lpp murein lipoprotein [Escherichia coli str. K-12 substr. MG1655] - Gene

Summary

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Official Symbol: lpp
Official Full Name: murein lipoprotein
Primary source: ECOCYC:EG10544
Locus tag: b1677
See related: ASAP:ABE-0005603
Gene type: protein coding
RefSeq status: PROVISIONAL
Organism: Escherichia coli str. K-12 substr. MG1655 (strain: K-12, substrain: MG1655)
Lineage: Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia
Also known as: ECK1673; mlpA
Summary: Lpp binds peptidoglycan, one third has a covalent bond to murein. [More information is available at EcoGene: EG10544]. Lpp, the major lipoprotein, is one of the most abundant proteins in Escherichia coli and is necessary for the stabilization and integrity of the bacterial cell envelope . [More information is available at EcoCyc: EG10544].
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Genomic context

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Sequence:: NC_000913.3 (1757421..1757657)

NC_000913.3 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Go to reference sequence details

Genomic Sequence:: NC_000913.3

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

When less is more: shortening the Lpp protein leads to increased vancomycin resistance in Escherichia coli.
Title: When less is more: shortening the Lpp protein leads to increased vancomycin resistance in Escherichia coli.
Adaptation of the periplasm to maintain spatial constraints essential for cell envelope processes and cell viability.
Title: Adaptation of the periplasm to maintain spatial constraints essential for cell envelope processes and cell viability.
Cleavage of Braun's lipoprotein Lpp from the bacterial peptidoglycan by a paralog of l,d-transpeptidases, LdtF.
Title: Cleavage of Braun's lipoprotein Lpp from the bacterial peptidoglycan by a paralog of l,d-transpeptidases, LdtF.
Here, the authors demonstrate that a mutant variant of an outer-membrane lipoprotein, Lpp(+Leu), can function as a novel allosteric effector that changes the dynamic range of DegP activity.
Title: Tripodal Lipoprotein Variants with C-Terminal Hydrophobic Residues Allosterically Modulate Activity of the DegP Protease.
From this work, the authors conclude that outer membrane vesicles production can be driven by distinct Lpp concentration-dependent and Lpp concentration-independent pathways.
Title: Modulation of bacterial outer membrane vesicle production by envelope structure and content.
The free and bound forms of Lpp are not largely associated with each other, but are found in distinct subcellular locations.
Title: The free and bound forms of Lpp occupy distinct subcellular locations in Escherichia coli.
The free form of Lpp is an integral outer membrane protein whose C-terminus is exposed on the cell surface.
Title: The double life of a bacterial lipoprotein.
N-terminus verified by Edman degradation on mature peptide
Title: 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.
Stable E. coli mRNAs as lpp and ompA were drastically destabilized immediately after phage T4 infection.
Title: Phage-induced change in the stability of mRNAs.
analysis of synthesis of cross-linked murein and its attachment to sacculi by PBP1A from Escherichia coli
Title: In vitro synthesis of cross-linked murein and its attachment to sacculi by PBP1A from Escherichia coli.

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General gene information

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Homology

Orthologs from OrthoDB

Gene Ontology Provided by EcoCyc

Function	Evidence Code	Pubs
enables identical protein binding	IPI Inferred from Physical Interaction more info	PubMed
enables lipid binding	IEA Inferred from Electronic Annotation more info
enables lipid binding	NAS Non-traceable Author Statement more info	PubMed
enables peptidoglycan binding	IEA Inferred from Electronic Annotation more info
enables peptidoglycan binding	TAS Traceable Author Statement more info	PubMed
enables protein binding	IPI Inferred from Physical Interaction more info	PubMed

Process	Evidence Code	Pubs
involved_in lipid modification	IEA Inferred from Electronic Annotation more info
involved_in lipid modification	IMP Inferred from Mutant Phenotype more info	PubMed
acts_upstream_of_or_within periplasmic space organization	IDA Inferred from Direct Assay more info	PubMed
involved_in periplasmic space organization	IEA Inferred from Electronic Annotation more info

Component	Evidence Code	Pubs
located_in cell outer membrane	IEA Inferred from Electronic Annotation more info
located_in cell outer membrane	NAS Non-traceable Author Statement more info	PubMed
located_in extracellular region	IEA Inferred from Electronic Annotation more info
located_in membrane	HDA more info	PubMed
located_in outer membrane	IEA Inferred from Electronic Annotation more info
located_in outer membrane-bounded periplasmic space	IDA Inferred from Direct Assay more info	PubMed

General protein information

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Preferred Names: murein lipoprotein

NCBI Reference Sequences (RefSeq)

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Genome Annotation

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference assembly

Genomic

NC_000913.3 Reference assembly

Range

1757421..1757657

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GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

NP_416192.1 murein lipoprotein [Escherichia coli str. K-12 substr. MG1655]

See identical proteins and their annotated locations for NP_416192.1

Status: PROVISIONAL

UniProtKB/TrEMBL

A0A5B9AYY1

Conserved Domains (1) summary

PRK15396
Location:1 → 78

PRK15396; major outer membrane lipoprotein