Cloning and nucleotide sequence of braC, the structural gene for the leucine-, isoleucine-, and valine-binding protein of Pseudomonas aeruginosa PAO.
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The braC plasmid restores LIV-I transport activity in the braC310 mutant.
"The plasmid carrying the LIVAT-BP gene restored the activity of the high-affinity branched-chain amino acid transport system (the leucine, isoleucine, valine [LIV-I] transport system) in the braC310 mutant of P. aeruginosa"
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Mature BraC lacks a cleaved 26-residue signal peptide and was purified from shock fluid.
"Determination of the N-terminal amino acid sequence of the LIVAT-BP purified from P. aeruginosa shock fluid suggested that the N-terminal 26 residues of the gene product are cleaved off posttranslationally"
High-throughput phenotypic characterization of Pseudomonas aeruginosa membrane transport genes.
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Each bra mutant is defective in alanine utilization; some also in valine and isoleucine utilization.
"In this work, mutants for each of these genes were found to be defective in Alanine metabolism, while utilization of L-Valine and L-Isoleucine was also altered in some cases"
Determination of Ligand Profiles for Pseudomonas aeruginosa Solute Binding Proteins.
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BraC binds the five LIVAT ligands with nanomolar affinity but not L-Met or D-Ala.
"ITC experiments revealed binding with nanomolar affinities for the five ligands identified in the study by Hoshino et al. [58] (Figure 6A), whereas no binding was detected for l-Met and d-Ala."
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BraC also binds L-homoserine with high affinity.
"However, PA1074 is not specific for proteinogenic amino acids since l-homoserine also bound with high affinity (Table 1)."
UniProt entry P21175
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BraC is a component of the LIV-I transport system.
"Component of the high-affinity leucine, isoleucine, valine transport system I (LIV-I)"
Gene Ontology annotation through association of InterPro records with GO terms
Annotation inferences using phylogenetic trees
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt.