; Q8INK6; -.
DR   OMA; TPECMKS; -.
DR   PhylomeDB; Q8INK6; -.
DR   BioGRID-ORCS; 41379; 0 hits in 3 CRISPR screens.
DR   EvolutionaryTrace; Q8INK6; -.
DR   GenomeRNAi; 41379; -.
DR   PRO; PR:Q8INK6; -.
DR   Proteomes; UP000000803; Chromosome 3R.
DR   Bgee; FBgn0037906; Expressed in adult midgut (Drosophila) and 19 other cell types or tissues.
DR   ExpressionAtlas; Q8INK6; baseline and differential.
DR   GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR   GO; GO:0008745; F:N-acetylmuramoyl-L-alanine amidase activity; IDA:FlyBase.
DR   GO; GO:0042834; F:peptidoglycan binding; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0050830; P:defense response to Gram-positive bacterium; IDA:UniProtKB.
DR   GO; GO:0045087; P:innate immune response; NAS:UniProtKB.
DR   GO; GO:0002814; P:negative regulation of biosynthetic process of antibacterial peptides active against Gram-negative bacteria; IMP:FlyBase.
DR   GO; GO:0061060; P:negative regulation of peptidoglycan recognition protein signaling pathway; IDA:FlyBase.
DR   GO; GO:0009253; P:peptidoglycan catabolic process; IDA:FlyBase.
DR   CDD; cd06583; PGRP; 1.
DR   Gene3D; 3.40.80.10; Peptidoglycan recognition protein-like; 1.
DR   InterPro; IPR036505; Amidase/PGRP_sf.
DR   InterPro; IPR002502; Amidase_domain.
DR   InterPro; IPR017331; Peptidoglycan_recognition.
DR   InterPro; IPR015510; PGRP.
DR   InterPro; IPR006619; PGRP_domain_met/bac.
DR   PANTHER; PTHR11022; PEPTIDOGLYCAN RECOGNITION PROTEIN; 1.
DR   PANTHER; PTHR11022:SF75; PEPTIDOGLYCAN-RECOGNITION PROTEIN LB-RELATED; 1.
DR   Pfam; PF01510; Amidase_2; 1.
DR   PIRSF; PIRSF037945; PGRPs; 1.
DR   SMART; SM00644; Ami_2; 1.
DR   SMART; SM00701; PGRP; 1.
DR   SUPFAM; SSF55846; N-acetylmuramoyl-L-alanine amidase-like; 1.
DR   Genevisible; Q8INK6; DM.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Disulfide bond; Glycoprotein;
KW   Hydrolase; Immunity; Innate immunity; Metal-binding; Reference proteome;
KW   Secreted; Signal; Zinc.
FT   SIGNAL          1..15
FT                   /evidence="ECO:0000255"
FT   CHAIN           16..232
FT                   /note="Peptidoglycan-recognition protein LB"
FT                   /id="PRO_0000023905"
FT   DOMAIN          53..179
FT                   /note="N-acetylmuramoyl-L-alanine amidase"
FT                   /evidence="ECO:0000255"
FT   REGION          213..232
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         59
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000269|PubMed:12845326,
FT                   ECO:0007744|PDB:1OHT"
FT   BINDING         169
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000269|PubMed:12845326,
FT                   ECO:0007744|PDB:1OHT"
FT   BINDING         177
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000269|PubMed:12845326,
FT                   ECO:0007744|PDB:1OHT"
FT   SITE            95
FT                   /note="Essential for zinc hydrate coordination"
FT                   /evidence="ECO:0000303|PubMed:12845326"
FT   CARBOHYD        196
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        67..73
FT                   /evidence="ECO:0000269|PubMed:12845326"
FT   VAR_SEQ         1..17
FT                   /note="Missing (in isoform A)"
FT                   /evidence="ECO:0000303|PubMed:11106397,
FT                   ECO:0000303|PubMed:12537569"
FT                   /id="VSP_013593"
FT   MUTAGEN         175
FT                   /note="T->K: Loss of function."
FT                   /evidence="ECO:0000269|PubMed:12845326"
FT   HELIX           36..38
FT                   /evidence="ECO:0007829|PDB:1OHT"
FT   STRAND          51..60
FT                   /evidence="ECO:0007829|PDB:1OHT"
FT   STRAND          62..64
FT                   /evidence="ECO:0007829|PDB:1OHT"
FT   HELIX           70..86
FT                   /evidence="ECO:0007829|PDB:1OHT"
FT   STRAND          94..99
FT                   /evidence="ECO:0007829|PDB:1OHT"
FT   STRAND          105..109
FT                   /evidence="ECO:0007829|PDB:1OHT"
FT   STRAND          116..118
FT                   /evidence="ECO:0007829|PDB:1OHT"
FT   TURN            119..123
FT                   /evidence="ECO:0007829|PDB:1OHT"
FT   STRAND          124..132
FT                   /evidence="ECO:0007829|PDB:1OHT"
FT   STRAND          135..137
FT                   /evidence="ECO:0007829|PDB:1OHT"
FT   HELIX           141..156
FT                   /evidence="ECO:0007829|PDB:1OHT"
FT   STRAND          159..168
FT                   /evidence="ECO:0007829|PDB:1OHT"
FT   HELIX           169..171
FT                   /evidence="ECO:0007829|PDB:1OHT"
FT   STRAND          173..175
FT                   /evidence="ECO:0007829|PDB:1OHT"
FT   HELIX           180..186
FT                   /evidence="ECO:0007829|PDB:1OHT"
FT   HELIX           195..197
FT                   /evidence="ECO:0007829|PDB:1OHT"
SQ   SEQUENCE   232 AA;  25436 MW;  7BD18D4EC41F021E CRC64;
     MTALGLVLLS MMGYSQHMQQ ANLGDGVATA RLLSRSDWGA RLPKSVEHFQ GPAPYVIIHH
     SYMPAVCYST PDCMKSMRDM QDFHQLERGW NDIGYSFGIG GDGMIYTGRG FNVIGAHAPK
     YNDKSVGIVL IGDWRTELPP KQMLDAAKNL IAFGVFKGYI DPAYKLLGHR QVRDTECPGG
     RLFAEISSWP HFTHINDTEG VSSTTAPVVP HVHPQAAAPQ KPHQSPPAAP KV
//