TreeGrafter-generated GO annotations
Combined Automated Annotation using Multiple IEA Methods
UniProtKB record A0A0H2M727 (A0A0H2M727_VARPD) - Taurine-binding periplasmic protein from Variovorax paradoxus TBEA6
-
VPARA_03650 (tauA, A0A0H2M727) is a 340-aa periplasmic taurine-binding protein (NCBIfam TIGR01729, InterPro IPR010068, PANTHER PTHR30024:SF47) with an N-terminal signal peptide at residues 1-30.
"DR NCBIfam; TIGR01729; taurine_ABC_bnd; 1."
-
VPARA_03650 (tauA) corresponds to EMBL CDS accession KLN58254.1 on genomic contig JZWI01000003, where consecutive CDS accessions (KLN58254.1-KLN58256.1) and locus tags stepping by 10 place tauA immediately upstream of tauB1 (VPARA_03660, KLN58255.1) and tauC (VPARA_03670, KLN58256.1).
"DR EMBL; JZWI01000003; KLN58254.1; -; Genomic_DNA."
Identification of sulfate starvation-regulated genes in Escherichia coli: a gene cluster involved in the utilization of taurine as a sulfur source.
-
Characterization of the E. coli tauABCD cluster showed that TauA carries a periplasmic signal peptide and functions with TauB and TauC as the taurine ABC uptake system supplying TauD.
"The TauA protein contained a putative signal peptide for transport into the periplasm; the TauB and TauC proteins showed sequence similarity to ATP-binding proteins and membrane proteins, respectively, of ABC-type transport systems"
Deletion analysis of the Escherichia coli taurine and alkanesulfonate transport systems.
-
In-frame deletion and complementation of E. coli tauABC and ssuABC showed that the two ABC importers are complementary and their subunits are not functionally exchangeable.
"Mutants in which only formation of hybrid transporters was possible were unable to grow with sulfonates, indicating that the individual components of the two transport systems were not functionally exchangeable."
Functional characteristics of TauA binding protein from TauABC Escherichia coli system.
-
Purified E. coli TauA binds taurine with high affinity (mean Kd = 11.3 nM) and specificity at a single ligand-binding site.
"Measurement of K (d) value (mean 11.3 nM) by binding/dialysis studies revealed high affinity and specificity with taurine and also indicated that TauA possessed a unique binding site for its ligand."