P15373 · PRLF_ECOLI

Function

function

Antitoxin component of a type II toxin-antitoxin (TA) system. Labile antitoxin that binds to the YhaV toxin and neutralizes its ribonuclease activity. Also acts as a transcription factor. The YhaV/PrlF complex binds the prlF-yhaV operon, probably negatively regulating its expression.
Negatively regulates its own expression as well as relieving the export block imposed by high-level synthesis of the LamB-LacZ hybrid protein. Overexpression leads to increased doubling time and also suppresses a htrA (degP) null phenotype.

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentcytoplasm
Cellular Componenttoxin-antitoxin complex
Molecular FunctionDNA binding
Molecular FunctionDNA-binding transcription factor activity
Molecular Functionenzyme binding
Molecular Functionidentical protein binding
Molecular Functiontoxin sequestering activity
Biological Processnegative regulation of DNA-templated transcription
Biological Processregulation of cell growth
Biological Processregulation of DNA-templated transcription
Biological Processregulation of growth
Biological Processsingle-species biofilm formation

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Antitoxin PrlF
  • Alternative names
    • HtrA suppressor protein SohA

Gene names

    • Name
      prlF
    • Synonyms
      sohA
    • Ordered locus names
      b3129, JW3098

Organism names

  • Taxonomic identifier
  • Strains
    • K12
    • K12 / MG1655 / ATCC 47076
    • K12 / W3110 / ATCC 27325 / DSM 5911
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Enterobacteriaceae > Escherichia

Accessions

  • Primary accession
    P15373
  • Secondary accessions
    • Q2M980

Proteomes

Subcellular Location

Keywords

Phenotypes & Variants

Disruption phenotype

Not essential.

Features

Showing features for mutagenesis.

TypeIDPosition(s)Description
Mutagenesis91-111In prlF1; suppresses overproduction lethality of lamB-lacZ gene fusions, leads to decreased beta-galactosidase activity. Partially alleviates YhaV toxic activity.

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00000720331-111Antitoxin PrlF

Proteomic databases

Interaction

Subunit

Homodimer; forms a complex with YhaV with stoichiometry PrlF2-YhaV4, possibly as a YhaV2-PrlF2-YhaV2 complex like the MazFE complex. This complex is seen to dimerize in solution.
View interactors in UniProtKB
View CPX-4102 in Complex Portal

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain12-59SpoVT-AbrB

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    111
  • Mass (Da)
    12,359
  • Last updated
    1990-04-01 v1
  • Checksum
    5FC0D5FF43F75D8A
MPANARSHAVLTTESKVTIRGQTTIPAPVREALKLKPGQDSIHYEILPGGQVFMCRLGDEQEDHTMNAFLRFLDADIQNNPQKTRPFNIQQGKKLVAGMDVNIDDEIGDDE

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
M30178
EMBL· GenBank· DDBJ
AAA24638.1
EMBL· GenBank· DDBJ
Genomic DNA
M32358
EMBL· GenBank· DDBJ
AAA24418.1
EMBL· GenBank· DDBJ
Genomic DNA
U18997
EMBL· GenBank· DDBJ
AAA57932.1
EMBL· GenBank· DDBJ
Genomic DNA
U00096
EMBL· GenBank· DDBJ
AAC76163.1
EMBL· GenBank· DDBJ
Genomic DNA
AP009048
EMBL· GenBank· DDBJ
BAE77176.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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