Detail Information for IndEnz0002008351
IED ID IndEnz0002008351
Enzyme Type ID protease008351
Protein Name Peptidoglycan-recognition protein SA
EC 3.4.17.13
Protein semmelweis
Gene Name PGRP-SA seml CG11709
Organism Drosophila melanogaster (Fruit fly)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Protostomia Ecdysozoa Panarthropoda Arthropoda Mandibulata Pancrustacea Hexapoda Insecta Dicondylia Pterygota (winged insects) Neoptera Endopterygota Diptera Brachycera Muscomorpha Eremoneura Cyclorrhapha Schizophora Acalyptratae Ephydroidea Drosophilidae (pomace flies) Drosophilinae Drosophilini Drosophila (fruit flies) Sophophora melanogaster group melanogaster subgroup Drosophila melanogaster (Fruit fly)
Enzyme Sequence MQPVRFGSPWIMAIGLVLLLLAFVSAGKSRQRSPANCPTIKLKRQWGGKPSLGLHYQVRPIRYVVIHHTVTGECSGLLKCAEILQNMQAYHQNELDFNDISYNFLIGNDGIVYEGTGWGLRGAHTYGYNAIGTGIAFIGNFVDKLPSDAALQAAKDLLACGVQQGELSEDYALIAGSQVISTQSPGLTLYNEIQEWPHWLSNP
Enzyme Length 203
Uniprot Accession Number Q9VYX7
Absorption
Active Site
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=H2O + N-acetyl-D-glucosaminyl-N-acetylmuramoyl-L-alanyl-D-glutamyl-6-carboxy-L-lysyl-D-alanine = D-alanine + N-acetyl-D-glucosaminyl-N-acetylmuramoyl-L-alanyl-D-glutamyl-6-carboxy-L-lysyl; Xref=Rhea:RHEA:48688, ChEBI:CHEBI:15377, ChEBI:CHEBI:57416, ChEBI:CHEBI:90762, ChEBI:CHEBI:90763; EC=3.4.17.13; Evidence={ECO:0000269|PubMed:15361936};
DNA Binding
EC Number 3.4.17.13
Enzyme Function FUNCTION: Peptidoglycan-recognition protein that plays a key role in innate immunity by binding to peptidoglycans (PGN) of Gram-positive bacteria and activating the Toll pathway upstream of spz activating enzyme SPE (PubMed:11106397, PubMed:16399077, PubMed:15448690). Has no activity against Gram-negative bacteria and fungi (PubMed:11742401). Shows some partial redundancy with PRPGP-SD in Gram-positive bacteria recognition (PubMed:11742401, PubMed:15448690). May act by forming a complex with GNBP1 that activates the proteolytic cleavage of Spatzle and the subsequent activation of Toll pathway (PubMed:14684822, PubMed:14722090, PubMed:11742401). Binds to diaminopimelic acid-type tetrapeptide PGN (DAP-type PGN) and lysine-type PGN (Lys-type PGN) (PubMed:15361936). Has some L,D-carboxypeptidase activity for DAP-type PGN, which are specific to prokaryotes, but not for Lys-type PGN (PubMed:15361936). {ECO:0000269|PubMed:11742401, ECO:0000269|PubMed:14684822, ECO:0000269|PubMed:14722090, ECO:0000269|PubMed:15361936, ECO:0000269|PubMed:15448690, ECO:0000269|PubMed:16399077}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Beta strand (8); Chain (1); Disulfide bond (2); Domain (1); Helix (5); Mutagenesis (12); Region (2); Signal peptide (1); Site (1); Turn (1)
Keywords 3D-structure;Direct protein sequencing;Disulfide bond;Hydrolase;Immunity;Innate immunity;Protease;Reference proteome;Secreted;Signal
Interact With Q9NHB0
Induction INDUCTION: Strongly up-regulated by PGN from B.subtilis. Regulated by both imd/Relish and Toll pathways. {ECO:0000269|PubMed:11106397, ECO:0000269|PubMed:12032070}.
Subcellular Location SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:11742401}. Note=Secreted in hemolymph.
Modified Residue
Post Translational Modification
Signal Peptide SIGNAL 1..26; /evidence=ECO:0000269|PubMed:11106397
Structure 3D X-ray crystallography (2)
Cross Reference PDB 1S2J; 1SXR;
Mapped Pubmed ID 11606746; 11733057; 11742098; 11742378; 11912488; 11912489; 11951023; 12364793; 12431377; 12496260; 12692550; 12888789; 14557290; 14603309; 14749722; 15032585; 15199954; 15199956; 15314671; 15324670; 15538387; 15621536; 15777795; 15791270; 15797611; 15843462; 16061818; 16360948; 16407137; 16497588; 16518472; 16631589; 17024181; 17190605; 17227774; 17352533; 17356067; 17409189; 17517334; 17588928; 18261909; 18304640; 18378641; 18474356; 18519585; 18519643; 18613977; 18628398; 18697931; 18724373; 18823557; 18854145; 18927626; 19079572; 19218090; 19520911; 19590012; 19822734; 19851448; 19888449; 20089584; 20220848; 20371351; 20551040; 20627393; 20813047; 21063077; 21074052; 21078848; 21209287; 21264297; 21300896; 21390224; 21576362; 21729928; 21775770; 22144903; 22355133; 22368770; 22383881; 22496930; 22559237; 22724070; 22824741; 22949833; 23071443; 23228366; 23519314; 23550122; 23632253; 23648644; 23764256; 23796791; 23868318; 23922788; 23988573; 23991285; 24120681; 24398387; 24439372; 24443439; 24692449; 24706930; 25180232; 25312911; 25421701; 25628309; 25901322; 25902518; 25951442; 26162375; 27851910; 29211760; 29269264; 29394281; 30034391; 30986429; 31018123; 31116990; 31430488; 31564469; 31773367; 31794428; 32047838; 32188787; 32498733; 32656090; 32774336; 32866212; 32901612; 33081607; 33109529; 33117196; 34705495;
Motif
Gene Encoded By
Mass 22,260
Kinetics BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=21.4 uM for GlcNAc-MurNAc(anhydro)-L-Ala-gamma-D-Glu-meso-DAP-D-Ala {ECO:0000269|PubMed:15361936};
Metal Binding
Rhea ID RHEA:48688
Cross Reference Brenda