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narJ nitrate reductase 1 molybdenum cofactor assembly chaperone [ Escherichia coli str. K-12 substr. MG1655 ]

Gene ID: 945807, updated on 23-Nov-2023

Summary

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Gene symbol
narJ
Gene description
nitrate reductase 1 molybdenum cofactor assembly chaperone
Primary source
ASAP:ABE-0004123
Locus tag
b1226
See related
ECOCYC:EG10641
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
ECK1220
Summary
NarJ has two NarG binding sites: one for Mo insertion and one to block membrane attachment via NarI until activation is complete. [More information is available at EcoGene: EG10641]. NarJ is parto of the redox enzyme maturation protein (REMP) family of chaperones . [More information is available at EcoCyc: EG10641].
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Genomic context

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Sequence:
NC_000913.3 (1285139..1285849)

NC_000913.3Genomic Context describing neighboring genes Neighboring gene nitrate:nitrite antiporter NarK Neighboring gene ncRNA Neighboring gene nitrate reductase A subunit alpha Neighboring gene nitrate reductase A subunit beta Neighboring gene nitrate reductase A subunit gamma Neighboring gene putative uncharacterized protein YchS

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. Biogenesis of a respiratory complex is orchestrated by a single accessory protein. Lanciano P, et al. J Biol Chem, 2007 Jun 15. PMID 17442677
  2. Characterization of NarJ, a system-specific chaperone required for nitrate reductase biogenesis in Escherichia coli. Liu X, et al. J Biol Chem, 1997 Sep 26. PMID 9305880
  3. Basis of recognition between the NarJ chaperone and the N-terminus of the NarG subunit from Escherichia coli nitrate reductase. Zakian S, et al. FEBS J, 2010 Apr. PMID 20236317
  4. In vivo associations of Escherichia coli NarJ with a peptide of the first 50 residues of nitrate reductase catalytic subunit NarG. Li H, et al. Can J Microbiol, 2009 Feb. PMID 19295650
  5. Twin-arginine translocase may have a role in the chaperone function of NarJ from Escherichia coli. Chan CS, et al. Biochem Biophys Res Commun, 2006 Apr 28. PMID 16540088

See all (31) citations in PubMed

GeneRIFs: Gene References Into Functions

What's a GeneRIF?
  1. NarJ associated with a peptide of the first 50 residues of nitrate reductase catalytic subunit NarG.
    Title: In vivo associations of Escherichia coli NarJ with a peptide of the first 50 residues of nitrate reductase catalytic subunit NarG.
  2. Data demonstrate that NarJ has a multifunctional role in nitrate reductase A biosynthesis, as it orchestrates both the maturation and the assembly steps.
    Title: Biogenesis of a respiratory complex is orchestrated by a single accessory protein.
  3. The interactome of NarJ exhibits Tat-dependence.
    Title: Twin-arginine translocase may have a role in the chaperone function of NarJ from Escherichia coli.
  4. the NarJ chaperone interacts at two distinct binding sites of the apoenzyme
    Title: NarJ chaperone binds on two distinct sites of the aponitrate reductase of Escherichia coli to coordinate molybdenum cofactor insertion and assembly.
Submit: New GeneRIF Correction

Pathways from PubChem

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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 metallochaperone activity IBA
Inferred from Biological aspect of Ancestor
more info
  
enables metallochaperone activity IMP
Inferred from Mutant Phenotype
more info
 PubMed 
enables protein binding IPI
Inferred from Physical Interaction
more info
 PubMed 
enables unfolded protein binding IEA
Inferred from Electronic Annotation
more info
  
Process Evidence Code Pubs
involved_in chaperone-mediated protein complex assembly IBA
Inferred from Biological aspect of Ancestor
more info
  
involved_in chaperone-mediated protein complex assembly IDA
Inferred from Direct Assay
more info
 PubMed 
involved_in chaperone-mediated protein complex assembly IEA
Inferred from Electronic Annotation
more info
  
acts_upstream_of_or_within chaperone-mediated protein complex assembly IMP
Inferred from Mutant Phenotype
more info
 PubMed 
involved_in nitrate assimilation IBA
Inferred from Biological aspect of Ancestor
more info
  
involved_in nitrate assimilation IDA
Inferred from Direct Assay
more info
 PubMed 
involved_in nitrate assimilation IEA
Inferred from Electronic Annotation
more info
  
Component Evidence Code Pubs
located_in cytoplasm IDA
Inferred from Direct Assay
more info
 PubMed 
located_in cytoplasm IEA
Inferred from Electronic Annotation
more info
  

General protein information

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Preferred Names
nitrate reductase 1 molybdenum cofactor assembly chaperone

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
    1285139..1285849
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. NP_415744.1 nitrate reductase 1 molybdenum cofactor assembly chaperone [Escherichia coli str. K-12 substr. MG1655]

    See identical proteins and their annotated locations for NP_415744.1

    Status: PROVISIONAL

    UniProtKB/TrEMBL
    A0A5N3CZB5, F4V198
    Conserved Domains (1) summary
    cl00958
    Location:1 → 234
    Nitrate_red_del; Nitrate reductase delta subunit
Nucleotide Protein
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