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glnA glutamine synthetase [ Bacillus subtilis subsp. subtilis str. 168 ]

Gene ID: 940020, updated on 6-Oct-2023

Summary

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Gene symbol
glnA
Gene description
glutamine synthetase
Locus tag
BSU_17460
Gene type
protein coding
RefSeq status
PROVISIONAL
Organism
Bacillus subtilis subsp. subtilis str. 168 (strain: 168, sub-species: subtilis, type-material: type strain of Bacillus subtilis)
Lineage
Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus
Old locus tag
BSU17460
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Genomic context

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Sequence:
NC_000964.3 (1878425..1879759)

NC_000964.3Genomic Context describing neighboring genes Neighboring gene putative C-S lyase Neighboring gene transcriptional regulator (nitrogen metabolism) Neighboring gene putative phage protein; defective, phage region Neighboring gene putative phage protein; defective phage region

Genomic regions, transcripts, and products

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Genomic Sequence:
NC_000964.3

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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Related articles in PubMed

  1. Functional roles of the conserved Glu304 loop of Bacillus subtilis glutamine synthetase. Wray LV Jr, et al. J Bacteriol, 2010 Oct. PMID 20656908, Free PMC Article
  2. Novel trans-Acting Bacillus subtilis glnA mutations that derepress glnRA expression. Fisher SH, et al. J Bacteriol, 2009 Apr. PMID 19233925, Free PMC Article
  3. The Molecular Basis of TnrA Control by Glutamine Synthetase in Bacillus subtilis. Hauf K, et al. J Biol Chem, 2016 Feb 12. PMID 26635369, Free PMC Article
  4. Transcription factor TnrA inhibits the biosynthetic activity of glutamine synthetase in Bacillus subtilis. Fedorova K, et al. FEBS Lett, 2013 May 2. PMID 23535029
  5. Bacillus subtilis GlnR contains an autoinhibitory C-terminal domain required for the interaction with glutamine synthetase. Wray LV Jr, et al. Mol Microbiol, 2008 Apr. PMID 18331450

See all (9) citations in PubMed

GeneRIFs: Gene References Into Functions

What's a GeneRIF?
  1. Data suggest GS (glutamine synthetase) controls TnrA activity at positively controlled promoters by stabilizing TnrA in DNA-bound state; ATP and glutamine bind to GS in competitive manner; AMP competes with ATP and favors GS--TnrA interaction.
    Title: The Molecular Basis of TnrA Control by Glutamine Synthetase in Bacillus subtilis.
  2. TnrA inhibits the biosynthetic activity of glutamine synthetase
    Title: Transcription factor TnrA inhibits the biosynthetic activity of glutamine synthetase in Bacillus subtilis.
  3. The residues in the highly conserved Glu304 flap appear to be optimized for glutamate binding because mutant enzymes with substitutions in five of the flap residues had increased glutamate Km values compared to that for wild-type GS.
    Title: Functional roles of the conserved Glu304 loop of Bacillus subtilis glutamine synthetase.
  4. These results are consistent with a model where feedback-inhibited GS is the only cellular factor involved in regulating the activity of GlnR in B. subtilis.
    Title: Novel trans-Acting Bacillus subtilis glnA mutations that derepress glnRA expression.
  5. The GlnR C-terminal domain is also required for the interaction between GlnR and feedback-inhibited glutamine synthetase.
    Title: Bacillus subtilis GlnR contains an autoinhibitory C-terminal domain required for the interaction with glutamine synthetase.
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Pathways from PubChem

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General gene information

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Homology

General protein information

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Preferred Names
glutamine synthetase
NP_389628.1
  • Evidence 1a: Function from experimental evidences in the studied strain; PubMedId: 13737, 11719184, 12142436, 16055443, 16885465, 19233925, 19251843; Product type e: enzyme

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_000964.3 Reference assembly

    Range
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. NP_389628.1 glutamine synthetase [Bacillus subtilis subsp. subtilis str. 168]

    See identical proteins and their annotated locations for NP_389628.1

    Status: PROVISIONAL

    UniProtKB/TrEMBL
    A0A5B7LKW5
    Conserved Domains (1) summary
    TIGR00653
    Location:7 → 442
    GlnA; glutamine synthetase, type I
Nucleotide Protein
Heading Accession and Version
Protein Accession Links
GenPept Link UniProtKB Link
P12425.3

Gene LinkOut

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Other Literature Sources
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Research Materials