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    lnt apolipoprotein N-acyltransferase [ Escherichia coli str. K-12 substr. MG1655 ]

    Gene ID: 946201, updated on 3-Dec-2024

    Summary

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    Official Symbol
    lnt
    Official Full Name
    apolipoprotein N-acyltransferase
    Primary source
    ECOCYC:EG10168
    Locus tag
    b0657
    See related
    ASAP:ABE-0002250
    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
    cutE; ECK0649
    Summary
    Apolipoprotein N-acyltransferase activity transfers palmitate to apolipoproteins, resulting in the maturation of lipoproteins from apolipoprotein precursors . [More information is available at EcoCyc: EG10168].
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    Genomic context

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    Sequence:
    NC_000913.3 (689343..690881, complement)

    NC_000913.3Genomic Context describing neighboring genes Neighboring gene ncRNA Neighboring gene glutamate/aspartate ABC transporter periplasmic binding protein Neighboring gene IS5 family transposase and trans-activator Neighboring gene CorC-HlyC family protein YbeX Neighboring gene endoribonuclease YbeY Neighboring gene PhoH-like protein

    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. Residues located on membrane-embedded flexible loops are essential for the second step of the apolipoprotein N-acyltransferase reaction. Gélis-Jeanvoine S, et al. Mol Microbiol, 2015 Feb. PMID 25471278
    2. Cloning and characterization of cutE, a gene involved in copper transport in Escherichia coli. Rogers SD, et al. J Bacteriol, 1991 Nov. PMID 1938881, Free PMC Article
    3. Identification and subcellular localization of apolipoprotein N-acyltransferase in Escherichia coli. Gupta SD, et al. FEMS Microbiol Lett, 1991 Feb. PMID 2032623
    4. Phosphatidylethanolamine is not essential for the N-acylation of apolipoprotein in Escherichia coli. Gupta SD, et al. J Biol Chem, 1991 May 25. PMID 2033085
    5. Biophysical characterization and stabilization of detergent-solubilized lipoprotein N-acyl transferase from P. aeruginosa and E. coli. Wiktor M, et al. Biochim Biophys Acta Biomembr, 2018 Jun. PMID 29573991

    See all (22) citations in PubMed

    GeneRIFs: Gene References Into Functions

    What's a GeneRIF?
    1. High-resolution crystal structures were obtained for membrane integral Lnt. Thermal stability was measured by circular dichroism. The detergent-solubilized form possessed N-acylation activity.
      Title: Biophysical characterization and stabilization of detergent-solubilized lipoprotein N-acyl transferase from P. aeruginosa and E. coli.
    2. data suggest that amino acids located on flexible cytoplasmic and periplasmic loops, predicted to be membrane embedded, are required for efficient N-acylation of lipoproteins
      Title: Residues located on membrane-embedded flexible loops are essential for the second step of the apolipoprotein N-acyltransferase reaction.
    3. Essential residues in Lnt were identified by using site-directed mutagenesis and complementation assay; besides the catalytic triad E267-K335-C387, 4 residues that directly affect the modification of Braun's lipoprotein Lpp are required for Lnt function.
      Title: Identification of essential residues in apolipoprotein N-acyl transferase, a member of the CN hydrolase family.
    4. Lnt is an essential protein in E. coli and the lethality is partially because of the retention of apoLpp in the plasma membrane
      Title: Depletion of apolipoprotein N-acyltransferase causes mislocalization of outer membrane lipoproteins in 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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    Homology

    Gene Ontology Provided by EcoCyc

    Function Evidence Code Pubs
    enables N-acyltransferase activity IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables N-acyltransferase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables acyltransferase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables protein binding IPI
    Inferred from Physical Interaction
    more info
    		 PubMed 
    Process Evidence Code Pubs
    acts_upstream_of_or_within lipoprotein biosynthetic process IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    involved_in lipoprotein biosynthetic process IEA
    Inferred from Electronic Annotation
    more info
    		  
    acts_upstream_of_or_within lipoprotein biosynthetic process IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    Component Evidence Code Pubs
    located_in membrane IEA
    Inferred from Electronic Annotation
    more info
    		  
    located_in outer membrane-bounded periplasmic space IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    located_in plasma membrane IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    located_in plasma membrane IEA
    Inferred from Electronic Annotation
    more info
    		  

    General protein information

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    Preferred Names
    apolipoprotein N-acyltransferase
    NP_415190.1

    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
      689343..690881 complement
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NP_415190.1 apolipoprotein N-acyltransferase [Escherichia coli str. K-12 substr. MG1655]

      See identical proteins and their annotated locations for NP_415190.1

      Status: PROVISIONAL

      UniProtKB/TrEMBL
      A0A8S7EMI4
      Conserved Domains (1) summary
      PRK00302
      Location:9 → 512
      lnt; apolipoprotein N-acyltransferase; Reviewed
    Nucleotide Protein
    Heading Accession and Version

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