v5.1.0.3
Cicer data from the Legume Information System
| Type | Family |
| Description | The ATP-binding cassette (ABC) type nickel transport system is comprised of five subunits NikABCDE: the two pore-forming integral inner membrane proteins NikB and NikC; the two inner membrane-associated proteins with ATPase activity NikD and NikE; and the periplasmic nickel binding NikA, the initial nickel receptor [ , ]. This entry represents NikA, which contains a pocket rich in aromatic and arginine residues that lodged a Ni-(H2O)5 2+ species. It has been shown that NikA is able to bind nickel and Fe(III)EDTA in the same pocket [ ] and that His416 is the only direct metal-protein contact []. This entry also includes metal-staphylopine-binding protein CntA from Staphylococcus aureus [, ]. CntA is involved in the import of divalent metals ions such as nickel, cobalt and zinc. It binds the metal via the metallophore StP, and transfers the StP-metal complex to the membrane-bound permease [, ].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 | NikA_ABC_Ni-bd |