Protein Domain : Molybdate ABC transporter, substrate-binding protein IPR005950

Type	Family
Description	This entry represents the molybdate ABC transporter periplasmic binding protein from bacteria and archaea. It has been shown experimentally by radioactive labeling that ModA is a hydrophylioc periplasmic-binding protein in Gram-negative organisms [ , ] and its counterpart in Gram-positive organisms is a lipoprotein. The other components of the system include ModB, an integral membrane protein and ModC, the ATP-binding subunit. Almost all of them display a common beta/alpha folding motif and have similar tertiary structures consisting of two globular domains.Bacterial high affinity transport systems are involved in active transport of solutes across the cytoplasmic membrane. Most of the bacterial ABC (ATP-binding cassette) importers are composed of one or two transmembrane permease proteins, one or two nucleotide-binding proteins and a highly specific periplasmic solute-binding protein. In Gram-negative bacteria the solute-binding proteins are dissolved in the periplasm, while in archaea and Gram-positive bacteria, their solute-binding proteins are membrane-anchored lipoproteins [ , ].
Short Name	ModA