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pepN aminopeptidase N [ Escherichia coli str. K-12 substr. MG1655 ]

Gene ID: 947253, updated on 6-Oct-2023

Summary

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Gene symbol
pepN
Gene description
aminopeptidase N
Primary source
ASAP:ABE-0003171
Locus tag
b0932
See related
ECOCYC:EG10696
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
ECK0923
Summary
Aminopeptidase N is an aminoendopeptidase, capable of breaking down small peptides as well as whole, native proteins . [More information is available at EcoCyc: EG10696].
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Genomic context

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Sequence:
NC_000913.3 (990622..993234)

NC_000913.3Genomic Context describing neighboring genes Neighboring gene asparagine--tRNA ligase Neighboring gene nicotinate phosphoribosyltransferase Neighboring gene aliphatic sulfonate ABC transporter ATP binding subunit Neighboring gene aliphatic sulfonate ABC transporter membrane subunit Neighboring gene FMNH2-dependent alkanesulfonate monooxygenase Neighboring gene aliphatic sulfonate ABC transporter periplasmic binding 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. Structural basis for the inhibition of M1 family aminopeptidases by the natural product actinonin: Crystal structure in complex with E. coli aminopeptidase N. Ganji RJ, et al. Protein Sci, 2015 May. PMID 25644575, Free PMC Article
  2. Catalytic activity of Peptidase N is required for adaptation of Escherichia coli to nutritional downshift and high temperature stress. Bhosale M, et al. Microbiol Res, 2013 Jan 15. PMID 22766257
  3. Structure of aminopeptidase N from Escherichia coli complexed with the transition-state analogue aminophosphinic inhibitor PL250. Fournié-Zaluski MC, et al. Acta Crystallogr D Biol Crystallogr, 2009 Aug. PMID 19622865, Free PMC Article
  4. Interaction between two residues in the inter-domain interface of Escherichia coli peptidase N modulates catalytic activity. Kumar A, et al. Protein Pept Lett, 2009. PMID 19356140
  5. Structural basis for the unusual specificity of Escherichia coli aminopeptidase N. Addlagatta A, et al. Biochemistry, 2008 May 13. PMID 18416562

See all (41) citations in PubMed

GeneRIFs: Gene References Into Functions

What's a GeneRIF?
  1. Here we describe the crystal structure of Escherichia coli aminopeptidase N (ePepN), a model protein of the M1 family aminopeptidases in complex with actinonin
    Title: Structural basis for the inhibition of M1 family aminopeptidases by the natural product actinonin: Crystal structure in complex with E. coli aminopeptidase N.
  2. Importantly, growth profiles of DeltapepN upon expression of wild-type or mutant proteins demonstrated the importance of catalytic activity during nutritional downshift and high temperature but not sodium salicylate-induced stress.
    Title: Catalytic activity of Peptidase N is required for adaptation of Escherichia coli to nutritional downshift and high temperature stress.
  3. Data show that PepN can effectively process heptapeptide-nucleotide microcin C (McC).
    Title: Escherichia coli peptidase A, B, or N can process translation inhibitor microcin C.
  4. N-terminus verified by Edman degradation on complete protein
    Title: Nucleotide sequence of the promoter and amino-terminal encoding region of the Escherichia coli pepN gene.
  5. structures of the ligand-free form and the enzyme-bestatin complex were determined at 1.5- and 1.6-A resolution, respectively
    Title: Crystal structure of aminopeptidase N (proteobacteria alanyl aminopeptidase) from Escherichia coli and conformational change of methionine 260 involved in substrate recognition.
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 aminopeptidase activity IDA
Inferred from Direct Assay
more info
 PubMed 
enables aminopeptidase activity IEA
Inferred from Electronic Annotation
more info
  
enables hydrolase activity IEA
Inferred from Electronic Annotation
more info
  
enables identical protein binding IPI
Inferred from Physical Interaction
more info
 PubMed 
enables metal ion binding IEA
Inferred from Electronic Annotation
more info
  
enables metallopeptidase activity IEA
Inferred from Electronic Annotation
more info
  
enables peptidase activity IEA
Inferred from Electronic Annotation
more info
  
enables protein binding IPI
Inferred from Physical Interaction
more info
 PubMed 
enables zinc ion binding IEA
Inferred from Electronic Annotation
more info
  
Process Evidence Code Pubs
involved_in proteolysis IEA
Inferred from Electronic Annotation
more info
  
acts_upstream_of_or_within proteolysis IMP
Inferred from Mutant Phenotype
more info
 PubMed 
Component Evidence Code Pubs
located_in membrane IEA
Inferred from Electronic Annotation
more info
  
located_in plasma membrane IEA
Inferred from Electronic Annotation
more info
  

General protein information

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Preferred Names
aminopeptidase N
NP_415452.1

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
    990622..993234
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. NP_415452.1 aminopeptidase N [Escherichia coli str. K-12 substr. MG1655]

    See identical proteins and their annotated locations for NP_415452.1

    Status: PROVISIONAL

    UniProtKB/TrEMBL
    A0A8S7JSA0
    Conserved Domains (1) summary
    PRK14015
    Location:1 → 870
    pepN; aminopeptidase N; Provisional
Nucleotide Protein
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