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SYSTEMATIC NAME
IUBMB Comments
ATP phosphohydrolase (sulfate-importing)
ABC-type (ATP-binding cassette-type) ATPase, characterized by the presence of two similar ATP-binding domains. Does not undergo phosphorylation during the transport process. A bacterial enzyme that imports sulfate and thiosulfate anions.
facilitation of bacterial sulfate uptake by Rv1739c requires CysA and its associated sulfate permease activity, thus Rv1739c may be a CysTWA-dependent sulfate transporter
facilitation of bacterial sulfate uptake by Rv1739c requires CysA and its associated sulfate permease activity, thus Rv1739c may be a CysTWA-dependent sulfate transporter
thiosulfate can be transported by two permease systems. One of theses systems is the sulfate permease, while the other does not required cysT and cysW gene products but uses other integral membrane components
facilitation of bacterial sulfate uptake by Rv1739c requires CysA and its associated sulfate permease activity, thus Rv1739c may be a CysTWA-dependent sulfate transporter
facilitation of bacterial sulfate uptake by Rv1739c requires CysA and its associated sulfate permease activity, thus Rv1739c may be a CysTWA-dependent sulfate transporter
facilitation of bacterial sulfate uptake by Rv1739c requires CysA and its associated sulfate permease activity, thus Rv1739c may be a CysTWA-dependent sulfate transporter
facilitation of bacterial sulfate uptake by Rv1739c requires CysA and its associated sulfate permease activity, thus Rv1739c may be a CysTWA-dependent sulfate transporter
the ABC-transoprter consists of both the membrane components - the products of the genes cysT, cysW and cysA and the periplasmic binders - the products of the genes cysP and sbp
cysA encodes the membrane-associated ATP-binding protein, sbpA encodes the sulfate-binding protein, cysT and cysW encode proteins that may form a channel for the transport of sulfate across the cytoplasmic membrane, cysT encodes a polypeptide that has some homology to a family of prokaryotic regulatory proteins
inducible expression of Rv1739c in an Escherichia coli strain EWP44 lacking CysA does not increase sulfate uptake by intact cells. Expression of Rv1739c in a Mycobacterium bovis BCG strain lacking the ABC sulfate permease subunit CysA cannot complement sulfate auxotrophy. Induction of Rv1739c expression in Escherichia coli increases bacterial uptake of sulfate, but not Cl-, formate, or oxalate. Sulfate uptake is also increased by overexpression of the Rv1739c transmembrane domain, but not of the cytoplasmic C-terminal STAS domain
mutation in the periplasmic sulfate receptor, dissociation of sulfate from the mutant enzyme is very slow under oxidizing conditions and increases more than 200-fold when reducing agent is added. This effect is attributed to a loss of interdomain structural flexibility in the presence of the disulfide
Engineered interdomain disulfide in the perplasmic receptor for sulfate transport reduces flexibility. Site-directed mutagenesis and ligand-binding studies