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Protein

Major outer membrane prolipoprotein Lpp

Gene

lpp

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: -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.

Miscellaneous

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

GO - Molecular functioni

  • identical protein binding Source: IntAct
  • lipid binding Source: UniProtKB
  • peptidoglycan binding Source: EcoCyc

GO - Biological processi

  • lipid modification Source: UniProtKB

Enzyme and pathway databases

BioCyciEcoCyc:EG10544-MONOMER

Protein family/group databases

TCDBi8.A.99.1.1 the blp braun's lipoprotein (lpp) family

Names & Taxonomyi

Protein namesi
Recommended name:
Major outer membrane prolipoprotein Lpp
Cleaved into the following chain:
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

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
ChainiPRO_00004402531 – 78Major outer membrane prolipoprotein LppAdd BLAST78
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-CutDBiP69776

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

GO - Molecular functioni

Protein-protein interaction databases

BioGridi4260276, 199 interactors
DIPiDIP-35674N
IntActiP69776, 5 interactors
STRINGi316385.ECDH10B_1811

Structurei

Secondary structure

178
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

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

Family and domain databases

InterProiView protein in InterPro
IPR006817 Lipoprotein_leucine-zipper_dom
IPR016367 Murein-lipoprotein
PANTHERiPTHR38763 PTHR38763, 1 hit
PfamiView protein in Pfam
PF04728 LPP, 1 hit
PIRSFiPIRSF002855 Murein-lipoprotein, 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.

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
PATRICifig|1411691.4.peg.581

Similar proteinsi

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, 5 interactors
STRINGi316385.ECDH10B_1811

Protein family/group databases

TCDBi8.A.99.1.1 the blp braun's lipoprotein (lpp) family

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
PATRICifig|1411691.4.peg.581

Organism-specific databases

EchoBASEiEB0539
EcoGeneiEG10544 lpp

Phylogenomic databases

eggNOGiENOG4105KMX Bacteria
COG4238 LUCA
HOGENOMiHOG000295473
KOiK06078

Enzyme and pathway databases

BioCyciEcoCyc:EG10544-MONOMER

Miscellaneous databases

EvolutionaryTraceiP69776
PMAP-CutDBiP69776
PROiPR:P69776

Family and domain databases

InterProiView protein in InterPro
IPR006817 Lipoprotein_leucine-zipper_dom
IPR016367 Murein-lipoprotein
PANTHERiPTHR38763 PTHR38763, 1 hit
PfamiView protein in Pfam
PF04728 LPP, 1 hit
PIRSFiPIRSF002855 Murein-lipoprotein, 1 hit
PROSITEiView protein in PROSITE
PS51257 PROKAR_LIPOPROTEIN, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiLPP_ECOLI
AccessioniPrimary (citable) accession number: P69776
Secondary accession number(s): P02937, Q53272
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: November 7, 2018
This is version 117 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, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

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