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Protein

Lipoprotein NlpE

Gene

nlpE

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-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 - Biological processi

  • regulation of cell-substrate adhesion Source: EcoCyc
Complete GO annotation...

Keywords - Biological processi

Cell adhesion

Keywords - Ligandi

Copper

Enzyme and pathway databases

BioCyciEcoCyc:EG12137-MONOMER.
ECOL316407:JW0188-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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG12137. nlpE.

Subcellular locationi

  • Cell outer membrane 1 Publication1 Publication; Lipid-anchor 2 Publications

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini21 – 236216Periplasmic1 PublicationAdd
BLAST

GO - Cellular componenti

  • cell outer membrane Source: EcoCyc
Complete GO annotation...

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)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi21 – 211C → A: No longer induces degP when overexpressed, targeted to the periplasm. 1 Publication
Mutagenesisi22 – 232NN → DD: Slightly stronger than normal induction of degP when overexpressed, mistargeted to inner membrane. 1 Publication
Mutagenesisi51 – 544CADC → SADS: Forms oxidized monomers. 1 Publication
Mutagenesisi51 – 511C → S: Forms oxidized monomers. 1 Publication
Mutagenesisi54 – 541C → S: Forms oxidized monomers. 1 Publication
Mutagenesisi165 – 1651C → S: No oxidized monomer forms; when associated with Ser-231. 1 Publication
Mutagenesisi231 – 2311C → S: No oxidized monomer forms; when associated with Ser-165. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2020Add
BLAST
Chaini21 – 236216Lipoprotein NlpEPRO_0000018036Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi21 – 211N-palmitoyl cysteinePROSITE-ProRule annotation1 Publication
Lipidationi21 – 211S-diacylglycerol cysteinePROSITE-ProRule annotation
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

Protein-protein interaction databases

BioGridi4260842. 204 interactions.
DIPiDIP-9353N.
IntActiP40710. 3 interactions.
STRINGi511145.b0192.

Structurei

Secondary structure

1
236
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi44 – 518Combined sources
Beta strandi54 – 6310Combined sources
Beta strandi67 – 7610Combined sources
Beta strandi80 – 9213Combined sources
Beta strandi95 – 1028Combined sources
Beta strandi107 – 1137Combined sources
Beta strandi116 – 1205Combined sources
Beta strandi128 – 1314Combined sources
Beta strandi134 – 1374Combined sources
Beta strandi147 – 1559Combined sources
Beta strandi160 – 1645Combined sources
Turni165 – 1673Combined sources
Beta strandi170 – 1734Combined sources
Helixi177 – 18711Combined sources
Beta strandi189 – 1913Combined sources
Beta strandi194 – 20512Combined sources
Turni208 – 2103Combined sources
Beta strandi214 – 2218Combined sources
Beta strandi225 – 2284Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2Z4HX-ray2.80A/B21-236[»]
2Z4IX-ray2.60A/B21-236[»]
ProteinModelPortaliP40710.
SMRiP40710. Positions 41-234.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP40710.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni21 – 10080N-terminal domain1 PublicationAdd
BLAST
Regioni126 – 236111C-terminal domain1 PublicationAdd
BLAST
Regioni144 – 15613Could contain a copper-binding motif1 PublicationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi51 – 544CXXC1 Publication

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

InterProiIPR007298. Cu-R_lipoprotein_NlpE.
IPR033450. NlpE_C.
[Graphical view]
PfamiPF04170. NlpE. 1 hit.
PF17185. NlpE_C. 1 hit.
[Graphical view]
PROSITEiPS51257. PROKAR_LIPOPROTEIN. 1 hit.
[Graphical view]

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.
PATRICi32115497. VBIEscCol129921_0200.

Cross-referencesi

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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2Z4HX-ray2.80A/B21-236[»]
2Z4IX-ray2.60A/B21-236[»]
ProteinModelPortaliP40710.
SMRiP40710. Positions 41-234.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4260842. 204 interactions.
DIPiDIP-9353N.
IntActiP40710. 3 interactions.
STRINGi511145.b0192.

Proteomic databases

PaxDbiP40710.
PRIDEiP40710.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC73303; AAC73303; b0192.
BAA77868; BAA77868; BAA77868.
GeneIDi946782.
KEGGiecj:JW0188.
eco:b0192.
PATRICi32115497. VBIEscCol129921_0200.

Organism-specific databases

EchoBASEiEB2058.
EcoGeneiEG12137. nlpE.

Phylogenomic databases

eggNOGiENOG4107EII. Bacteria.
COG3015. LUCA.
HOGENOMiHOG000116933.
InParanoidiP40710.
KOiK06079.
OMAiGTWVMNQ.

Enzyme and pathway databases

BioCyciEcoCyc:EG12137-MONOMER.
ECOL316407:JW0188-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP40710.
PROiP40710.

Family and domain databases

InterProiIPR007298. Cu-R_lipoprotein_NlpE.
IPR033450. NlpE_C.
[Graphical view]
PfamiPF04170. NlpE. 1 hit.
PF17185. NlpE_C. 1 hit.
[Graphical view]
PROSITEiPS51257. PROKAR_LIPOPROTEIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiNLPE_ECOLI
AccessioniPrimary (citable) accession number: P40710
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: September 7, 2016
This is version 121 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references

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.