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napD NapA signal peptide-binding chaperone NapD [ Escherichia coli str. K-12 substr. MG1655 ]

Gene ID: 945187, updated on 3-Dec-2024
Official Symbol
napD
Official Full Name
NapA signal peptide-binding chaperone NapD
Primary source
ECOCYC:EG12143
Locus tag
b2207
See related
ASAP:ABE-0007291
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
ECK2199; yojF
Summary
Nap has a strong anti-transport actvity in vitro, but is essential for NapA activity and transport in vivo. [More information is available at EcoGene: EG12143]. NapD is a dedicated chaperone for NapA, the molybdoprotein subunit of the periplasmic nitrate reductase. [More information is available at EcoCyc: EG12143].
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Sequence:
NC_000913.3 (2302750..2303013, complement)

NC_000913.3Genomic Context describing neighboring genes Neighboring gene periplasmic nitrate reductase cytochrome c550 protein Neighboring gene ferredoxin-type protein NapH Neighboring gene ferredoxin-type protein NapG Neighboring gene periplasmic nitrate reductase subunit NapA Neighboring gene ferredoxin-type protein Neighboring gene uncharacterized protein YojO Neighboring gene serine protease inhibitor ecotin

Genomic Sequence:
NC_000913.3

Go to nucleotide: Graphics FASTA GenBank

Related articles in PubMed

  1. Characterization of a periplasmic nitrate reductase in complex with its biosynthetic chaperone. Dow JM, et al. FEBS J, 2014 Jan. PMID 24314029, Free PMC Article
  2. Overlapping transport and chaperone-binding functions within a bacterial twin-arginine signal peptide. Grahl S, et al. Mol Microbiol, 2012 Mar. PMID 22329966, Free PMC Article
  3. Structural diversity in twin-arginine signal peptide-binding proteins. Maillard J, et al. Proc Natl Acad Sci U S A, 2007 Oct 2. PMID 17901208, Free PMC Article
  4. Comparing system-specific chaperone interactions with their Tat dependent redox enzyme substrates. Chan CS, et al. FEBS Lett, 2010 Nov 19. PMID 20974141, Free PMC Article
  5. Nitrate reduction to ammonia by enteric bacteria: redundancy, or a strategy for survival during oxygen starvation? Cole J. FEMS Microbiol Lett, 1996 Feb 1. PMID 8919448

See all (18) citations in PubMed

GeneRIFs: Gene References Into Functions

What's a GeneRIF?
  1. The NapA signal peptide adopts an alpha-helical conformation upon binding NapD.
    Title: Overlapping transport and chaperone-binding functions within a bacterial twin-arginine signal peptide.
Submit: New GeneRIF Correction
Products Interactant Other Gene Complex Source Pubs Description

Homology

Gene Ontology Provided by EcoCyc

Function Evidence Code Pubs
enables protein binding IPI
Inferred from Physical Interaction
more info
 PubMed 
enables signal sequence binding IEA
Inferred from Electronic Annotation
more info
  
enables signal sequence binding IPI
Inferred from Physical Interaction
more info
 PubMed 
Process Evidence Code Pubs
involved_in negative regulation of protein transport IBA
Inferred from Biological aspect of Ancestor
more info
  
acts_upstream_of_or_within negative regulation of protein transport IDA
Inferred from Direct Assay
more info
 PubMed 
involved_in negative regulation of protein transport IEA
Inferred from Electronic Annotation
more info
  
Component Evidence Code Pubs
is_active_in cytoplasm IBA
Inferred from Biological aspect of Ancestor
more info
  
located_in cytoplasm IDA
Inferred from Direct Assay
more info
 PubMed 
located_in cytoplasm IEA
Inferred from Electronic Annotation
more info
  
Preferred Names
NapA signal peptide-binding chaperone NapD

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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
    2302750..2303013 complement
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. NP_416711.1 NapA signal peptide-binding chaperone NapD [Escherichia coli str. K-12 substr. MG1655]

    See identical proteins and their annotated locations for NP_416711.1

    Status: PROVISIONAL

    UniProtKB/TrEMBL
    A0A828PCB3
    Conserved Domains (1) summary
    PRK10553
    Location:1 → 87
    PRK10553; chaperone NapD
Nucleotide Protein
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