ID   PGSC1_DROSI             Reviewed;         185 AA.
AC   Q70PU2;
DT   10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 71.
DE   RecName: Full=Peptidoglycan-recognition protein SC1a/b;
DE            EC=3.5.1.28;
DE   Flags: Precursor;
GN   Name=PGRP-SC1a;
GN   and
GN   Name=PGRP-SC1b;
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).
CC   -!- FUNCTION: N-acetylmuramyl-L-alanine amidase involved in innate immunity
CC       by degrading bacterial peptidoglycans (PGN). Plays a scavenger role by
CC       digesting biologically active PGN into biologically inactive fragments.
CC       Has no direct bacteriolytic activity (By similarity). {ECO:0000250}.
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:0000250|UniProtKB:Q8INK6};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the N-acetylmuramoyl-L-alanine amidase 2 family.
CC       {ECO:0000305}.
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DR   EMBL; AJ556587; CAD89152.1; -; Genomic_DNA.
DR   EMBL; AJ556610; CAD89175.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q70PU2; -.
DR   SMR; Q70PU2; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0008745; F:N-acetylmuramoyl-L-alanine amidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0042834; F:peptidoglycan binding; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR   GO; GO:0009253; P:peptidoglycan catabolic process; IEA:InterPro.
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; Hydrolase; Immunity; Innate immunity; Metal-binding;
KW   Secreted; Signal; Zinc.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..185
FT                   /note="Peptidoglycan-recognition protein SC1a/b"
FT                   /id="PRO_0000023911"
FT   DOMAIN          46..170
FT                   /note="N-acetylmuramoyl-L-alanine amidase"
FT                   /evidence="ECO:0000255"
FT   BINDING         51
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:Q8INK6"
FT   BINDING         160
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:Q8INK6"
FT   BINDING         168
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:Q8INK6"
FT   SITE            86
FT                   /note="Important for catalytic activity; essential for
FT                   amidase activity and zinc hydrate coordination"
FT                   /evidence="ECO:0000250|UniProtKB:P00806"
FT   DISULFID        58..64
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   185 AA;  20366 MW;  F6368B74A378FC1E CRC64;
     MVSKVALLLA VLVCSQYMAQ GVYVVSKAEW GGRGAKWTVA LGNYLSYAII HHTAGSYCET
     RAQCNAVLQS VQAYHMDSLG WPDIGYNFLI GGDGNVYEGR GWNNMGAHAA EWNPYSIGIS
     FLGNYNWDTL EPNMISAAQQ LLNDAVNRGQ LSSGYILYGH RQVSATECPG THIWNEIRGW
     SHWSG