ID PGSC2_DROSI Reviewed; 184 AA. AC Q70PU1; B2XZX6; B4QG79; Q2XY96; DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2004, sequence version 1. DT 27-MAR-2024, entry version 98. DE RecName: Full=Peptidoglycan-recognition protein SC2; DE EC=3.5.1.28; DE Flags: Precursor; GN Name=PGRP-SC2; ORFNames=GD10595; 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 [LARGE SCALE GENOMIC DNA]. RX PubMed=17994087; DOI=10.1038/nature06341; RG Drosophila 12 genomes consortium; RT "Evolution of genes and genomes on the Drosophila phylogeny."; RL Nature 450:203-218(2007). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 8-178. RC STRAIN=Ky-a, and Ky-b; RX PubMed=16120803; DOI=10.1093/molbev/msi246; RA Comeron J.M., Guthrie T.B.; RT "Intragenic Hill-Robertson interference influences selection intensity on RT synonymous mutations in Drosophila."; RL Mol. Biol. Evol. 22:2519-2530(2005). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 8-178, AND VARIANT VAL-12. RC STRAIN=01FG, 02FG, 03FG, 04FG, 05FG, 06FG, 07FG, 08FG, 09FG, 10FG, RC 11FG, 12FG, 13FG, 14FG, 15FG, and 16FG; RX PubMed=18288436; DOI=10.1007/s00239-008-9072-x; RA Llopart A., Mabille A., Peters-Hall J.R., Comeron J.M., Kliman R.M.; RT "A new test for selection applied to codon usage in Drosophila simulans and RT D. mauritiana."; RL J. Mol. Evol. 66:224-231(2008). 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 (By similarity). CC {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}. 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; AJ556611; CAD89176.1; -; Genomic_DNA. DR EMBL; CM000362; EDX06229.1; -; Genomic_DNA. DR EMBL; DQ138765; ABA86371.1; -; Genomic_DNA. DR EMBL; DQ138766; ABA86372.1; -; Genomic_DNA. DR EMBL; EU313688; ABY56488.1; -; Genomic_DNA. DR EMBL; EU313689; ABY56489.1; -; Genomic_DNA. DR EMBL; EU313690; ABY56490.1; -; Genomic_DNA. DR EMBL; EU313691; ABY56491.1; -; Genomic_DNA. DR EMBL; EU313692; ABY56492.1; -; Genomic_DNA. DR EMBL; EU313693; ABY56493.1; -; Genomic_DNA. DR EMBL; EU313694; ABY56494.1; -; Genomic_DNA. DR EMBL; EU313695; ABY56495.1; -; Genomic_DNA. DR EMBL; EU313696; ABY56496.1; -; Genomic_DNA. DR EMBL; EU313697; ABY56497.1; -; Genomic_DNA. DR EMBL; EU313698; ABY56498.1; -; Genomic_DNA. DR EMBL; EU313699; ABY56499.1; -; Genomic_DNA. DR EMBL; EU313700; ABY56500.1; -; Genomic_DNA. DR EMBL; EU313701; ABY56501.1; -; Genomic_DNA. DR EMBL; EU313702; ABY56502.1; -; Genomic_DNA. DR EMBL; EU313703; ABY56503.1; -; Genomic_DNA. DR RefSeq; XP_002080644.1; XM_002080608.2. DR AlphaFoldDB; Q70PU1; -. DR SMR; Q70PU1; -. DR STRING; 7240.Q70PU1; -. DR EnsemblMetazoa; FBtr0210505; FBpp0208997; FBgn0068645. DR GeneID; 6733590; -. DR HOGENOM; CLU_037559_3_2_1; -. DR OMA; WIDIAYH; -. DR OrthoDB; 2282228at2759; -. DR PhylomeDB; Q70PU1; -. DR Proteomes; UP000000304; Chromosome 2r. DR Bgee; FBgn0068645; Expressed in adult organism and 3 other cell types or tissues. 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:0002814; P:negative regulation of biosynthetic process of antibacterial peptides active against Gram-negative bacteria; IEA:EnsemblMetazoa. DR GO; GO:0061060; P:negative regulation of peptidoglycan recognition protein signaling pathway; IEA:EnsemblMetazoa. DR GO; GO:0009253; P:peptidoglycan catabolic process; IEA:InterPro. DR GO; GO:0160032; P:Toll receptor ligand protein activation cascade; IEA:EnsemblMetazoa. 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:SF41; PEPTIDOGLYCAN-RECOGNITION PROTEIN SC1A-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. PE 3: Inferred from homology; KW Disulfide bond; Hydrolase; Immunity; Innate immunity; Metal-binding; KW Reference proteome; Secreted; Signal; Zinc. FT SIGNAL 1..20 FT /evidence="ECO:0000255" FT CHAIN 21..184 FT /note="Peptidoglycan-recognition protein SC2" FT /id="PRO_0000023913" FT DOMAIN 45..169 FT /note="N-acetylmuramoyl-L-alanine amidase" FT /evidence="ECO:0000255" FT BINDING 50 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000250|UniProtKB:Q8INK6" FT BINDING 159 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000250|UniProtKB:Q8INK6" FT BINDING 167 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000250|UniProtKB:Q8INK6" FT SITE 85 FT /note="Important for catalytic activity; essential for FT amidase activity and zinc hydrate coordination" FT /evidence="ECO:0000250|UniProtKB:P00806" FT DISULFID 57..63 FT /evidence="ECO:0000250" FT VARIANT 12 FT /note="L -> V (in strain: 08FG)" FT /evidence="ECO:0000269|PubMed:18288436" SQ SEQUENCE 184 AA; 19788 MW; BF4070F2313D53C5 CRC64; MANKALILLA VLFCAQAVLG VTIVSKSEWG GRSATSKTSL ASYLSYAVIH HTAGNYCSTK AACITQLKNI QAYHMDSLGW ADIGYNFLIG GDGNVYEGRG WNVMGAHATN WNSKSIGISF LGNYNTNTLT SAQITAAKGL LSDAVSRGQI VSGYILYGHR QVGSTECPGT NIWNEIRTWS NWKA //