ID   PGSB2_DROSI             Reviewed;         182 AA.
AC   Q70PW6;
DT   10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   22-FEB-2023, entry version 71.
DE   RecName: Full=Peptidoglycan-recognition protein SB2;
DE            EC=3.5.1.28;
DE   Flags: Precursor;
GN   Name=PGRP-SB2;
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].
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). 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; AJ556586; CAD89151.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q70PW6; -.
DR   SMR; Q70PW6; -.
DR   GlyCosmos; Q70PW6; 1 site, No reported glycans.
DR   GO; GO:0005576; C:extracellular region; ISS:UniProtKB.
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; 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:SF75; PEPTIDOGLYCAN-RECOGNITION PROTEIN LB-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; Glycoprotein; Hydrolase; Immunity; Innate immunity;
KW   Metal-binding; Secreted; Signal; Zinc.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000255"
FT   CHAIN           18..182
FT                   /note="Peptidoglycan-recognition protein SB2"
FT                   /id="PRO_0000023909"
FT   DOMAIN          40..165
FT                   /note="N-acetylmuramoyl-L-alanine amidase"
FT                   /evidence="ECO:0000255"
FT   BINDING         47
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:Q8INK6"
FT   BINDING         155
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:Q8INK6"
FT   BINDING         163
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:Q8INK6"
FT   SITE            81
FT                   /note="Important for catalytic activity; essential for
FT                   amidase activity and zinc hydrate coordination"
FT                   /evidence="ECO:0000250|UniProtKB:P00806"
FT   CARBOHYD        149
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        54..60
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   182 AA;  20512 MW;  C74D0CEFD5561BC4 CRC64;
     MKLQLALVLC GLTLALGQIV PRSSWCPVPI SPRIPRLMVP VRLIIIHHTV TAPCFNPHQC
     QLVLRQIRAD HMRRKFRDIG YNFLIGGDGR IYEGLGFGIR GEHAPRYNSQ SIGIAFIGNF
     QTGLPPSQML QAARTLIQIA VQRRQVSPNY SLVGHCQTKA TACPGRHLLN ELKKWPRWQP
     KP
//