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P69776

- LPP_ECOLI

UniProt

P69776 - LPP_ECOLI

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Protein

Major outer membrane lipoprotein Lpp

Gene

lpp

Organism
Escherichia coli (strain K12)
Status
Reviewed - 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

  1. identical protein binding Source: IntAct
  2. lipid binding Source: UniProtKB
  3. peptidoglycan binding Source: UniProtKB

GO - Biological processi

  1. 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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG10544. lpp.

Subcellular locationi

Cell outer membrane; Lipid-anchor. Cell outer membrane; Peptidoglycan-anchor
Note: Found in the inner leaflet of the outer membrane. Targeted by the SRP/Sec/YidC pathway.

GO - Cellular componenti

  1. cell outer membrane Source: UniProtKB
  2. integral component of cell outer membrane Source: EcoCyc
  3. membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell outer membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi22 – 221S → 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 Publication
Mutagenesisi70 – 701D → E, G or S: Does not affect the formation of murein-bound lipoprotein. 1 Publication
Mutagenesisi75 – 751K → S or T: Does not affect the formation of murein-bound lipoprotein. 1 Publication
Mutagenesisi76 – 761Y → C, D, E, G, N, P or S: Reduces the formation of murein-bound lipoprotein. 1 Publication
Mutagenesisi76 – 761Y → F, H, I or L: Does not affect the formation of murein-bound lipoprotein. 1 Publication
Mutagenesisi77 – 771R → D or L: Reduces the formation of murein-bound lipoprotein. 1 Publication
Mutagenesisi78 – 781K → R: Abolishes the formation of murein-bound lipoprotein. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 20202 PublicationsPROSITE-ProRule annotationAdd
BLAST
Chaini21 – 7858Major outer membrane lipoprotein LppPRO_0000018331Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-formylmethionine1 Publication
Lipidationi21 – 211N-palmitoyl cysteine1 PublicationPROSITE-ProRule annotation
Lipidationi21 – 211S-diacylglycerol cysteine1 PublicationPROSITE-ProRule annotation
Modified residuei78 – 781N6-murein peptidoglycan lysine

Keywords - PTMi

Formylation, Lipoprotein, Palmitate, Peptidoglycan-anchor

Proteomic databases

PaxDbiP69776.
PRIDEiP69776.

Miscellaneous databases

PMAP-CutDBP69776.

Expressioni

Gene expression databases

GenevestigatoriP69776.

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

DIPiDIP-35674N.
IntActiP69776. 3 interactions.
STRINGi511145.b1677.

Structurei

Secondary structure

1
78
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi25 – 7147Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 22-77.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP69776.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati24 – 3411Add
BLAST
Repeati38 – 4811Add
BLAST

Sequence similaritiesi

Belongs to the Lpp family.Curated

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiCOG4238.
HOGENOMiHOG000295473.
KOiK06078.
OMAiCANTSKV.
OrthoDBiEOG6MD98C.

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti29 – 291Q → E AA sequence (PubMed:4261992)Curated

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.
YP_489939.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC74747; AAC74747; b1677.
BAA16044; BAA16044; BAA16044.
GeneIDi12931282.
946175.
KEGGiecj:Y75_p1652.
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 .
PIRi A90783. LPECW.
RefSeqi NP_416192.1. NC_000913.3.
YP_489939.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1EQ7 X-ray 1.90 A 22-77 [» ]
1JCC X-ray 1.70 A/B/C 22-77 [» ]
1JCD X-ray 1.30 A/B/C 22-73 [» ]
1KFM X-ray 2.00 A 22-77 [» ]
1KFN X-ray 1.65 A 22-77 [» ]
1MLP model - A/B 21-78 [» ]
1T8Z X-ray 1.45 A/B/C/D/E 22-74 [» ]
2GUS X-ray 1.75 A 22-77 [» ]
2GUV X-ray 1.40 A/B/C/D/E 22-77 [» ]
ProteinModelPortali P69776.
SMRi P69776. Positions 22-77.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-35674N.
IntActi P69776. 3 interactions.
STRINGi 511145.b1677.

Proteomic databases

PaxDbi P69776.
PRIDEi P69776.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC74747 ; AAC74747 ; b1677 .
BAA16044 ; BAA16044 ; BAA16044 .
GeneIDi 12931282.
946175.
KEGGi ecj:Y75_p1652.
eco:b1677.
PATRICi 32118660. VBIEscCol129921_1748.

Organism-specific databases

EchoBASEi EB0539.
EcoGenei EG10544. lpp.

Phylogenomic databases

eggNOGi COG4238.
HOGENOMi HOG000295473.
KOi K06078.
OMAi CANTSKV.
OrthoDBi EOG6MD98C.

Enzyme and pathway databases

BioCyci EcoCyc:EG10544-MONOMER.
ECOL316407:JW1667-MONOMER.

Miscellaneous databases

EvolutionaryTracei P69776.
PMAP-CutDB P69776.
PROi P69776.

Gene expression databases

Genevestigatori P69776.

