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Protein

Lipoprotein NlpE

Gene

nlpE

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

Functioni

Involved in copper homeostasis, could be involved in both copper efflux and the delivery of copper to copper-dependent enzymes (PubMed:7635807). Required for efficient binding of stationary phase cells to hydrophobic surfaces, part of the process of biofilm formation (PubMed:11830644). Functions during envelope stress responses; when overproduced induces degP through the activation of the two-component envelope stress response system CpxA/CpxR (PubMed:7635808, PubMed:15252048). DegP induction seems to require membrane anchoring of this protein (PubMed:15252048). Structural changes and/or interaction of the CXXC motif with its environment may lead to activation of the Cpx stress response (PubMed:17698001).4 Publications

GO - Molecular functioni

  • identical protein binding Source: IntAct

GO - Biological processi

  • cell adhesion Source: UniProtKB-KW
  • regulation of cell-substrate adhesion Source: EcoCyc

Keywordsi

Biological processCell adhesion
LigandCopper

Enzyme and pathway databases

BioCyciEcoCyc:EG12137-MONOMER

Names & Taxonomyi

Protein namesi
Recommended name:
Lipoprotein NlpE1 Publication
Alternative name(s):
Copper homeostasis protein CutF1 Publication
Gene namesi
Name:nlpE1 Publication
Synonyms:cutF1 Publication
Ordered Locus Names:b0192, JW0188
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG12137 nlpE

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini21 – 236Periplasmic1 PublicationAdd BLAST216

GO - Cellular componenti

  • cell outer membrane Source: EcoCyc

Keywords - Cellular componenti

Cell outer membrane, Membrane

Pathology & Biotechi

Disruption phenotypei

No visible phenotype (PubMed:7635808). Slightly copper sensitive (PubMed:7635807). Decreased numbers of stationary phase cells bind to hydrophobic surfaces, cellular adhesion has altered dynamic properties; no induction of cpxR when cells bind to hydrophobic surfaces (PubMed:11830644).3 Publications

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi21C → A: No longer induces degP when overexpressed, targeted to the periplasm. 1 Publication1
Mutagenesisi22 – 23NN → DD: Slightly stronger than normal induction of degP when overexpressed, mistargeted to inner membrane. 1 Publication2
Mutagenesisi51 – 54CADC → SADS: Forms oxidized monomers. 1 Publication4
Mutagenesisi51C → S: Forms oxidized monomers. 1 Publication1
Mutagenesisi54C → S: Forms oxidized monomers. 1 Publication1
Mutagenesisi165C → S: No oxidized monomer forms; when associated with Ser-231. 1 Publication1
Mutagenesisi231C → S: No oxidized monomer forms; when associated with Ser-165. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 20Add BLAST20
ChainiPRO_000001803621 – 236Lipoprotein NlpEAdd BLAST216

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Lipidationi21N-palmitoyl cysteinePROSITE-ProRule annotation1 Publication1
Lipidationi21S-diacylglycerol cysteinePROSITE-ProRule annotation1
Disulfide bondi165 ↔ 2311 Publication

Post-translational modificationi

Palmitoylated.1 Publication
Seems to only form a disulfide bond between Cys-165 and Cys-231. The 2 other cysteine residues may however be chemically active.1 Publication

Keywords - PTMi

Disulfide bond, Lipoprotein, Palmitate

Proteomic databases

PaxDbiP40710
PRIDEiP40710

Interactioni

Subunit structurei

Probably exists as a monomer in vivo, can however form homodimers which swap domains (PubMed:17698001).1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
itself3EBI-1116525,EBI-1116525

GO - Molecular functioni

  • identical protein binding Source: IntAct

Protein-protein interaction databases

BioGridi4260842, 209 interactors
DIPiDIP-9353N
IntActiP40710, 3 interactors
STRINGi316385.ECDH10B_0173

Structurei

Secondary structure

1236
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi44 – 51Combined sources8
Beta strandi54 – 63Combined sources10
Beta strandi67 – 76Combined sources10
Beta strandi80 – 92Combined sources13
Beta strandi95 – 102Combined sources8
Beta strandi107 – 113Combined sources7
Beta strandi116 – 120Combined sources5
Beta strandi128 – 131Combined sources4
Beta strandi134 – 137Combined sources4
Beta strandi147 – 155Combined sources9
Beta strandi160 – 164Combined sources5
Turni165 – 167Combined sources3
Beta strandi170 – 173Combined sources4
Helixi177 – 187Combined sources11
Beta strandi189 – 191Combined sources3
Beta strandi194 – 205Combined sources12
Turni208 – 210Combined sources3
Beta strandi214 – 221Combined sources8
Beta strandi225 – 228Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2Z4HX-ray2.80A/B21-236[»]
2Z4IX-ray2.60A/B21-236[»]
ProteinModelPortaliP40710
SMRiP40710
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP40710

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni21 – 100N-terminal domain1 PublicationAdd BLAST80
Regioni126 – 236C-terminal domain1 PublicationAdd BLAST111
Regioni144 – 156Could contain a copper-binding motif1 PublicationAdd BLAST13

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi51 – 54CXXC1 Publication4

Domaini

The mature protein has 2 domains, the N-terminus (residues 21-100) and the C-terminus (residues 126-236) joined by a flexible linker; both domains form beta-barrels. In the crystal structure of the soluble mutant (Ala-21) the N-terminus of 1 subunit interacts with the C-terminus of the other.1 Publication

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG4107EII Bacteria
COG3015 LUCA
HOGENOMiHOG000116933
InParanoidiP40710
KOiK06079
OMAiGTWVMNQ

Family and domain databases

Gene3Di2.40.50.540, 1 hit
InterProiView protein in InterPro
IPR007298 Cu-R_lipoprotein_NlpE
IPR033450 NlpE_C
IPR038139 NlpE_C_dom_sf
PfamiView protein in Pfam
PF04170 NlpE, 1 hit
PF17185 NlpE_C, 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.

P40710-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVKKAIVTAM AVISLFTLMG CNNRAEVDTL SPAQAAELKP MPQSWRGVLP
60 70 80 90 100
CADCEGIETS LFLEKDGTWV MNERYLGARE EPSSFASYGT WARTADKLVL
110 120 130 140 150
TDSKGEKSYY RAKGDALEML DREGNPIESQ FNYTLEAAQS SLPMTPMTLR
160 170 180 190 200
GMYFYMADAA TFTDCATGKR FMVANNAELE RSYLAARGHS EKPVLLSVEG
210 220 230
HFTLEGNPDT GAPTKVLAPD TAGKFYPNQD CSSLGQ
Length:236
Mass (Da):25,844
Last modified:February 1, 1995 - v1
Checksum:i016DAD52EBBE366C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U18345 Genomic DNA Translation: AAA86093.1
L38619 Genomic DNA Translation: AAA82972.1
D49445 Genomic DNA Translation: BAA08433.1
U70214 Genomic DNA Translation: AAB08620.1
U00096 Genomic DNA Translation: AAC73303.1
AP009048 Genomic DNA Translation: BAA77868.1
PIRiH64743
RefSeqiNP_414734.1, NC_000913.3
WP_000239163.1, NZ_LN832404.1

Genome annotation databases

EnsemblBacteriaiAAC73303; AAC73303; b0192
BAA77868; BAA77868; BAA77868
GeneIDi946782
KEGGiecj:JW0188
eco:b0192
PATRICifig|1411691.4.peg.2086

Similar proteinsi

Entry informationi

Entry nameiNLPE_ECOLI
AccessioniPrimary (citable) accession number: P40710
Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: March 28, 2018
This is version 130 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