Schultz et al. (1998) Proc. Natl. Acad. Sci. USA 95, 5857-5864
Letunic et al. (2012) Nucleic Acids Res , doi:10.1093/nar/gkr931

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PGRP Animal peptidoglycan recognition proteins homologous to Bacteriophage T3 lysozyme.

SMART accession number:	SM00701
Description:	The bacteriophage molecule, but not its moth homologue, has been shown to have N-acetylmuramoyl-L-alanine amidase activity. One member of this family, Tag7, is a cytokine.
Interpro abstract (IPR006619):	This domain is found in a family of animal peptidoglycan recognition proteins homologous to Bacteriophage T3 lysozyme [(PUBMED:9707603)], and some bacterial homologues. The bacteriophage molecule, but not its moth homologue, has been shown to have N-acetylmuramoyl-L-alanine amidase activity. One member of this family, Tag7, is a cytokine [(PUBMED:9660837)].
GO process:	peptidoglycan catabolic process (GO:0009253)
GO function:	zinc ion binding (GO:0008270), N-acetylmuramoyl-L-alanine amidase activity (GO:0008745)
Family alignment:	View or CHROMA formatCLUSTALW formatMSF formatFASTA formatPIR format

There are 521 PGRP domains in 477 proteins in SMART's nrdb database.

Click on the following links for more information.

• Evolution (species in which this domain is found)

• Click on to expand nodes. To display all proteins with a PGRP domain in a specific node, click on it.

  This tree shows only several representative species. The complete taxonomic breakdown of all proteins with PGRP domain is also avaliable.

  Useful shortcuts: Expand all nodes or Collapse tree
  Go to specific node: Anopheles gambiae, Drosophila melanogaster, Homo sapiens, Mus musculus, Rattus norvegicus

• Cellular role (predicted cellular role)

• Binding / catalysis: Peptidoglycan-binding

• Literature (relevant references for this domain)

• Primary literature is listed below; Automatically-derived, secondary literature is also avaliable.

  • Kang D, Liu G, Lundstrom A, Gelius E, Steiner H
  • A peptidoglycan recognition protein in innate immunity conserved frominsects to humans.
  • Proc Natl Acad Sci U S A. 1998; 95: 10078-82
  • Display abstract

  • Innate nonself recognition must rely on common structures of invadingmicrobes. In a differential display screen for up-regulated immune genesin the moth Trichoplusia ni we have found mechanisms for recognition ofbacterial cell wall fragments. One bacteria-induced gene encodes a proteinthat, after expression in the baculovirus system, was shown to be apeptidoglycan recognition protein (PGRP). It binds strongly toGram-positive bacteria. We have also cloned the corresponding cDNA frommouse and human and shown this gene to be expressed in a variety oforgans, notably organs of the immune system-i.e., bone marrow and spleen.In addition, purified recombinant murine PGRP was shown to possesspeptidoglycan affinity. From our results and the sequence homology, weconclude that PGRP is a ubiquitous protein involved in innate immunity,conserved from insects to humans.

  • Kiselev SL et al.
  • Molecular cloning and characterization of the mouse tag7 gene encoding anovel cytokine.
  • J Biol Chem. 1998; 273: 18633-9
  • Display abstract

  • Cloning of the mouse tag7 gene encoding a novel cytokine is described. TheTag7 protein consists of 182 amino acids. Genomic organization of the tag7gene and its promoter region remind those of the genes of the tumornecrosis factor locus, although the tag7 gene is not linked to this locus.The gene is located on chromosome 7 at the area that corresponds to band7A3, which has genetic linkage with lupus-like disease in mouse models.tag7 transcription is essential for lymphoid organs. It is also detectedin certain areas of lungs, brain, and intestine and in some tumors. Tag7protein is detectable in both cell-associated and soluble forms. Thesoluble form of Tag7 triggers apoptosis in mouse L929 cells in vitro anddoes not involve NF-kappaB activation. The relationship between Tag7 andtumor necrosis factor family of ligands is discussed.

