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Protein

Major outer membrane lipoprotein Lpp

Gene

lpp

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Interacts with the peptidoglycan both covalently and noncovalently. This interaction contributes to the maintenance of the structural and functional integrity of the cell envelope.

GO - Molecular functioni

  • lipid binding Source: UniProtKB
  • peptidoglycan binding Source: UniProtKB

GO - Biological processi

  • lipid modification Source: UniProtKB
Complete GO annotation...

Enzyme and pathway databases

BioCyciEcoCyc:EG10544-MONOMER.
ECOL316407:JW1667-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Major outer membrane lipoprotein Lpp
Alternative name(s):
Braun lipoprotein
Murein-lipoprotein
Gene namesi
Name:lpp
Synonyms:mlpA, mulI
Ordered Locus Names:b1677, JW1667
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10544. lpp.

Subcellular locationi

GO - Cellular componenti

  • cell outer membrane Source: UniProtKB
  • integral component of cell outer membrane Source: EcoCyc
  • membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell outer membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi22S → D: Localizes to the inner membrane, where it associates with peptidoglycan, thereby preventing separation of the two membranes. Prolonged expression is lethal for the cell. 1 Publication1
Mutagenesisi70D → E, G or S: Does not affect the formation of murein-bound lipoprotein. 1 Publication1
Mutagenesisi75K → S or T: Does not affect the formation of murein-bound lipoprotein. 1 Publication1
Mutagenesisi76Y → C, D, E, G, N, P or S: Reduces the formation of murein-bound lipoprotein. 1 Publication1
Mutagenesisi76Y → F, H, I or L: Does not affect the formation of murein-bound lipoprotein. 1 Publication1
Mutagenesisi77R → D or L: Reduces the formation of murein-bound lipoprotein. 1 Publication1
Mutagenesisi78K → R: Abolishes the formation of murein-bound lipoprotein. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 20PROSITE-ProRule annotation2 PublicationsAdd BLAST20
ChainiPRO_000001833121 – 78Major outer membrane lipoprotein LppAdd BLAST58

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-formylmethionine1 Publication1
Lipidationi21N-palmitoyl cysteinePROSITE-ProRule annotation1 Publication1
Lipidationi21S-diacylglycerol cysteinePROSITE-ProRule annotation1 Publication1
Modified residuei78N6-murein peptidoglycan lysine1

Keywords - PTMi

Formylation, Lipoprotein, Palmitate, Peptidoglycan-anchor

Proteomic databases

EPDiP69776.
PaxDbiP69776.
PRIDEiP69776.

Miscellaneous databases

PMAP-CutDBP69776.

Interactioni

Subunit structurei

Homotrimer. Seems to interact with TolB, Pal and TonB. Has been isolated from outer membrane preparations as an approximately 87 kDa complex, suggesting it also forms larger complexes.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself2EBI-909750,EBI-909750
tonBP029292EBI-909750,EBI-6399993

Protein-protein interaction databases

BioGridi4260276. 199 interactors.
DIPiDIP-35674N.
IntActiP69776. 4 interactors.
STRINGi511145.b1677.

Structurei

Secondary structure

178
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi25 – 71Combined sources47

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1EQ7X-ray1.90A22-77[»]
1JCCX-ray1.70A/B/C22-77[»]
1JCDX-ray1.30A/B/C22-73[»]
1KFMX-ray2.00A22-77[»]
1KFNX-ray1.65A22-77[»]
1MLPmodel-A/B21-78[»]
1T8ZX-ray1.45A/B/C/D/E22-74[»]
2GUSX-ray1.75A22-77[»]
2GUVX-ray1.40A/B/C/D/E22-77[»]
ProteinModelPortaliP69776.
SMRiP69776.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP69776.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati24 – 34Add BLAST11
Repeati38 – 48Add BLAST11

Sequence similaritiesi

Belongs to the Lpp family.Curated

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiENOG4105KMX. Bacteria.
COG4238. LUCA.
HOGENOMiHOG000295473.
KOiK06078.
OMAiNCASTNK.

