lptD lipopolysaccharide assembly protein LptD [Escherichia coli str. K-12 substr. MG1655] - Gene

Summary

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Official Symbol: lptD
Official Full Name: lipopolysaccharide assembly protein LptD
Primary source: ECOCYC:EG11569
Locus tag: b0054
See related: ASAP:ABE-0000183
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: ECK0055; imp; ostA; yabG
Summary: The outer membrane of an lptD(imp) mutant is permeable to large maltodextrins and sensitive to antibiotics and detergents. lptD is stress induced. [More information is available at EcoGene: EG11569]. The LptD (Increased membrane permeability) protein is an essential outer membrane (OM) protein which is involved with lipopolysaccharide assembly in the outer membrane as part of the outer membrane LPS assembly complex with RlpB . [More information is available at EcoCyc: EG11569].
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Genomic context

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Sequence:: NC_000913.3 (54755..57109, complement)

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?

Edge-strand of BepA interacts with immature LptD on the beta-barrel assembly machine to direct it to on- and off-pathways.
Title: Edge-strand of BepA interacts with immature LptD on the β-barrel assembly machine to direct it to on- and off-pathways.
The Escherichia coli Outer Membrane beta-Barrel Assembly Machinery (BAM) Anchors the Peptidoglycan Layer by Spanning It with All Subunits.
Title: The Escherichia coli Outer Membrane β-Barrel Assembly Machinery (BAM) Anchors the Peptidoglycan Layer by Spanning It with All Subunits.
The results support a model in which the interior wall of BamA acts as a chaperone to catalyze b-barrel assembly via binding with its substrate, LptD.
Title: Formation of a β-barrel membrane protein is catalyzed by the interior surface of the assembly machine protein BamA.
Placement of a substrate LPS molecule also causes an increase in the average separation of the LptD lateral gate strands and a lowering of the energetic barrier to lateral gate opening.
Title: Presence of substrate aids lateral gate separation in LptD.
Data show that LptD is folded around LptE, and both components interact with the two essential beta-barrel assembly machine (Bam) components, BamA and BamD.
Title: Characterization of a stalled complex on the β-barrel assembly machine.
These results demonstrate that multiple periplasmic proteases monitor outer membrane proteins at distinct points in the assembly process as in the case of degradation of the outer membrane protein LptD by the DegP, BepA and YcaL proteases.
Title: Distinctive Roles for Periplasmic Proteases in the Maintenance of Essential Outer Membrane Protein Assembly.
the mutant protein lptD4213 is synthetically lethal with the deletion of dsbB as well as with DsbB inhibitors
Title: Inhibition of virulence-promoting disulfide bond formation enzyme DsbB is blocked by mutating residues in two distinct regions.
findings suggest lptE14 causes poor plugging of the LptD beta barrel and that a reduction of ineffectively plugged LptD-LptE14 complexes in the outer membrane decreases permeability to erythromycin; lptE14 supports a proposed plug-and-barrel LptE-LptD arrangement
Title: Dominant negative lptE mutation that supports a role for LptE as a plug in the LptD barrel.
disulfide bond-dependent protein folding of LptD requires the proper assembly of a two-protein complex to promote disulfide bond rearrangement.
Title: Disulfide rearrangement triggered by translocon assembly controls lipopolysaccharide export.
Data found that the periplasmic disulfide isomerase DsbC cooperates with SurA and the thiol oxidase DsbA in the folding of the essential beta-barrel protein LptD.
Title: The protein-disulfide isomerase DsbC cooperates with SurA and DsbA in the assembly of the essential β-barrel protein LptD.

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Interactions

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Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

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Homology

Orthologs from OrthoDB

Gene Ontology Provided by EcoCyc

Function	Evidence Code	Pubs
enables protein binding	IPI Inferred from Physical Interaction more info	PubMed

Process	Evidence Code	Pubs
involved_in Gram-negative-bacterium-type cell outer membrane assembly	IEA Inferred from Electronic Annotation more info
involved_in Gram-negative-bacterium-type cell outer membrane assembly	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in Gram-negative-bacterium-type cell outer membrane assembly	NAS Non-traceable Author Statement more info	PubMed
involved_in lipopolysaccharide transport	IEA Inferred from Electronic Annotation more info
involved_in lipopolysaccharide transport	NAS Non-traceable Author Statement more info	PubMed

Component	Evidence Code	Pubs
is_active_in cell outer membrane	IBA Inferred from Biological aspect of Ancestor more info
located_in cell outer membrane	IDA Inferred from Direct Assay more info	PubMed
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
part_of transporter complex	IBA Inferred from Biological aspect of Ancestor more info
part_of transporter complex	IDA Inferred from Direct Assay more info	PubMed

General protein information

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Preferred Names: lipopolysaccharide assembly protein LptD

NP_414596.1

EC 7.5.2.5

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

54755..57109 complement

Download

GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

NP_414596.1 lipopolysaccharide assembly protein LptD [Escherichia coli str. K-12 substr. MG1655]

See identical proteins and their annotated locations for NP_414596.1

Status: PROVISIONAL

UniProtKB/TrEMBL

A0A7H9NGN5

Conserved Domains (1) summary

PRK03761
Location:1 → 782

PRK03761; LPS assembly outer membrane complex protein LptD; Provisional