The domain within your query sequence starts at position 213 and ends at position 354; the E-value for the PGRP domain shown below is 2.13e-72.

PHIVPRSVWGARDSHCSRMTLPAKYAIILHTAGRTCSQPDECRLLVRDLQSFFMNRLNAC
DIGYNFLVGQDGGVYEGVGWNNQGSKTDSYNDISLSITFMGTFTGSPPNAAALEAAQDLI
RCAVVKGYLTPNYLLMGHSDVS

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: N-acetylmuramoyl-L-alanine amidase activity (GO:0008745), zinc ion binding (GO:0008270)

There are 5568 PGRP domains in 5206 proteins in SMART's nrdb database.

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

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

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)

% 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	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)
2xz4	Crystal structure of the LFZ ectodomain of the peptidoglycan recognition protein LF
2xz8	CRYSTAL STRUCTURE OF THE LFW ECTODOMAIN OF THE PEPTIDOGLYCAN RECOGNITION PROTEIN LF
2z9n	Crystal structure of cameline peptidoglycan recognition protein at 3.2 A resolution
3c2x	Crystal structure of peptidoglycan recognition protein at 1.8A 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
3ng4	Ternary complex of peptidoglycan recognition protein (PGRP-S) with Maltose and N-Acetylglucosamine at 1.7 A Resolution
3nno	Crystal structure of the complex of peptidoglycan recognition protein (PGRP-S) with Alpha-Rhamnose at 2.9 A resolution
3nw3	Crystal structure of the complex of peptidoglycan recognition protein (PGRP-S) with the PGN Fragment at 2.5 A resolution
3o4k	Crystal structure of the complex of peptidoglycan recognition protein (PGRP-S) and lipoteichoic acid at 2.1 A resolution
3ogx	Crystal structure of the complex of Peptidoglycan Recognition protein (PGRP-s) with Heparin-Dissacharide at 2.8 A resolution
3qj1	Crystal structure of camel peptidoglycan recognition protein, PGRP-S with a trapped diethylene glycol in the ligand diffusion channel at 3.2 A resolution
3qs0	Crystal structure of the complex of peptidoglycan recognition protein (PGRP-S) with a bound N-acetylglucosamine in the diffusion channel at 2.5 A resolution
3qv4	Crystal structure of the complex of peptidoglycan recognition protein (PGRP-S) with dipeptide L-ALA D-GLU at 2.7 A resolution
3rt4	Structural Basis of Recognition of Pathogen-associated Molecular Patterns and Inhibition of Proinflammatory Cytokines by Camel Peptidoglycan Recognition Protein
3t2v	Crystal structure of the complex of peptidoglycan recognition protein-short (CPGRP-S) with mycolic acid at 2.5 A resolution
3t39	Crystal structure of the complex of camel peptidoglycan recognition protein(CPGRP-S) with a mycobacterium metabolite shikimate at 2.7 A resolution
3tru	Crystal structure of the complex of peptidoglycan recognition protein with cellular metabolite chorismate at 3.2 A resolution
3uil	Crystal Structure of the complex of PGRP-S with lauric acid at 2.2 A resolution
3uml	Crystal structure of PGRP-S complexed with chorismate at 2.15 A resolution
3umq	Crystal structure of peptidoglycan recognition protein-S complexed with butyric acid at 2.2 A resolution
3usx	Crystal structure of PGRP-S complexed with Myristic Acid at 2.28 A resolution
4fnn	Crystal structure of the complex of CPGRP-S with stearic acid at 2.2 A RESOLUTION
4gf9	Structural insights into the dual strategy of recognition of peptidoglycan recognition protein, PGRP-S: ternary complex of PGRP-S with LPS and fatty acid
4opp	Crystal structure of the ternary complex of camel peptidoglycan recognition protein PGRP-S with 11-cyclohexylundecanoic acid and N- acetylglucosamine at 2.30 A resolution
4orv	Crystal structure of the ternary complex of camel peptidoglycan recognition protein PGRP-S with 7- phenylheptanoic acid and N- acetylglucosamine at 2.50 A resolution
4oug	Crystal structure of the ternary complex of camel peptidoglycan recognition protein, PGRP-S with lipopolysaccharide and palmitic acid at 2.46 A resolution
4q8s	Crystal structure of mammalian Peptidoglycan recognition protein PGRP-S with paranitrophenyl palmitate and N-acetyl glucosamine at 2.09 A resolution
4q9e	Structure of the ternary complex of peptidoglycan recognition protein, PGRP-S with N-acetyl glucosamine and paranitro benzaldehyde at 2.3 A resolution
4z8i	4Z8I
4zxm	4ZXM
5dwf	5DWF
5e0a	5E0A
5e0b	5E0B

Links (links to other resources describing this domain)

• INTERPRO: IPR006619