Family and domain databases

InterProiIPR006817. Lipoprotein_leucine-zipper_dom.
IPR016367. Murein-lipoprotein.
[Graphical view]
PfamiPF04728. LPP. 1 hit.
[Graphical view]
PIRSFiPIRSF002855. Murein-lipoprotein. 1 hit.
PROSITEiPS51257. PROKAR_LIPOPROTEIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P69776-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKATKLVLGA VILGSTLLAG CSSNAKIDQL SSDVQTLNAK VDQLSNDVNA
60 70
MRSDVQAAKD DAARANQRLD NMATKYRK
Length:78
Mass (Da):8,323
Last modified:July 21, 1986 - v1
Checksum:i19F41D5251913C93
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti29Q → E AA sequence (PubMed:4261992).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
V00302 Genomic DNA. Translation: CAA23580.1.
X68953 Genomic DNA. Translation: CAA48767.1.
U00096 Genomic DNA. Translation: AAC74747.1.
AP009048 Genomic DNA. Translation: BAA16044.1.
S42225 mRNA. Translation: AAB22836.1.
PIRiA90783. LPECW.
RefSeqiNP_416192.1. NC_000913.3.
WP_000648420.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC74747; AAC74747; b1677.
BAA16044; BAA16044; BAA16044.
GeneIDi946175.
KEGGiecj:JW1667.
eco:b1677.
PATRICi32118660. VBIEscCol129921_1748.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
V00302 Genomic DNA. Translation: CAA23580.1.
X68953 Genomic DNA. Translation: CAA48767.1.
U00096 Genomic DNA. Translation: AAC74747.1.
AP009048 Genomic DNA. Translation: BAA16044.1.
S42225 mRNA. Translation: AAB22836.1.
PIRiA90783. LPECW.
RefSeqiNP_416192.1. NC_000913.3.
WP_000648420.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1EQ7X-ray1.90A22-77[»]
1JCCX-ray1.70A/B/C22-77[»]
1JCDX-ray1.30A/B/C22-73[»]
1KFMX-ray2.00A22-77[»]
1KFNX-ray1.65A22-77[»]
1MLPmodel-A/B21-78[»]
1T8ZX-ray1.45A/B/C/D/E22-74[»]
2GUSX-ray1.75A22-77[»]
2GUVX-ray1.40A/B/C/D/E22-77[»]
ProteinModelPortaliP69776.
SMRiP69776.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4260276. 199 interactors.
DIPiDIP-35674N.
IntActiP69776. 4 interactors.
STRINGi511145.b1677.

Proteomic databases

EPDiP69776.
PaxDbiP69776.
PRIDEiP69776.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC74747; AAC74747; b1677.
BAA16044; BAA16044; BAA16044.
GeneIDi946175.
KEGGiecj:JW1667.
eco:b1677.
PATRICi32118660. VBIEscCol129921_1748.

Organism-specific databases

EchoBASEiEB0539.
EcoGeneiEG10544. lpp.

Phylogenomic databases

eggNOGiENOG4105KMX. Bacteria.
COG4238. LUCA.
HOGENOMiHOG000295473.
KOiK06078.
OMAiNCASTNK.

Enzyme and pathway databases

BioCyciEcoCyc:EG10544-MONOMER.
ECOL316407:JW1667-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP69776.
PMAP-CutDBP69776.
PROiP69776.

Family and domain databases

InterProiIPR006817. Lipoprotein_leucine-zipper_dom.
IPR016367. Murein-lipoprotein.
[Graphical view]
PfamiPF04728. LPP. 1 hit.
[Graphical view]
PIRSFiPIRSF002855. Murein-lipoprotein. 1 hit.
PROSITEiPS51257. PROKAR_LIPOPROTEIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiLPP_ECOLI
AccessioniPrimary (citable) accession number: P69776
Secondary accession number(s): P02937, Q53272
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: November 2, 2016
This is version 104 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

About one-third of Lpp is covalently bound to peptidoglycan.

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, 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
  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.