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Protein

LPS-assembly lipoprotein LptE

Gene

lptE

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Together with LptD, is involved in the assembly of lipopolysaccharide (LPS) at the surface of the outer membrane. Required for the proper assembly of LptD. Binds LPS and may serve as the LPS recognition site at the outer membrane.UniRule annotation3 Publications

GO - Molecular functioni

  • lipopolysaccharide binding Source: EcoCyc

GO - Biological processi

  • Gram-negative-bacterium-type cell outer membrane assembly Source: EcoCyc
  • lipopolysaccharide transport Source: EcoCyc

Enzyme and pathway databases

BioCyciEcoCyc:EG10855-MONOMER
MetaCyc:EG10855-MONOMER

Protein family/group databases

TCDBi1.B.42.1.2 the outer membrane lipopolysaccharide export porin (lps-ep) family

Names & Taxonomyi

Protein namesi
Recommended name:
LPS-assembly lipoprotein LptEUniRule annotation
Alternative name(s):
Rare lipoprotein B
Gene namesi
Name:lptEUniRule annotation
Synonyms:rlpB
Ordered Locus Names:b0641, JW0636
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10855 lptE

Subcellular locationi

GO - Cellular componenti

  • cell outer membrane Source: EcoCyc

Keywords - Cellular componenti

Cell outer membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi117 – 119PIS → R: Affects interaction with LptD and LptD biogenesis. Increases outer membrane permeability. 1 Publication3

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 18Add BLAST18
ChainiPRO_000001818519 – 193LPS-assembly lipoprotein LptEAdd BLAST175

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Lipidationi19N-palmitoyl cysteineUniRule annotation1
Lipidationi19S-diacylglycerol cysteineUniRule annotation1

Keywords - PTMi

Lipoprotein, Palmitate

Proteomic databases

EPDiP0ADC1
PaxDbiP0ADC1
PRIDEiP0ADC1

Interactioni

Subunit structurei

Component of the lipopolysaccharide transport and assembly complex. Interacts with LptD. May interact with LptD during its assembly by the beta-barrel assembly machine. Directly contacts LptD at a wide range of positions, encompassing multiple surfaces of LptE. In one specific interaction, LptE contacts a predicted extracellular loop of LptD through the lumen of the beta-barrel. This specific interaction is required for proper folding of LptD and assembly of the complex.UniRule annotation4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
lptDP3155419EBI-1119442,EBI-549369

Protein-protein interaction databases

BioGridi4260757, 230 interactors
DIPiDIP-35987N
IntActiP0ADC1, 6 interactors
STRINGi316385.ECDH10B_0710

Structurei

Secondary structure

1193
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi31 – 33Combined sources3
Beta strandi34 – 41Combined sources8
Helixi46 – 57Combined sources12
Beta strandi61 – 63Combined sources3
Turni69 – 71Combined sources3
Beta strandi74 – 110Combined sources37
Turni111 – 113Combined sources3
Beta strandi114 – 126Combined sources13
Helixi130 – 132Combined sources3
Helixi140 – 156Combined sources17
Helixi159 – 168Combined sources10

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4NHRX-ray2.34A20-182[»]
4RH8X-ray2.20A/B/C/D20-186[»]
4RHBX-ray3.35B/D19-193[»]
ProteinModelPortaliP0ADC1
SMRiP0ADC1
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the LptE lipoprotein family.UniRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG4108U2H Bacteria
COG2980 LUCA
HOGENOMiHOG000256192
KOiK03643
OMAiTTVNRNY

Family and domain databases

HAMAPiMF_01186 LPS_assembly_LptE, 1 hit
InterProiView protein in InterPro
IPR007485 LPS_assembly_LptE
PANTHERiPTHR38098 PTHR38098, 1 hit
PfamiView protein in Pfam
PF04390 LptE, 1 hit
PROSITEiView protein in PROSITE
PS51257 PROKAR_LIPOPROTEIN, 1 hit

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P0ADC1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRYLATLLLS LAVLITAGCG WHLRDTTQVP STMKVMILDS GDPNGPLSRA
60 70 80 90 100
VRNQLRLNGV ELLDKETTRK DVPSLRLGKV SIAKDTASVF RNGQTAEYQM
110 120 130 140 150
IMTVNATVLI PGRDIYPISA KVFRSFFDNP QMALAKDNEQ DMIVKEMYDR
160 170 180 190
AAEQLIRKLP SIRAADIRSD EEQTSTTTDT PATPARVSTT LGN
Length:193
Mass (Da):21,357
Last modified:December 6, 2005 - v1
Checksum:iC9387BC2008ADEDC
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti117P → S in AAA24554 (PubMed:3316191).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M18277 Genomic DNA Translation: AAA24554.1
U82598 Genomic DNA Translation: AAB40842.1
U00096 Genomic DNA Translation: AAC73742.1
AP009048 Genomic DNA Translation: BAA35288.1
PIRiG64798 LPECRB
RefSeqiNP_415174.1, NC_000913.3
WP_001269673.1, NZ_LN832404.1

Genome annotation databases

EnsemblBacteriaiAAC73742; AAC73742; b0641
BAA35288; BAA35288; BAA35288
GeneIDi946257
KEGGiecj:JW0636
eco:b0641
PATRICifig|1411691.4.peg.1627

Similar proteinsi

Entry informationi

Entry nameiLPTE_ECOLI
AccessioniPrimary (citable) accession number: P0ADC1
Secondary accession number(s): P10101, P77576
Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 6, 2005
Last sequence update: December 6, 2005
Last modified: March 28, 2018
This is version 101 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome
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Main funding by: National Institutes of Health