PGPLB_DROME
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 03-AUG-2022, entry version 144.
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 GlyGen; Q8INK6; 1 site.
DR PaxDb; Q8INK6; -.
DR PRIDE; Q8INK6; -.
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 CTD; 41379; -.
DR FlyBase; FBgn0037906; PGRP-LB.
DR VEuPathDB; VectorBase:FBgn0037906; -.
DR eggNOG; ENOG502QR3D; Eukaryota.
DR InParanoid; Q8INK6; -.
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 tissues.
DR ExpressionAtlas; Q8INK6; baseline and differential.
DR Genevisible; Q8INK6; DM.
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; -; 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; PTHR11022; 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; SSF55846; 1.
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
