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

Gene ID: 946201, updated on 30-Jul-2025
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
REVIEWED
Organism
Escherichia coli str. K-12 substr. MG1655 (strain: K-12, substrain: MG1655)
Lineage
Bacteria; Pseudomonadati; 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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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 transposase and trans-activator Neighboring gene CorC-HlyC family protein YbeX Neighboring gene endoribonuclease YbeY Neighboring gene PhoH-like protein

Genomic Sequence:
NC_000913.3

Go to nucleotide: Graphics FASTA GenBank

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. Characterization of a temperature-sensitive mutant of Salmonella typhimurium defective in apolipoprotein N-acyltransferase. Gupta SD, et al. J Biol Chem, 1993 Aug 5. PMID 8344936

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
Products Interactant Other Gene Complex Source Pubs Description

Homology

Gene Ontology Provided by EcoCyc

Function Evidence Code Pubs
enables N-acyltransferase activity IBA
Inferred from Biological aspect of Ancestor
more info
  
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 
enables transferase activity IEA
Inferred from Electronic Annotation
more info
  
Process Evidence Code Pubs
involved_in lipoprotein biosynthetic process IBA
Inferred from Biological aspect of Ancestor
more info
  
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 
is_active_in plasma membrane IBA
Inferred from Biological aspect of Ancestor
more info
  
located_in plasma membrane IDA
Inferred from Direct Assay
more info
 PubMed 
located_in plasma membrane IEA
Inferred from Electronic Annotation
more info
  
Preferred Names
apolipoprotein N-acyltransferase
NP_415190.1

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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

    See identical proteins and their annotated locations for NP_415190.1

    Status: REVIEWED

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