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Protein

Peptidoglycan-recognition protein LE

Gene

PGRP-LE

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

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.2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei206Murein1
Binding sitei254Murein1

GO - Molecular functioni

  • peptidoglycan binding Source: FlyBase
  • peptidoglycan receptor activity Source: FlyBase
  • zinc ion binding Source: InterPro

GO - Biological processi

  • defense response to bacterium Source: FlyBase
  • defense response to Gram-positive bacterium Source: UniProtKB
  • determination of adult lifespan Source: FlyBase
  • immune response Source: FlyBase
  • innate immune response Source: UniProtKB
  • peptidoglycan catabolic process Source: UniProtKB
  • peptidoglycan recognition protein signaling pathway Source: FlyBase
  • positive regulation of innate immune response Source: FlyBase
  • signal transduction Source: FlyBase

Keywordsi

Biological processImmunity, Innate immunity

Enzyme and pathway databases

ReactomeiR-DME-209171 Peptidoglycans (PGN) bind to a peptidoglycan recognition protein receptor, PGRP-LC/LE
R-DME-209266 Peptidoglycan bound PGRP-LC/LE oligomerises
R-DME-214397 Assembly of the PGN:PGRP-LC/LE receptor 'signalling complex'
R-DME-214399 Activated IkappaB kinase (IKK) complex, Phospho IRD5:KEY dimer, phosphorylates REL in the PGN:PGRP-LC/LE receptor 'signalling complex'
R-DME-214411 REL binds to DREDD in the PGN:PGRP-LC/LE receptor 'signalling complex'
R-DME-214416 Phosphorylated REL is cleaved by and dissociates from DREDD
R-DME-6798695 Neutrophil degranulation
R-DME-6803157 Antimicrobial peptides

Names & Taxonomyi

Protein namesi
Recommended name:
Peptidoglycan-recognition protein LE
Gene namesi
Name:PGRP-LE
ORF Names:CG8995
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraHolometabolaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome X

Organism-specific databases

FlyBaseiFBgn0030695 PGRP-LE

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi231E → L: Loss of peptidoglycan-induced oligomerization. 1 Publication1
Mutagenesisi232S → E: Loss of peptidoglycan-induced oligomerization. Strongly reduced affinity for peptidoglycan. 1 Publication1
Mutagenesisi254R → T: Strongly reduced affinity for peptidoglycan. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002206261 – 345Peptidoglycan-recognition protein LEAdd BLAST345

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi52N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi95N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi98N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi106N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi318N-linked (GlcNAc...) asparagineSequence analysis1

Keywords - PTMi

Glycoprotein

Proteomic databases

PaxDbiQ9VXN9
PRIDEiQ9VXN9

Expressioni

Tissue specificityi

Expressed in hemolymph. Localizes at the lumenal surface of the trachea (at protein level).1 Publication

Developmental stagei

Highly expressed in 0-5 hours embryos and in adult females, suggesting that it is expressed maternally.1 Publication

Gene expression databases

BgeeiFBgn0030695
ExpressionAtlasiQ9VXN9 differential
GenevisibleiQ9VXN9 DM

Interactioni

Subunit structurei

Monomer. Peptidoglycan binding induces oligomerization.1 Publication

Protein-protein interaction databases

BioGridi58882, 145 interactors
IntActiQ9VXN9, 4 interactors
STRINGi7227.FBpp0300347

Structurei

Secondary structure

1345
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi180 – 183Combined sources4
Beta strandi197 – 206Combined sources10
Helixi215 – 231Combined sources17
Beta strandi241 – 244Combined sources4
Beta strandi250 – 254Combined sources5
Beta strandi261 – 263Combined sources3
Turni264 – 266Combined sources3
Helixi267 – 269Combined sources3
Beta strandi270 – 277Combined sources8
Beta strandi280 – 282Combined sources3
Helixi286 – 301Combined sources16
Beta strandi304 – 313Combined sources10
Helixi314 – 316Combined sources3
Beta strandi318 – 320Combined sources3
Helixi325 – 331Combined sources7

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2CB3X-ray2.40A/B/C/D173-345[»]
ProteinModelPortaliQ9VXN9
SMRiQ9VXN9
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9VXN9

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni229 – 240Murein bindingAdd BLAST12
Regioni261 – 267Murein binding7
Regioni314 – 322Murein binding9

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG410IIH1 Eukaryota
ENOG4111PAY LUCA
GeneTreeiENSGT00390000016833
InParanoidiQ9VXN9
KOiK01446
OMAiTWPHFYN
OrthoDBiEOG091G0O6Z
PhylomeDBiQ9VXN9

Family and domain databases

CDDicd06583 PGRP, 1 hit
Gene3Di3.40.80.10, 1 hit
InterProiView protein in InterPro
IPR036505 Amidase/PGRP_sf
IPR002502 Amidase_domain
IPR015510 PGRP
IPR006619 PGRP_domain_met/bac
PANTHERiPTHR11022 PTHR11022, 1 hit
PfamiView protein in Pfam
PF01510 Amidase_2, 1 hit
SMARTiView protein in SMART
SM00644 Ami_2, 1 hit
SM00701 PGRP, 1 hit
SUPFAMiSSF55846 SSF55846, 1 hit

Sequencei

Sequence statusi: Complete.

Q9VXN9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSESGIKKLS QERTREWLAS QEDEELESIA ESSVVDSLDY DYTEEEEDAD
60 70 80 90 100
QNTSEEISTM TLGTQIATKK HSIISDTIRD LMNSINSIQT LGNVNISNST
110 120 130 140 150
NVHIGNVTNI NGNIQIIADG LTQNRRDRRH VSPPRDNAPK TPTHFEDDYQ
160 170 180 190 200
DESEERVRSD VFIRRQKFKI PKELSAIIPR SSWLAQKPMD EPLPLQLPVK
210 220 230 240 250
YVVILHTATE SSEKRAINVR LIRDMQCFHI ESRGWNDIAY NFLVGCDGNI
260 270 280 290 300
YEGRGWKTVG AHTLGYNRIS LGISFIGCFM KELPTADALN MCRNLLARGV
310 320 330 340
EDGHISTDYR LICHCQCNST ESPGRRLYEE IQTWPHFYNI EEEEQ
Length:345
Mass (Da):39,426
Last modified:May 1, 2000 - v1
Checksum:i66CC484B54705AD7
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF313391 mRNA Translation: AAG32064.1
AE014298 Genomic DNA Translation: AAF48519.1
AY058258 mRNA Translation: AAL13487.1
RefSeqiNP_001245695.1, NM_001258766.3
NP_573078.1, NM_132850.4
UniGeneiDm.3371

Genome annotation databases

EnsemblMetazoaiFBtr0074183; FBpp0073968; FBgn0030695
FBtr0307978; FBpp0300347; FBgn0030695
GeneIDi32534
KEGGidme:Dmel_CG8995

Similar proteinsi

Entry informationi

Entry nameiPGPLE_DROME
AccessioniPrimary (citable) accession number: Q9VXN9
Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 10, 2005
Last sequence update: May 1, 2000
Last modified: March 28, 2018
This is version 129 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health