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alaS alanine--tRNA ligase/DNA-binding transcriptional repressor [ Escherichia coli str. K-12 substr. MG1655 ]

Gene ID: 947175, updated on 2-May-2024

Summary

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Gene symbol
alaS
Gene description
alanine--tRNA ligase/DNA-binding transcriptional repressor
Primary source
ASAP:ABE-0008869
Locus tag
b2697
See related
ECOCYC:EG10034
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
act; ala-act; ECK2692; lovB
Summary
Alanyl-tRNA synthetase (AlaRS) is a member of the family of aminoacyl-tRNA synthetases, which interpret the genetic code by covalently linking amino acids to their specific tRNA molecules. [More information is available at EcoCyc: EG10034].
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Genomic context

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Sequence:
NC_000913.3 (2819381..2822011, complement)

NC_000913.3Genomic Context describing neighboring genes Neighboring gene tRNA-Ser Neighboring gene carbon storage regulator Neighboring gene RecA inhibitor RecX Neighboring gene DNA recombination/repair protein RecA

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. Allosteric interaction of nucleotides and tRNA(ala) with E. coli alanyl-tRNA synthetase. Dignam JD, et al. Biochemistry, 2011 Nov 15. PMID 21985608
  2. The C-Ala domain brings together editing and aminoacylation functions on one tRNA. Guo M, et al. Science, 2009 Aug 7. PMID 19661429, Free PMC Article
  3. Small molecules: big players in the evolution of protein synthesis. Ataide SF, et al. ACS Chem Biol, 2006 Jun 20. PMID 17163757
  4. Distinct kinetic mechanisms of the two classes of Aminoacyl-tRNA synthetases. Zhang CM, et al. J Mol Biol, 2006 Aug 11. PMID 16843487
  5. Structure-specific tRNA determinants for editing a mischarged amino acid. Beebe K, et al. J Biol Chem, 2003 Nov 14. PMID 12949076

See all (86) citations in PubMed

GeneRIFs: Gene References Into Functions

What's a GeneRIF?
  1. Here, the authors show that DTD's active site architecture can efficiently edit mischarged Gly-tRNA(Ala) species four orders of magnitude more efficiently than even AlaRS, the only ubiquitous cellular checkpoint known for clearing the error.
    Title: Role of D-aminoacyl-tRNA deacylase beyond chiral proofreading as a cellular defense against glycine mischarging by AlaRS.
  2. ATP binding to full length enzyme (ARS875) and to an N-terminal construct (ARS461) is endothermic (DeltaH = 3-4 kcal mol(-1)) with stoichiometries of 1:1 for ARS461 and 2:1 for full-length dimer.
    Title: Allosteric interaction of nucleotides and tRNA(ala) with E. coli alanyl-tRNA synthetase.
  3. findings show that the C-Ala domain plays a key role in alanyl-tRNA synthetases (AlaRS) function; C-Ala forms an ancient single-stranded nucleic acid binding motif that promotes cooperative binding of both aminoacylation and editing domains to tRNA(Ala)
    Title: The C-Ala domain brings together editing and aminoacylation functions on one tRNA.
  4. the editing site of alanyl-tRNA synthetase targets mischarged tRNA(Ala) using a structural motif unrelated to that for aminoacylation, so that, remarkably, two motifs in the same enzyme independently provide determinants for tRNA(Ala) recognition
    Title: Distinct domains of tRNA synthetase recognize the same base pair.
  5. N-terminus verified by Edman degradation on mature peptide
    Title: Mass spectra of partial protein hydrolysates as a multiple phase check for long polypeptides deduced from DNA sequences: NH2-terminal segment of alanine tRNA synthetase.
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 ATP binding IEA
Inferred from Electronic Annotation
more info
  
enables DNA-binding transcription repressor activity IDA
Inferred from Direct Assay
more info
 PubMed 
enables Ser-tRNA(Ala) hydrolase activity IDA
Inferred from Direct Assay
more info
 PubMed 
enables alanine-tRNA ligase activity IBA
Inferred from Biological aspect of Ancestor
more info
  
enables alanine-tRNA ligase activity IDA
Inferred from Direct Assay
more info
 PubMed 
enables alanine-tRNA ligase activity IEA
Inferred from Electronic Annotation
more info
  
enables aminoacyl-tRNA editing activity IBA
Inferred from Biological aspect of Ancestor
more info
  
enables aminoacyl-tRNA editing activity IDA
Inferred from Direct Assay
more info
 PubMed 
enables aminoacyl-tRNA editing activity IMP
Inferred from Mutant Phenotype
more info
 PubMed 
enables aminoacyl-tRNA ligase 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 nucleic acid binding IEA
Inferred from Electronic Annotation
more info
  
enables protein homodimerization activity IDA
Inferred from Direct Assay
more info
 PubMed 
enables tRNA binding IEA
Inferred from Electronic Annotation
more info
  
enables zinc ion binding IDA
Inferred from Direct Assay
more info
 PubMed 
enables zinc ion binding IEA
Inferred from Electronic Annotation
more info
  
Process Evidence Code Pubs
involved_in alanyl-tRNA aminoacylation IBA
Inferred from Biological aspect of Ancestor
more info
  
acts_upstream_of_or_within alanyl-tRNA aminoacylation IDA
Inferred from Direct Assay
more info
 PubMed 
involved_in alanyl-tRNA aminoacylation IEA
Inferred from Electronic Annotation
more info
  
involved_in aminoacyl-tRNA metabolism involved in translational fidelity IEA
Inferred from Electronic Annotation
more info
  
involved_in negative regulation of DNA-templated transcription IBA
Inferred from Biological aspect of Ancestor
more info
  
acts_upstream_of_or_within negative regulation of DNA-templated transcription IDA
Inferred from Direct Assay
more info
 PubMed 
involved_in translation IEA
Inferred from Electronic Annotation
more info
  
Component Evidence Code Pubs
located_in cytoplasm IEA
Inferred from Electronic Annotation
more info
  
located_in cytosol HDA PubMed 
is_active_in cytosol IBA
Inferred from Biological aspect of Ancestor
more info
  
located_in cytosol IDA
Inferred from Direct Assay
more info
 PubMed 
located_in membrane HDA PubMed 

General protein information

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Preferred Names
alanine--tRNA ligase/DNA-binding transcriptional repressor
NP_417177.1

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
    2819381..2822011 complement
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. NP_417177.1 alanine--tRNA ligase/DNA-binding transcriptional repressor [Escherichia coli str. K-12 substr. MG1655]

    See identical proteins and their annotated locations for NP_417177.1

    Status: PROVISIONAL

    UniProtKB/TrEMBL
    A0AA88ERG5
    Conserved Domains (1) summary
    PRK00252
    Location:2 → 875
    alaS; alanyl-tRNA synthetase; Reviewed
Nucleotide Protein
Heading Accession and Version

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