Q9VXN9 (PGPLE_DROME) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Peptidoglycan-recognition protein LE

Gene names

Name:	PGRP-LE
ORF Names:	CG8995

Organism

Drosophila melanogaster (Fruit fly)

Taxonomic identifier

7227 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Ephydroidea › Drosophilidae › Drosophila › Sophophora

Protein attributes

Sequence length	345 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Peptidoglycan-recognition protein that plays a key role in innate immnunity by binding to murein peptidoglycans (PGN) of Gram-negative bacteria and activating the imd/Relish pathway. Has no activity against on Gram-positive bacteria. Binds to diaminopimelic acid-type PGN (DAP-type PGN), an activator of the imd/Relish pathway. Functions synergistically with PGRP-LC in producing resistance to E.coli and B.megaterium infections, which have the DAP-type peptidoglycan. Acts both upstream and in parallel with PGRP-LC in the imd/Relish pathway, and is required for infection-dependent activation of melanization. Required for Relish processing and nuclear translocation following proteolytic cleavage. Its localization suggests a role in the recognition and subsequent activation of the signaling at the first point of contact with invading bacteria. Ref.5 Ref.6
Subunit structure	Monomer. Peptidoglycan binding induces oligomerization. Ref.7
Subcellular location	Secreted. Note: However, no signal sequence are predicted by sequence analysis tools. Ref.6
Tissue specificity	Expressed in hemolymph. Localizes at the lumenal surface of the trachea (at protein level). Ref.6
Developmental stage	Highly expressed in 0-5 hours embryos and in adult females, suggesting that it is expressed maternally. Ref.1
Sequence similarities	Belongs to the N-acetylmuramoyl-L-alanine amidase 2 family.

Ontologies

Keywords
Biological process	Immunity Innate immunity
Cellular component	Secreted
PTM	Glycoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	defense response to Gram-positive bacterium Inferred from direct assay Ref.6. Source: UniProtKB determination of adult lifespan Inferred from mutant phenotype. Source: FlyBase innate immune response Non-traceable author statement Ref.1. Source: UniProtKB peptidoglycan catabolic process Non-traceable author statement Ref.1. Source: UniProtKB
Cellular component	extracellular region Inferred from direct assay Ref.6. Source: UniProtKB
Molecular function	N-acetylmuramoyl-L-alanine amidase activity Inferred from electronic annotation. Source: InterPro peptidoglycan binding Non-traceable author statement Ref.1. Source: UniProtKB peptidoglycan receptor activity Non-traceable author statement. Source: FlyBase protein binding Inferred from physical interaction. Source: FlyBase zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
itself		1	EBI-154008,EBI-154008
wee	P54350	1	EBI-154008,EBI-188100

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 345

345

Peptidoglycan-recognition protein LE

PRO_0000220626

Regions

Region

229 – 240

12

Murein binding

Region

261 – 267

7

Murein binding

Region

314 – 322

9

Murein binding

Sites

Binding site

206

1

Murein

Binding site

254

1

Murein

Amino acid modifications

Glycosylation

52

1

N-linked (GlcNAc...) Potential

Glycosylation

95

1

N-linked (GlcNAc...) Potential

Glycosylation

98

1

N-linked (GlcNAc...) Potential

Glycosylation

106

1

N-linked (GlcNAc...) Potential

Glycosylation

318

1

N-linked (GlcNAc...) Potential

Experimental info

Mutagenesis

231

1

E → L: Loss of peptidoglycan-induced oligomerization. Ref.7

Mutagenesis

232

1

S → E: Loss of peptidoglycan-induced oligomerization. Strongly reduced affinity for peptidoglycan. Ref.7

Mutagenesis

254

1

R → T: Strongly reduced affinity for peptidoglycan. Ref.7

Secondary structure

1

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345

Helix Strand Turn

Details...

Helix

180 – 183

4

Beta strand

197 – 206

10

Helix

215 – 231

17

Beta strand

241 – 244

4

Beta strand

250 – 254

5

Beta strand

261 – 263

3

Turn

264 – 266

3

Helix

267 – 269

3

Beta strand

270 – 277

8

Beta strand

280 – 282

3

Helix

286 – 301

16

Beta strand

304 – 313

10

Helix

314 – 316

3

Beta strand

318 – 320

3

Helix

325 – 331

7

Sequences

	Sequence		Length	Mass (Da)
	Q9VXN9 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: 66CC484B54705AD7	FASTA	345	39,426
	10 20 30 40 50 60 MSESGIKKLS QERTREWLAS QEDEELESIA ESSVVDSLDY DYTEEEEDAD QNTSEEISTM 70 80 90 100 110 120 TLGTQIATKK HSIISDTIRD LMNSINSIQT LGNVNISNST NVHIGNVTNI NGNIQIIADG 130 140 150 160 170 180 LTQNRRDRRH VSPPRDNAPK TPTHFEDDYQ DESEERVRSD VFIRRQKFKI PKELSAIIPR 190 200 210 220 230 240 SSWLAQKPMD EPLPLQLPVK YVVILHTATE SSEKRAINVR LIRDMQCFHI ESRGWNDIAY 250 260 270 280 290 300 NFLVGCDGNI YEGRGWKTVG AHTLGYNRIS LGISFIGCFM KELPTADALN MCRNLLARGV 310 320 330 340 EDGHISTDYR LICHCQCNST ESPGRRLYEE IQTWPHFYNI EEEEQ

