ID   PGPSD_DROSI             Reviewed;         186 AA.
AC   Q70PR8; Q6V6G1; Q6V6G3; Q6V6G4; Q6V6G5; Q6V6G7;
DT   10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 65.
DE   RecName: Full=Peptidoglycan-recognition protein SD;
DE   Flags: Precursor;
GN   Name=PGRP-SD;
OS   Drosophila simulans (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7240;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=C167.4;
RX   PubMed=14738318; DOI=10.1007/s00239-003-2506-6;
RA   Jiggins F.M., Hurst G.D.D.;
RT   "The evolution of parasite recognition genes in the innate immune system:
RT   purifying selection on Drosophila melanogaster peptidoglycan recognition
RT   proteins.";
RL   J. Mol. Evol. 57:598-605(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 39-178.
RC   STRAIN=Sim1, Sim2, Sim3, Sim4, Sim5, Sim6, Sim7, and Sim8;
RX   PubMed=12930753; DOI=10.1093/genetics/164.4.1471;
RA   Schlenke T.A., Begun D.J.;
RT   "Natural selection drives Drosophila immune system evolution.";
RL   Genetics 164:1471-1480(2003).
CC   -!- FUNCTION: Peptidoglycan-recognition protein that plays a key role in
CC       innate immunity by binding to peptidoglycans (PGN) of Gram-positive
CC       bacteria and activating the Toll pathway. Has no activity against on
CC       Gram-negative bacteria and fungi. Shows some partial redundancy with
CC       PRPGP-SA in Gram-positive bacteria recognition. May act by activating
CC       the proteolytic cleavage of Spatzle and the subsequent activation of
CC       Toll pathway. Recognizes S.aureus PGN (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the N-acetylmuramoyl-L-alanine amidase 2 family.
CC       {ECO:0000305}.
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DR   EMBL; AJ556634; CAD89199.1; -; Genomic_DNA.
DR   EMBL; AY349823; AAQ64774.1; -; Genomic_DNA.
DR   EMBL; AY349824; AAQ64775.1; -; Genomic_DNA.
DR   EMBL; AY349825; AAQ64776.1; -; Genomic_DNA.
DR   EMBL; AY349826; AAQ64777.1; -; Genomic_DNA.
DR   EMBL; AY349827; AAQ64778.1; -; Genomic_DNA.
DR   EMBL; AY349828; AAQ64779.1; -; Genomic_DNA.
DR   EMBL; AY349829; AAQ64780.1; -; Genomic_DNA.
DR   EMBL; AY349830; AAQ64781.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q70PR8; -.
DR   SMR; Q70PR8; -.
DR   GO; GO:0005576; C:extracellular region; ISS:UniProtKB.
DR   GO; GO:0005615; C:extracellular space; IEA:EnsemblMetazoa.
DR   GO; GO:0008745; F:N-acetylmuramoyl-L-alanine amidase activity; IEA:InterPro.
DR   GO; GO:0042834; F:peptidoglycan binding; IEA:EnsemblMetazoa.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0050829; P:defense response to Gram-negative bacterium; IEA:EnsemblMetazoa.
DR   GO; GO:0050830; P:defense response to Gram-positive bacterium; ISS:UniProtKB.
DR   GO; GO:0032499; P:detection of peptidoglycan; IEA:EnsemblMetazoa.
DR   GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR   GO; GO:0009253; P:peptidoglycan catabolic process; IEA:InterPro.
DR   GO; GO:0061059; P:positive regulation of peptidoglycan recognition protein signaling pathway; IEA:EnsemblMetazoa.
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   3: Inferred from homology;
KW   Disulfide bond; Glycoprotein; Immunity; Innate immunity; Secreted; Signal.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   CHAIN           19..186
FT                   /note="Peptidoglycan-recognition protein SD"
FT                   /id="PRO_0000023915"
FT   DOMAIN          47..169
FT                   /note="N-acetylmuramoyl-L-alanine amidase"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        181
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        57..63
FT                   /evidence="ECO:0000250"
FT   VARIANT         127
FT                   /note="Q -> R (in strain: Sim1, Sim2, Sim3, Sim4, Sim5,
FT                   Sim6, Sim7 and Sim8)"
FT   VARIANT         138
FT                   /note="K -> R (in strain: Sim2, Sim3, Sim6, Sim7 and Sim8)"
FT   VARIANT         171
FT                   /note="A -> T (in strain: Sim5)"
SQ   SEQUENCE   186 AA;  20125 MW;  3290C5A4C59E9DC1 CRC64;
     MTWIGLLIVG LTAIAVQGEV PIVTRAEWNA KPPNGAIDSM ETPLPRAVIA HTAGGACADD
     VTCSQHMRNL QNFQMSKQKF SDIGYHYLIG GNGKVYEGRS PSQRGAFAGP NNDGSLGIAF
     IGNFEKQAPN KEALDAAKEL LEQAVKQAQL VEGYKLLGHR QVSATMSPGE ALYALIQQWP
     NWSEEM