secM SecA translation regulator [Escherichia coli str. K-12 substr. MG1655] - Gene

Summary

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Official Symbol: secM
Official Full Name: SecA translation regulator
Primary source: ECOCYC:EG11087
Locus tag: b0097
See related: ASAP:ABE-0000340
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: ECK0098; srrA; yacA
Summary: Translation and secretion of SecM regulates downstream secA gene expression. [More information is available at EcoGene: EG11087]. SecM regulates production of co-translated SecA; reduced secretion of SecM acts as a "sensor" that stimulates translation of the SecA translocation factor via a translational pause at Pro166 that is caused by an arrest sequence that interacts with the ribosomal exit tunnel . [More information is available at EcoCyc: EG11087].
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Genomic context

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Sequence:: NC_000913.3 (107705..108217)

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?

the folded nascent SecM chain that emerges from the ribosome exit tunnel interacts with the outer surface of the ribosome to stabilize translation arrest.
Title: Nascent SecM chain interacts with outer ribosomal surface to stabilize translation arrest.
SecM can regulate its own synthesis by the force generated during folding, tuning ribosome activity to structure acquisition by a nascent polypeptide
Title: Ribosome. Mechanical force releases nascent chain-mediated ribosome arrest in vitro and in vivo.
Residues at positions between 161 and 166 of SecM showed decreased ribosome stalling.
Title: Identification of a hyperactive variant of the SecM motif involved in ribosomal arrest.
The authors found that signal peptide mutations that alter targeting kinetics and insertions or deletions that change the distance between the SecM signal peptide and the arrest motif perturb the regulation of SecA synthesis.
Title: The translational regulatory function of SecM requires the precise timing of membrane targeting.
results suggest that cotranslational targeting of nascent SecM to the translocon plays previously unrecognized roles of facilitating the formation of functional SecA molecules
Title: SecM facilitates translocase function of SecA by localizing its biosynthesis.
secM-encoded Pro166-tRNA functions as a nonpolypeptide element in fulfilling SecM's role as a secretion monitor.
Title: Genetically encoded but nonpolypeptide prolyl-tRNA functions in the A site for SecM-mediated ribosomal stall.
compared atomic models fitted by real-space refinement into cryo-electron microscopy reconstructions of a pretranslocational and SecM-stalled ribosome complex
Title: Elongation arrest by SecM via a cascade of ribosomal RNA rearrangements.
RNA SsrA tagging of secretory monitor SecM would rescue ribosomes to avoid excessive jamming of the translation apparatus on stop-less secM mRNA
Title: SsrA tagging of Escherichia coli SecM at its translation arrest sequence.

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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 translation regulator activity	IDA Inferred from Direct Assay more info	PubMed
enables translation regulator activity	IEA Inferred from Electronic Annotation more info

Process	Evidence Code	Pubs
involved_in regulation of translation	IDA Inferred from Direct Assay more info	PubMed

Component	Evidence Code	Pubs
located_in cytoplasm	IEA Inferred from Electronic Annotation more info
is_active_in cytosol	IDA Inferred from Direct Assay more info	PubMed
located_in cytosol	IEA Inferred from Electronic Annotation more info
located_in periplasmic space	IEA Inferred from Electronic Annotation more info