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

Gene ID: 946201, updated on 19-Sep-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. 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
  2. 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
  3. Kinetics and phospholipid specificity of apolipoprotein N-acyltransferase. Hillmann F, et al. J Biol Chem, 2011 Aug 12. PMID 21676878, Free PMC Article
  4. Identification of essential residues in apolipoprotein N-acyl transferase, a member of the CN hydrolase family. Vidal-Ingigliardi D, et al. J Bacteriol, 2007 Jun. PMID 17416655, Free PMC Article
  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

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
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