PGSC2_DROSI
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 03-AUG-2022, entry version 93.
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, 11FG,
RC 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}.
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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; FKGDHSS; -.
DR PhylomeDB; Q70PU1; -.
DR Proteomes; UP000000304; Chromosome 2r.
DR Bgee; FBgn0068645; Expressed in adult organism and 3 other 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:0045752; P:positive regulation of Toll 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; 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
