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ECOLI:LPP

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Species (Taxon ID) Escherichia coli (strain K12). (83333)
Gene Name(s) lpp (synonyms: mlpA, mulI)
Protein Name(s) Major outer membrane prolipoprotein Lpp

Major outer membrane lipoprotein Lpp Braun lipoprotein Murein-lipoprotein

External Links
UniProt P69776
EMBL V00302
X68953
U00096
AP009048
S42225
PIR A90783
RefSeq NP_416192.1
WP_000648420.1
PDB 1EQ7
1JCC
1JCD
1KFM
1KFN
1MLP
1T8Z
2GUS
2GUV
PDBsum 1EQ7
1JCC
1JCD
1KFM
1KFN
1MLP
1T8Z
2GUS
2GUV
ProteinModelPortal P69776
SMR P69776
BioGrid 4260276
DIP DIP-35674N
IntAct P69776
STRING 316385.ECDH10B_1811
TCDB 8.A.99.1.1
EPD P69776
PaxDb P69776
PRIDE P69776
EnsemblBacteria AAC74747
BAA16044
GeneID 946175
KEGG ecj:JW1667
eco:b1677
PATRIC fig|1411691.4.peg.581
EchoBASE EB0539
EcoGene EG10544
eggNOG ENOG4105KMX
COG4238
HOGENOM HOG000295473
KO K06078
OMA NLGNKVD
BioCyc EcoCyc:EG10544-MONOMER
EvolutionaryTrace P69776
PMAP-CutDB P69776
PRO PR:P69776
Proteomes UP000000318
UP000000625
GO GO:0009279
GO:0045203
GO:0016020
GO:0042802
GO:0008289
GO:0042834
GO:0030258
InterPro IPR006817
IPR016367
PANTHER PTHR38763
Pfam PF04728
PIRSF PIRSF002855
PROSITE PS51257

Annotations

Qualifier GO ID GO term name Reference ECO ID ECO term name with/from Aspect Extension Notes Status

involved_in

GO:0030258

lipid modification

PMID:1527082[1]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0016020

membrane

PMID:16858726[2]

ECO:0007005

high throughput direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0009279

cell outer membrane

PMID:322142[3]

ECO:0000303

author statement without traceable support used in manual assertion

C

Seeded From UniProt

complete

enables

GO:0008289

lipid binding

PMID:4575979[4]

ECO:0000303

author statement without traceable support used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0042834

peptidoglycan binding

PMID:21873635[5]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG10544
PANTHER:PTN002215178

F

Seeded From UniProt

complete

part_of

GO:0031230

intrinsic component of cell outer membrane

PMID:21873635[5]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

PANTHER:PTN002215178
UniProtKB:Q7CQN4
UniProtKB:Q8ZPP9

C

Seeded From UniProt

complete

enables

GO:0042802

identical protein binding

PMID:16858726[2]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:P69776

F

Seeded From UniProt

complete

enables

GO:0042802

identical protein binding

PMID:16079137[6]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:P69776

F

Seeded From UniProt

complete

part_of

GO:0045203

integral component of cell outer membrane

PMID:21219470[7]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

enables

GO:0042834

peptidoglycan binding

PMID:4899922[8]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0042834

peptidoglycan binding

PMID:4245367[9]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

part_of

GO:0019867

outer membrane

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR006817

C

Seeded From UniProt

complete

enables

GO:0042834

peptidoglycan binding

PMID:1527082[1]

ECO:0000304

author statement supported by traceable reference used in manual assertion

F

Seeded From UniProt

complete

part_of

GO:0016020

membrane

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0472

C

Seeded From UniProt

complete

part_of

GO:0009279

cell outer membrane

GO_REF:0000037
GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0998
UniProtKB-SubCell:SL-0040

C

Seeded From UniProt

complete

Notes

References

See Help:References for how to manage references in GONUTS.

  1. 1.0 1.1 Zhang, WY et al. (1992) Neither lipid modification nor processing of prolipoprotein is essential for the formation of murein-bound lipoprotein in Escherichia coli. J. Biol. Chem. 267 19631-5 PubMed GONUTS page
  2. 2.0 2.1 Lasserre, JP et al. (2006) A complexomic study of Escherichia coli using two-dimensional blue native/SDS polyacrylamide gel electrophoresis. Electrophoresis 27 3306-21 PubMed GONUTS page
  3. Inouye, S et al. (1977) Amino acid sequence for the peptide extension on the prolipoprotein of the Escherichia coli outer membrane. Proc. Natl. Acad. Sci. U.S.A. 74 1004-8 PubMed GONUTS page
  4. Hantke, K & Braun, V (1973) 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. Eur. J. Biochem. 34 284-96 PubMed GONUTS page
  5. 5.0 5.1 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
  6. Stenberg, F et al. (2005) Protein complexes of the Escherichia coli cell envelope. J. Biol. Chem. 280 34409-19 PubMed GONUTS page
  7. Cowles, CE et al. (2011) The free and bound forms of Lpp occupy distinct subcellular locations in Escherichia coli. Mol. Microbiol. 79 1168-81 PubMed GONUTS page
  8. Braun, V & Rehn, K (1969) Chemical characterization, spatial distribution and function of a lipoprotein (murein-lipoprotein) of the E. coli cell wall. The specific effect of trypsin on the membrane structure. Eur. J. Biochem. 10 426-38 PubMed GONUTS page
  9. Braun, V & Sieglin, U (1970) The covalent murein-lipoprotein structure of the Escherichia coli cell wall. The attachment site of the lipoprotein on the murein. Eur. J. Biochem. 13 336-46 PubMed GONUTS page