• Metabolism (metabolic pathways involving proteins which contain this domain)

• Click the image to view the interactive version of the map in iPath

  % proteins involved KEGG pathway ID Description 70.00 map00550 Peptidoglycan biosynthesis 5.00 map00380 Tryptophan metabolism 5.00 map00220 Urea cycle and metabolism of amino groups 5.00 map00643 Styrene degradation 5.00 map00460 Cyanoamino acid metabolism 5.00 map00360 Phenylalanine metabolism 5.00 map00632 Benzoate degradation via CoA ligation This information is based on mapping of SMART genomic protein database to KEGG orthologous groups. Percentage points are related to the number of proteins with PGRP domain which could be assigned to a KEGG orthologous group, and not all proteins containing PGRP domain. Please note that proteins can be included in multiple pathways, ie. the numbers above will not always add up to 100%.

• Structure (3D structures containing this domain)

• 3D Structures of PGRP domains in PDB

  PDB code	Main view	Title
  1aro		T7 rna polymerase complexed with t7 lysozyme
  1lba		The structure of bacteriophage t7 lysozyme, a zinc amidase and an inhibitor of t7 rna polymerase
  1oht		Peptidoglycan recognition protein-lb
  1s2j		Crystal structure of the drosophila pattern-recognition receptor pgrp-sa
  1sk3		Crystal structure of the c-terminal peptidoglycan-binding domain of human peptidoglycan recognition protein ialpha
  1sk4		Crystal structure of the c-terminal peptidoglycan-binding domain of human peptidoglycan recognition protein ialpha
  1sxr		Drosophila peptidoglycan recognition protein (pgrp)-sa
  1twq		Crystal structure of the c-terminal pgn-binding domain of human pgrp-ialpha in complex with pgn analog muramyl tripeptide
  1yck		Crystal structure of human peptidoglycan recognition protein (pgrp-s)
  1z6i		Crystal structure of the ectodomain of drosophila transmembrane receptor pgrp-lca
  2aph		Crystal structure of human pgrp-ialphac in complex with muramyl pentapeptide
  2cb3		Crystal structure of peptidoglycan recognition protein-le in complex with tracheal cytotoxin (monomeric diaminopimelic acid-type peptidoglycan)
  2eav		Crystal structure of the c-terminal peptidoglycan-binding domain of human peptidoglycan recognition protein ibeta
  2eax		Crystal structure of human pgrp-ibetac in complex with glycosamyl muramyl pentapeptide
  2f2l		Crystal structure of tracheal cytotoxin (tct) bound to the ectodomain complex of peptidoglycan recognition proteins lca (pgrp-lca) and lcx (pgrp-lcx)
  2r2k		Crystal structure of the complex of camel peptidoglycan recognition protein with disaccharide at 3.2a resolution
  2r90		Crystal structure of cameline peptidoglycan recognition protein at 2.8a resolution
  2rkq		Crystal structure of drosophila peptidoglycan recognition protein sd (pgrp-sd)
  2z9n		Crystal structure of cameline peptidoglycan recognition protein at 3.2 a resolution
  3c2x		Crystal structure of peptidoglycan recognition protein at 1.8a resolution
  3c93		Crystal structure of the complex of peptidoglycan recognition protein (pgrp-s) with n-acetyl glucosamine (nag) at 2.6 a resolution
  3cg9		Crystal structure of the complex of peptidoglycan recognition protein with methyloxane-2,3,4,5-tetrol at 2.9 a resolution
  3cor		Crystal structure of the complex of peptidoglycan recognition protein (pgrp-s) with n-acetylgalactosamine at 3.1 a resolution
  3cxa		Crystal structure of the complex of peptidoglycan recognition protein with alpha-d-glucopyranosyl alpha-d- glucopyranoside at 3.4 a resolution
  3ep1		Structure of the pgrp-hd from alvinella pompejana

• Links (links to other resources describing this domain)

• INTERPRO	IPR006619

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