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 |