Family and domain databases

InterProi IPR006817. Lipoprotein_leucine-zipper_dom.
IPR016367. Murein-lipoprotein.
[Graphical view ]
Pfami PF04728. LPP. 1 hit.
[Graphical view ]
PIRSFi PIRSF002855. Murein-lipoprotein. 1 hit.
PROSITEi PS51257. PROKAR_LIPOPROTEIN. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "DNA sequence of the gene for the outer membrane lipoprotein of E. coli: an extremely AT-rich promoter."
    Nakamura K., Inouye M.
    Cell 18:1109-1117(1979) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: B.
  2. "Messenger ribonucleic acid of the lipoprotein of the Escherichia coli outer membrane. II. The complete nucleotide sequence."
    Nakamura K., Pirtle R.M., Pirtle I.L., Takeishi K., Inouye M.
    J. Biol. Chem. 255:210-216(1980) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  5. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  6. "Amino acid sequence for the peptide extension on the prolipoprotein of the Escherichia coli outer membrane."
    Inouye S., Wang S., Sekizawa J., Halegoua S., Inouye M.
    Proc. Natl. Acad. Sci. U.S.A. 74:1004-1008(1977) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1-20, FORMYLATION AT MET-1.
  7. "Sequence of the murein-lipoprotein and the attachment site of the lipid."
    Braun V., Bosch V.
    Eur. J. Biochem. 28:51-69(1972) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 21-78.
  8. "Covalent binding of lipid to protein. Diglyceride and amide-linked fatty acid at the N-terminal end of the murein-lipoprotein of the Escherichia coli outer membrane."
    Hantke K., Braun V.
    Eur. J. Biochem. 34:284-296(1973) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 21-24, DIACYLGLYCEROL AT CYS-21, PALMITOYLATION AT CYS-21.
  9. "Poly(A) RNA in Escherichia coli: nucleotide sequence at the junction of the lpp transcript and the polyadenylate moiety."
    Cao G.J., Sarkar N.
    Proc. Natl. Acad. Sci. U.S.A. 89:7546-7550(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 44-78.
    Strain: SK5726.
  10. "Trimeric structure and localization of the major lipoprotein in the cell surface of Escherichia coli."
    Choi D.-S., Yamada H., Mizuno T., Mizushima S.
    J. Biol. Chem. 261:8953-8957(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT, SUBCELLULAR LOCATION.
  11. "Alterations of the carboxyl-terminal amino acid residues of Escherichia coli lipoprotein affect the formation of murein-bound lipoprotein."
    Zhang W.-Y., Wu H.C.
    J. Biol. Chem. 267:19560-19564(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF ASP-70; LYS-75; TYR-76; ARG-77 AND LYS-78.
    Strain: K12.
  12. "Escherichia coli proteome analysis using the gene-protein database."
    VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.
    Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY 2D-GEL.
  13. "Lethality of the covalent linkage between mislocalized major outer membrane lipoprotein and the peptidoglycan of Escherichia coli."
    Yakushi T., Tajima T., Matsuyama S., Tokuda H.
    J. Bacteriol. 179:2857-2862(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF SER-22.
    Strain: K12 / ATCC 35607 / JM83.
  14. "TolB protein of Escherichia coli K-12 interacts with the outer membrane peptidoglycan-associated proteins Pal, Lpp and OmpA."
    Clavel T., Germon P., Vianney A., Portalier R., Lazzaroni J.-C.
    Mol. Microbiol. 29:359-367(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TOLB.
  15. "Pal lipoprotein of Escherichia coli plays a major role in outer membrane integrity."
    Cascales E., Bernadac A., Gavioli M., Lazzaroni J.-C., Lloubes R.
    J. Bacteriol. 184:754-759(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PAL.
  16. "TonB interacts with nonreceptor proteins in the outer membrane of Escherichia coli."
    Higgs P.I., Letain T.E., Merriam K.K., Burke N.S., Park H., Kang C., Postle K.
    J. Bacteriol. 184:1640-1648(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TONB.
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  17. "Targeting and translocation of two lipoproteins in Escherichia coli via the SRP/Sec/YidC pathway."
    Froderberg L., Houben E.N., Baars L., Luirink J., de Gier J.W.
    J. Biol. Chem. 279:31026-31032(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: TRANSLOCATION BY SRP/SEC/YIDC PATHWAY.
  18. Cited for: SUBUNIT, SUBCELLULAR LOCATION.
    Strain: BL21-DE3.
  19. "The double helix coiled coil structure of murein lipoprotein from Escherichia coli."
    McLachlan A.D.
    J. Mol. Biol. 121:493-506(1978) [PubMed] [Europe PMC] [Abstract]
    Cited for: 3D-STRUCTURE MODELING.
  20. "Core structure of the outer membrane lipoprotein from Escherichia coli at 1.9 A resolution."
    Shu W., Liu J., Ji H., Lu M.
    J. Mol. Biol. 299:1101-1112(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 22-77, SUBUNIT.
  21. "An alanine-zipper structure determined by long range intermolecular interactions."
    Liu J., Lu M.
    J. Biol. Chem. 277:48708-48713(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.3 ANGSTROMS) OF 22-71 OF MUTANT ALA-14.
  22. "Core side-chain packing and backbone conformation in Lpp-56 coiled-coil mutants."
    Liu J., Cao W., Lu M.
    J. Mol. Biol. 318:877-888(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 22-77 OF MUTANTS ALA-5 AND ALA-7.
  23. "Zinc-mediated helix capping in a triple-helical protein."
    Liu J., Dai J., Lu M.
    Biochemistry 42:5657-5664(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 22-77 OF MUTANT ALA-10(56).
  24. Cited for: X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) OF 22-73 OF MUTANT TRP-14.

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 26, 2014
This is version 93 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

External Data

Dasty 3