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Literature summary for 3.4.21.105 extracted from

  • Stevenson, L.G.; Strisovsky, K.; Clemmer, K.M.; Bhatt, S.; Freeman, M.; Rather, P.N.
    Rhomboid protease AarA mediates quorum-sensing in Providencia stuartii by activating TatA of the twin-arginine translocase (2007), Proc. Natl. Acad. Sci. USA, 104, 1003-1008.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.4.21.105

Cloned(Commentary)

Cloned (Comment) Organism
gene aarA, DNA and amino acid sequence determination and analysis, expression of the C-terminally His-tagged AarA in Escherichia coli, expression of the tat operon is not dependent on aarA Providencia stuartii

Protein Variants

Protein Variants Comment Organism
additional information construction of aarA knockout mutants, AarA mutants are defective in Tat function and rescued by tatA in multicopy, TatA protein missing the first 7 amino acids restores the aarA-dependent phenotypes, the Tat system is responsible for the various phenotypes exhibited by an aarA mutant, e.g. in extracellular signal production, overview Providencia stuartii
S150A site-directed mutagenesis, catalytic residue mutation, inactive mutant Providencia stuartii

Localization

Localization Comment Organism GeneOntology No. Textmining
membrane
-
 Providencia stuartii 16020
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
Gurken-derived peptide + H2O Providencia stuartii
-
 ?
-
 ?
Gurken-derived peptide + H2O Providencia stuartii XD37
-
 ?
-
 ?
TatA + H2O Providencia stuartii rhomboid protease AarA mediates quorum-sensing by activating TatA of the twin-arginine translocase, TatA is a component of the twin-arginine translocase, Tat, protein secretion pathway and likely forms a secretion pore, TatA in Providencia stuartii has a short N-terminal extension, which is proteolytically removed by AarA, overview processed TatA + N-terminal extension peptide
-
 ?
TatA + H2O Providencia stuartii XD37 rhomboid protease AarA mediates quorum-sensing by activating TatA of the twin-arginine translocase, TatA is a component of the twin-arginine translocase, Tat, protein secretion pathway and likely forms a secretion pore, TatA in Providencia stuartii has a short N-terminal extension, which is proteolytically removed by AarA, overview processed TatA + N-terminal extension peptide
-
 ?

Organism

Organism UniProt Comment Textmining
Providencia stuartii
-
-
-
Providencia stuartii XD37
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant C-terminally His-tagged AarA from Escherichia coli by nickel affinity chromatography to homogeneity Providencia stuartii

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
Gurken-derived peptide + H2O
-
 Providencia stuartii ?
-
 ?
Gurken-derived peptide + H2O
-
 Providencia stuartii XD37 ?
-
 ?
TatA + H2O
-
 Providencia stuartii processed TatA + N-terminal extension peptide
-
 ?
TatA + H2O rhomboid protease AarA mediates quorum-sensing by activating TatA of the twin-arginine translocase, TatA is a component of the twin-arginine translocase, Tat, protein secretion pathway and likely forms a secretion pore, TatA in Providencia stuartii has a short N-terminal extension, which is proteolytically removed by AarA, overview Providencia stuartii processed TatA + N-terminal extension peptide
-
 ?
TatA + H2O
-
 Providencia stuartii XD37 processed TatA + N-terminal extension peptide
-
 ?
TatA + H2O rhomboid protease AarA mediates quorum-sensing by activating TatA of the twin-arginine translocase, TatA is a component of the twin-arginine translocase, Tat, protein secretion pathway and likely forms a secretion pore, TatA in Providencia stuartii has a short N-terminal extension, which is proteolytically removed by AarA, overview Providencia stuartii XD37 processed TatA + N-terminal extension peptide
-
 ?

Synonyms

Synonyms Comment Organism
AarA
-
 Providencia stuartii
More AarA is a member of the rhomboid family of intramembrane serine proteases Providencia stuartii