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Protein

Peptidoglycan-recognition protein LE

Gene

PGRP-LE

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei206 – 2061Murein
Binding sitei254 – 2541Murein

GO - Molecular functioni

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

GO - Biological processi

  • defense response Source: FlyBase
  • 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
  • pattern recognition receptor signaling pathway Source: GOC
  • peptidoglycan catabolic process Source: UniProtKB
  • peptidoglycan recognition protein signaling pathway Source: FlyBase
  • positive regulation of innate immune response Source: FlyBase
  • signal transduction Source: FlyBase
Complete GO annotation...

Keywords - Biological processi

Immunity, Innate immunity

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 lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome X

Organism-specific databases

FlyBaseiFBgn0030695. PGRP-LE.

Subcellular locationi

  • Secreted 1 Publication

  • Note: However, no signal sequence are predicted by sequence analysis tools.

GO - Cellular componenti

  • extracellular region Source: UniProtKB
  • integral component of plasma membrane Source: FlyBase
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi231 – 2311E → L: Loss of peptidoglycan-induced oligomerization. 1 Publication
Mutagenesisi232 – 2321S → E: Loss of peptidoglycan-induced oligomerization. Strongly reduced affinity for peptidoglycan. 1 Publication
Mutagenesisi254 – 2541R → T: Strongly reduced affinity for peptidoglycan. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 345345Peptidoglycan-recognition protein LEPRO_0000220626Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi52 – 521N-linked (GlcNAc...)Sequence analysis
Glycosylationi95 – 951N-linked (GlcNAc...)Sequence analysis
Glycosylationi98 – 981N-linked (GlcNAc...)Sequence analysis
Glycosylationi106 – 1061N-linked (GlcNAc...)Sequence analysis
Glycosylationi318 – 3181N-linked (GlcNAc...)Sequence analysis

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

BgeeiQ9VXN9.
ExpressionAtlasiQ9VXN9. differential.
GenevisibleiQ9VXN9. DM.

Interactioni

Subunit structurei

Monomer. Peptidoglycan binding induces oligomerization.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
itself1EBI-154008,EBI-154008
weeP543501EBI-154008,EBI-188100

Protein-protein interaction databases

BioGridi58882. 139 interactions.
IntActiQ9VXN9. 1 interaction.
MINTiMINT-956800.
STRINGi7227.FBpp0300347.

Structurei

Secondary structure

1
345
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi180 – 1834Combined sources
Beta strandi197 – 20610Combined sources
Helixi215 – 23117Combined sources
Beta strandi241 – 2444Combined sources
Beta strandi250 – 2545Combined sources
Beta strandi261 – 2633Combined sources
Turni264 – 2663Combined sources
Helixi267 – 2693Combined sources
Beta strandi270 – 2778Combined sources
Beta strandi280 – 2823Combined sources
Helixi286 – 30116Combined sources
Beta strandi304 – 31310Combined sources
Helixi314 – 3163Combined sources
Beta strandi318 – 3203Combined sources
Helixi325 – 3317Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2CB3X-ray2.40A/B/C/D173-345[»]
ProteinModelPortaliQ9VXN9.
SMRiQ9VXN9. Positions 173-343.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9VXN9.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni229 – 24012Murein bindingAdd
BLAST
Regioni261 – 2677Murein binding
Regioni314 – 3229Murein binding

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG410IIH1. Eukaryota.
ENOG4111PAY. LUCA.
GeneTreeiENSGT00390000016833.
InParanoidiQ9VXN9.
KOiK01446.
OMAiTWPHFYN.
OrthoDBiEOG757CZ5.
PhylomeDBiQ9VXN9.

Family and domain databases

Gene3Di3.40.80.10. 1 hit.
InterProiIPR002502. Amidase_domain.
IPR015510. PGRP.
IPR006619. PGRP_domain_met/bac.
[Graphical view]
PANTHERiPTHR11022. PTHR11022. 1 hit.
PfamiPF01510. Amidase_2. 1 hit.
[Graphical view]
SMARTiSM00644. Ami_2. 1 hit.
SM00701. PGRP. 1 hit.
[Graphical view]
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.

Cross-referencesi

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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2CB3X-ray2.40A/B/C/D173-345[»]
ProteinModelPortaliQ9VXN9.
SMRiQ9VXN9. Positions 173-343.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi58882. 139 interactions.
IntActiQ9VXN9. 1 interaction.
MINTiMINT-956800.
STRINGi7227.FBpp0300347.

Proteomic databases

PaxDbiQ9VXN9.
PRIDEiQ9VXN9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi32534.
FlyBaseiFBgn0030695. PGRP-LE.

Phylogenomic databases

eggNOGiENOG410IIH1. Eukaryota.
ENOG4111PAY. LUCA.
GeneTreeiENSGT00390000016833.
InParanoidiQ9VXN9.
KOiK01446.
OMAiTWPHFYN.
OrthoDBiEOG757CZ5.
PhylomeDBiQ9VXN9.

Miscellaneous databases

EvolutionaryTraceiQ9VXN9.
GenomeRNAii32534.
PROiQ9VXN9.

Gene expression databases

BgeeiQ9VXN9.
ExpressionAtlasiQ9VXN9. differential.
GenevisibleiQ9VXN9. DM.

Family and domain databases

Gene3Di3.40.80.10. 1 hit.
InterProiIPR002502. Amidase_domain.
IPR015510. PGRP.
IPR006619. PGRP_domain_met/bac.
[Graphical view]
PANTHERiPTHR11022. PTHR11022. 1 hit.
PfamiPF01510. Amidase_2. 1 hit.
[Graphical view]
SMARTiSM00644. Ami_2. 1 hit.
SM00701. PGRP. 1 hit.
[Graphical view]
SUPFAMiSSF55846. SSF55846. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Berkeley.
  3. 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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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.

Entry informationi

Entry nameiPGPLE_DROME
AccessioniPrimary (citable) accession number: Q9VXN9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 10, 2005
Last sequence update: May 1, 2000
Last modified: June 8, 2016
This is version 110 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.