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

Summary

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Official Symbol: alaS
Official Full Name: alanine--tRNA ligase/DNA-binding transcriptional repressor
Primary source: ECOCYC:EG10034
Locus tag: b2697
See related: ASAP:ABE-0008869
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_000913.3 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Go to reference sequence details

Genomic Sequence:: NC_000913.3

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

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.
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.
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.
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.
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.

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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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Homology

Orthologs from OrthoDB

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 peptide lactyltransferase (ATP-dependent) activity	IDA Inferred from Direct Assay more info	PubMed
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 more info	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 more info	PubMed

General protein information

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Preferred Names: alanine--tRNA ligase/DNA-binding transcriptional repressor

NP_417177.1

EC 6.1.1.7

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

NC_000913.3 Reference assembly

Range

2819381..2822011 complement

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GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

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

A0A1V2GGL5

Conserved Domains (1) summary

PRK00252
Location:2 → 875

alaS; alanyl-tRNA synthetase; Reviewed