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A family of peptidoglycan recognition proteins in the fruit fly Drosophila melanogaster." Werner T., Liu G., Kang D., Ekengren S., Steiner H., Hultmark D. Proc. Natl. Acad. Sci. U.S.A. 97:13772-13777(2000) [PubMed: 11106397] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], DEVELOPMENTAL STAGE.
[2]	"The genome sequence of Drosophila melanogaster." Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D. , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C. Science 287:2185-2195(2000) [PubMed: 10731132] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Berkeley.
[3]	"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review." Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E. Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed: 12537572] [Abstract] Cited for: GENOME REANNOTATION. Strain: Berkeley.
[4]	"A Drosophila full-length cDNA resource." Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E. Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed: 12537569] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Berkeley. Tissue: Head.
[5]	"Overexpression of a pattern-recognition receptor, peptidoglycan-recognition protein-LE, activates imd/relish-mediated antibacterial defense and the prophenoloxidase cascade in Drosophila larvae." Takehana A., Katsuyama T., Yano T., Oshima Y., Takada H., Aigaki T., Kurata S. Proc. Natl. Acad. Sci. U.S.A. 99:13705-13710(2002) [PubMed: 12359879] [Abstract] Cited for: FUNCTION.
[6]	"Peptidoglycan recognition protein (PGRP)-LE and PGRP-LC act synergistically in Drosophila immunity." Takehana A., Yano T., Mita S., Kotani A., Oshima Y., Kurata S. EMBO J. 23:4690-4700(2004) [PubMed: 15538387] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[7]	"Structural basis for preferential recognition of diaminopimelic acid-type peptidoglycan by a subset of peptidoglycan recognition proteins." Lim J.-H., Kim M.-S., Kim H.-E., Yano T., Oshima Y., Aggarwal K., Goldman W.E., Silverman N., Kurata S., Oh B.-H. J. Biol. Chem. 281:8286-8295(2006) [PubMed: 16428381] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 173-345 IN COMPLEX WITH PEPTIDOGLYCAN FRAGMENT, SUBUNIT, MUTAGENESIS OF GLU-231; SER-232 AND ARG-254.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF313391 mRNA. Translation: AAG32064.1.
AE014298 Genomic DNA. Translation: AAF48519.1.
AY058258 mRNA. Translation: AAL13487.1.

RefSeq

NP_573078.1. NM_132850.2.

UniGene

Dm.3371.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2CB3	X-ray	2.40	A/B/C/D	173-345	[»]

ProteinModelPortal

Q9VXN9.

SMR

Q9VXN9. Positions 173-343.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q9VXN9. 2 interactions.

MINT

MINT-956800.

STRING

Q9VXN9.

Proteomic databases

PRIDE

Q9VXN9.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblMetazoa

FBtr0074183; FBpp0073968; FBgn0030695.
FBtr0307978; FBpp0300347; FBgn0030695.

GeneID

32534.

KEGG

dme:Dmel_CG8995.

NMPDR

fig|7227.3.peg.18021.

Organism-specific databases

CTD

32534.

FlyBase

FBgn0030695. PGRP-LE.

Phylogenomic databases

eggNOG

inNOG09946.

GeneTree

EMGT00050000009248.

InParanoid

Q9VXN9.

OMA

NINGNIQ.

OrthoDB

EOG431ZDS.

PhylomeDB

Q9VXN9.

Gene expression databases

Bgee

Q9VXN9.

GermOnline

CG8995. Drosophila melanogaster.

Family and domain databases

InterPro

IPR002502. Amidase_domain.
IPR015510. PGRP.
IPR006619. PGRP_domain_met/bac.
[Graphical view]

Gene3D

G3DSA:3.40.80.10. Amidase_2. 1 hit.

KO

K01446.

PANTHER

PTHR11022. PGRPs. 1 hit.

Pfam

PF01510. Amidase_2. 1 hit.
[Graphical view]

SMART

SM00644. Ami_2. 1 hit.
SM00701. PGRP. 1 hit.
[Graphical view]

SUPFAM

SSF55846. Amidase_2. 1 hit.

ProtoNet

Search...

Other

NextBio

778973.

Entry information

Entry name

PGPLE_DROME

Accession

Primary (citable) accession number: Q9VXN9

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 10, 2005
Last sequence update:	May 1, 2000
Last modified:	January 25, 2012
This is version 79 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Drosophila annotation project