A0A6S6M2D3 · A0A6S6M2D3_9BACT

  • Protein
    Energy-dependent translational throttle protein EttA
  • Gene
    ettA
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    3/5

Function

function

A translation factor that gates the progression of the 70S ribosomal initiation complex (IC, containing tRNA(fMet) in the P-site) into the translation elongation cycle by using a mechanism sensitive to the ATP/ADP ratio. Binds to the 70S ribosome E-site where it modulates the state of the translating ribosome during subunit translocation. ATP hydrolysis probably frees it from the ribosome, which can enter the elongation phase.

Caution

Lacks conserved residue(s) required for the propagation of feature annotation.

Catalytic activity

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site361-368ATP 2 (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytoplasm
Molecular FunctionATP binding
Molecular FunctionATP hydrolysis activity
Molecular Functionribosome binding
Molecular FunctionrRNA binding
Molecular FunctiontRNA binding
Biological Processnegative regulation of translational elongation
Biological Processtranslation

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Energy-dependent translational throttle protein EttA
  • EC number
  • Alternative names
    • Translational regulatory factor EttA

Gene names

    • Name
      ettA
    • ORF names
      GEOBRER4_n3443

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • R4
  • Taxonomic lineage
    Bacteria > Thermodesulfobacteriota > Desulfuromonadia > Geobacterales > Geobacteraceae > Citrifermentans

Accessions

  • Primary accession
    A0A6S6M2D3

Proteomes

Subcellular Location

Cytoplasm
Note: Associates with ribosomes and polysomes.

Keywords

Interaction

Subunit

Monomer. Probably contacts ribosomal proteins L1, L5, L33 and S7, the 16S and 23S rRNA and the P-site containing tRNA(fMet).

Family & Domains

Features

Showing features for domain, region.

TypeIDPosition(s)Description
Domain10-264ABC transporter
Region247-327PtIM
Domain329-555ABC transporter

Domain

The P-site tRNA interaction motif (PtIM domain) probably interacts with the P-site tRNA(fMet) as well as the 23S rRNA.
The arm domain is inserted in the first ABC transporter domain. Probably contacts ribosomal protein L1.

Sequence similarities

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    561
  • Mass (Da)
    63,164
  • Last updated
    2020-12-02 v1
  • Checksum
    3454E9762E3EBB83
MALDPNKVIYSMIGVSKFYDKKPVLKDIYLSYFYGAKIGVLGLNGSGKSSLLKILAGVDKEFNGKTILSPGYTVGYLAQEPQLDPNKTVRQCVEEGVQEIVDLMNEFNEINMKFGEEMSDADMEKLCDRQAKVQEKLDHFDAWDLDSRLELAMDALRCPPPETNVANLSGGEKRRVALCRLLLQKPDILLLDEPTNHLDAESVAWLEQHLQRYAGTIIAVTHDRYFLDNVAGWILELDRGQGIPWQGNYSSWLEQKEKRLAQEEKTESERQKTLKRELEWIRMSPKGRHAKGKARINSYEDLLNTESEKRGRDLEIYIPPGPRLGGVVVEAENVAKGYGDKLLVEGMEFRLPPGGIVGVIGPNGAGKTTLFRMITGEEKPDSGTFKIGETVKLAYVDQSRDALDPEQTIWEAISGGQEQLQLGKQLVNSRAYVARFNFSGADQQKKLGMLSGGERNRVHLAKMLKEGGNVILLDEPTNDLDVNTMRALEEALENFAGCAVVISHDRWFLDRIATHILAFEGDSKVVWFEGNYSEYEEDRHARLGTAADQPHRIMYRQLTRV

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AP023213
EMBL· GenBank· DDBJ
BCG48547.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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