Cloned (Comment) | Organism |
---|---|
gene cusS, recombinant expression of the enzyme's periplasmic domain from pTXB3CusSs plasmid, encoding CusS amino acids 39-187 with a chitin binding domain (CBD) affinity tag, in Escherichia coli strain BL21(DE3) | Escherichia coli |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
membrane | a periplasmic sensor domain is flanked by transmembrane alpha-helices which link it to conserved cytoplasmic catalytic domains | Escherichia coli | 16020 | - |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Ag+ | the periplasmic sensor domain of CusS directly interacts with Ag(I) ions and undergoes a conformational change upon metal binding. Metal binding also enhances the tendency of the domain to dimerize. No molecules of Ag+ per enzyme molecule for the purified enzyme, and 3.82 molecules of Ag+ per enzyme molecule after dialysis against Ag+, Ni2+, Zn2+, and Cu+ ions | Escherichia coli | |
Cu+ | 0.14 molecules of Cu+ per enzyme molecule for the purified enzyme, and 0.23 molecules of Cu+ per enzyme molecule after dialysis against Ag+, Ni2+, Zn2+, and Cu+ ions | Escherichia coli | |
additional information | the enzyme does not bind Ni2+ or Zn2+ | Escherichia coli |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
additional information | - |
CusSs samples for analytical ultracentrifugation experiments are prepared by dialysis against 5fold molar excesses of AgNO3, ZnCl2 or NiCl2 | Escherichia coli |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | P77485 | W3110 | - |
Purification (Comment) | Organism |
---|---|
recombinant CBD-tagged enzyme from Escherichia coli strain BL21(DE3) by chitin affinity chromatography with DTT thiol-induced cleavage and gel filtration to over 95% purity | Escherichia coli |
Subunits | Comment | Organism |
---|---|---|
dimer | periplasmic sensor domain of CusS directly interacts with Ag(I) ions and undergoes a conformational change upon metal binding. Metal binding also enhances the tendency of the domain to dimerize | Escherichia coli |
More | CusS is predicted to be a canonical histidine kinase with a periplasmic sensor domain connected by transmembrane helices to the catalytic cytoplasmic domains | Escherichia coli |
Synonyms | Comment | Organism |
---|---|---|
CusS | - |
Escherichia coli |
General Information | Comment | Organism |
---|---|---|
evolution | the CusS histidine kinase has overall sequence identity to putative metal-sensing HKs such as SilS (56%), CopS (42%), PcoS (38%) and CinS (35%) | Escherichia coli |
additional information | the periplasmic sensor domain of CusS directly interacts with Ag(I) ions and undergoes a conformational change upon metal binding. Metal binding also enhances the tendency of the domain to dimerize. For NMR structure analysis, the enzyme is prepared with Ag+, Ni2+, Zn2+, and Cu+ ions via dialysis | Escherichia coli |
physiological function | CusS is a prototypical periplasmic sensing histidine kinase, the histidine kinase CusS of the CusRS two-component system functions as a Ag(I)/Cu(I)-responsive sensor kinase and is essential for induction of the genes encoding the CusCFBA efflux pump. CusS has an important role in silver resistance and regulation of copper homeostasis | Escherichia coli |