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    lptE lipopolysaccharide assembly protein LptE [ Escherichia coli str. K-12 substr. MG1655 ]

    Gene ID: 946257, updated on 23-Nov-2023

    Summary

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    Gene symbol
    lptE
    Gene description
    lipopolysaccharide assembly protein LptE
    Primary source
    ASAP:ABE-0002194
    Locus tag
    b0641
    See related
    ECOCYC:EG10855
    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
    ECK0634; rlpB
    Summary
    First 18 aa are a type II signal peptide. [More information is available at EcoGene: EG10855]. LptE (formally RlpB) is involved with lipopolysaccharide assembly in the outer membrane as part of the outer membrane LPS assembly complex with Imp . [More information is available at EcoCyc: EG10855].
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    Genomic context

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    Sequence:
    NC_000913.3 (671605..672186, complement)

    NC_000913.3Genomic Context describing neighboring genes Neighboring gene putative adenosylcobalamin phosphatase/alpha-ribazole phosphatase Neighboring gene nicotinate-nucleotide adenylyltransferase Neighboring gene DNA polymerase III subunit delta Neighboring gene leucine--tRNA ligase Neighboring gene DUF1451 domain-containing protein YbeL

    Genomic regions, transcripts, and products

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    Genomic Sequence:
    NC_000913.3

    Go to nucleotide: Graphics FASTA GenBank

    Bibliography

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    Related articles in PubMed

    1. LptE binds to and alters the physical state of LPS to catalyze its assembly at the cell surface. Malojčić G, et al. Proc Natl Acad Sci U S A, 2014 Jul 1. PMID 24938785, Free PMC Article
    2. Dominant negative lptE mutation that supports a role for LptE as a plug in the LptD barrel. Grabowicz M, et al. J Bacteriol, 2013 Mar. PMID 23316047, Free PMC Article
    3. The complex that inserts lipopolysaccharide into the bacterial outer membrane forms a two-protein plug-and-barrel. Freinkman E, et al. Proc Natl Acad Sci U S A, 2011 Feb 8. PMID 21257904, Free PMC Article
    4. Nonconsecutive disulfide bond formation in an essential integral outer membrane protein. Ruiz N, et al. Proc Natl Acad Sci U S A, 2010 Jul 6. PMID 20566849, Free PMC Article
    5. Characterization of the two-protein complex in Escherichia coli responsible for lipopolysaccharide assembly at the outer membrane. Chng SS, et al. Proc Natl Acad Sci U S A, 2010 Mar 23. PMID 20203010, Free PMC Article

    See all (24) citations in PubMed

    GeneRIFs: Gene References Into Functions

    What's a GeneRIF?
    1. 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.
    2. LptE binds to and alters the physical state of LPS to catalyze its assembly at the cell surface.
      Title: LptE binds to and alters the physical state of LPS to catalyze its assembly at the cell surface.
    3. 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.
    4. Data show that oxidation of LptD is not required for the formation of the LptD/E complex but it is essential for function.
      Title: Nonconsecutive disulfide bond formation in an essential integral outer membrane protein.
    5. LptD contains a soluble N-terminal domain and a C-terminal transmembrane domain. LptE stabilizes LptD by interacting with the C-terminal domain of LptD. LptE binds LPS specifically and may serve as a substrate recognition site at the outer membrane.
      Title: Characterization of the two-protein complex in Escherichia coli responsible for lipopolysaccharide assembly at the outer membrane.
    6. Results show that RlpB is essential for cell viability and that the Imp/RlpB complex is responsible for lipopolysaccharides reaching the outer surface of the outer membrane.
      Title: Identification of a protein complex that assembles lipopolysaccharide in the outer membrane of Escherichia coli.
    Submit: New GeneRIF Correction

    Interactions

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    Products Interactant Other Gene Complex Source Pubs Description

    General gene information

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    Gene Ontology Provided by EcoCyc

    Function Evidence Code Pubs
    enables lipopolysaccharide binding IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    enables lipopolysaccharide binding IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    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 IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    involved_in Gram-negative-bacterium-type cell outer membrane assembly IEA
    Inferred from Electronic Annotation
    more info
    		  
    acts_upstream_of_or_within 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 IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    acts_upstream_of_or_within lipopolysaccharide transport IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    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 
    located_in membrane IEA
    Inferred from Electronic Annotation
    more info
    		  
    located_in outer membrane IEA
    Inferred from Electronic Annotation
    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 LptE
    NP_415174.1

    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

    1. NC_000913.3 Reference assembly

      Range
      671605..672186 complement
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NP_415174.1 lipopolysaccharide assembly protein LptE [Escherichia coli str. K-12 substr. MG1655]

      See identical proteins and their annotated locations for NP_415174.1

      Status: PROVISIONAL

      UniProtKB/TrEMBL
      A0A5B9ADK9, A0A6M9WT04, A0A7D7PT64, A0A8S7EG23
      Conserved Domains (1) summary
      PRK10796
      Location:1 → 189
      PRK10796; LPS-assembly lipoprotein RlpB; Provisional
    Nucleotide Protein
    Heading Accession and Version

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