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P69776

- LPP_ECOLI

UniProt

P69776 - LPP_ECOLI

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
  1. 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
    4. protein binding Source: IntAct

    GO - Biological processi

    1. lipid modification Source: UniProtKB

    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

    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 – 7147

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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

    MKATKLVLGA VILGSTLLAG CSSNAKIDQL SSDVQTLNAK VDQLSNDVNA   50
    MRSDVQAAKD DAARANQRLD NMATKYRK 78
    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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:
    PDBe
    RCSB PDB
    PDBj
    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

    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: October 1, 2014
    This is version 91 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