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P69776 (LPP_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 90. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Major outer membrane lipoprotein Lpp
Alternative name(s):
Braun lipoprotein
Murein-lipoprotein
Gene names
Name:lpp
Synonyms:mlpA, mulI
Ordered Locus Names:b1677, JW1667
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length78 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Subunit structure

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. Ref.10 Ref.18 Ref.20

Subcellular location

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. Ref.10 Ref.18

Miscellaneous

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

Sequence similarities

Belongs to the Lpp family.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

itself2EBI-909750,EBI-909750
tonBP029292EBI-909750,EBI-6399993

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2020 Ref.7 Ref.8
Chain21 – 7858Major outer membrane lipoprotein Lpp
PRO_0000018331

Regions

Repeat24 – 3411
Repeat38 – 4811

Amino acid modifications

Modified residue11N-formylmethionine
Modified residue781N6-murein peptidoglycan lysine
Lipidation211N-palmitoyl cysteine Ref.8
Lipidation211S-diacylglycerol cysteine

Experimental info

Mutagenesis221S → 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. Ref.13
Mutagenesis701D → E, G or S: Does not affect the formation of murein-bound lipoprotein. Ref.11
Mutagenesis751K → S or T: Does not affect the formation of murein-bound lipoprotein. Ref.11
Mutagenesis761Y → C, D, E, G, N, P or S: Reduces the formation of murein-bound lipoprotein. Ref.11
Mutagenesis761Y → F, H, I or L: Does not affect the formation of murein-bound lipoprotein. Ref.11
Mutagenesis771R → D or L: Reduces the formation of murein-bound lipoprotein. Ref.11
Mutagenesis781K → R: Abolishes the formation of murein-bound lipoprotein. Ref.11
Sequence conflict291Q → E AA sequence Ref.7

Secondary structure

... 78
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P69776 [UniParc].

Last modified July 21, 1986. Version 1.
Checksum: 19F41D5251913C93

FASTA788,323
        10         20         30         40         50         60 
MKATKLVLGA VILGSTLLAG CSSNAKIDQL SSDVQTLNAK VDQLSNDVNA MRSDVQAAKD 

        70 
DAARANQRLD NMATKYRK 

« Hide

References

« Hide 'large scale' references
[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]"A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 28.0-40.1 min region on the linkage map."
Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T., Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T., Mizobuchi K., Mori H., Mori T., Motomura K. expand/collapse author list , Nakade S., Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y., Wada C., Yamamoto Y., Horiuchi T.
DNA Res. 3:363-377(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[4]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
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]"Protein complexes of the Escherichia coli cell envelope."
Stenberg F., Chovanec P., Maslen S.L., Robinson C.V., Ilag L., von Heijne G., Daley D.O.
J. Biol. Chem. 280:34409-34419(2005) [PubMed] [Europe PMC] [Abstract]
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]"Atomic structure of a tryptophan-zipper pentamer."
Liu J., Yong W., Deng Y., Kallenbach N.R., Lu M.
Proc. Natl. Acad. Sci. U.S.A. 101:16156-16161(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) OF 22-73 OF MUTANT TRP-14.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRLPECW. A90783.
RefSeqNP_416192.1. NC_000913.3.
YP_489939.1. NC_007779.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
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[»]
ProteinModelPortalP69776.
SMRP69776. Positions 22-77.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-35674N.
IntActP69776. 3 interactions.
STRING511145.b1677.

Proteomic databases

PaxDbP69776.
PRIDEP69776.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC74747; AAC74747; b1677.
BAA16044; BAA16044; BAA16044.
GeneID12931282.
946175.
KEGGecj:Y75_p1652.
eco:b1677.
PATRIC32118660. VBIEscCol129921_1748.

Organism-specific databases

EchoBASEEB0539.
EcoGeneEG10544. lpp.

Phylogenomic databases

eggNOGCOG4238.
HOGENOMHOG000295473.
KOK06078.
OMACANTSKV.
OrthoDBEOG6MD98C.

Enzyme and pathway databases

BioCycEcoCyc:EG10544-MONOMER.
ECOL316407:JW1667-MONOMER.

Gene expression databases

GenevestigatorP69776.

Family and domain databases

InterProIPR006817. Lipoprotein_leucine-zipper_dom.
IPR016367. Murein-lipoprotein.
[Graphical view]
PfamPF04728. LPP. 1 hit.
[Graphical view]
PIRSFPIRSF002855. Murein-lipoprotein. 1 hit.
PROSITEPS51257. PROKAR_LIPOPROTEIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP69776.
PMAP-CutDBP69776.
PROP69776.

Entry information

Entry nameLPP_ECOLI
AccessionPrimary (citable) accession number: P69776
Secondary accession number(s): P02937, Q53272
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: July 9, 2014
This is version 90 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene