PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 7957084-3 1994 Among such suppressors, arcB and barA are of particular interest because these gene products are unique in the sense that they contain both an autophosphorylated histidine site (or transmitter module) and a phospho-accepting aspartate site (or receiver module) in their primary amino acid sequences. Histidine 162-171 hypothetical protein Escherichia coli 24-28 7957084-4 1994 Here we report that ArcB and BarA possess in the C-terminal region a phosphorylated histidine site which has never been noticed, in addition to the authentic one identified previously. Histidine 84-93 hypothetical protein Escherichia coli 20-24 7957084-5 1994 This newly identified histidine in ArcB and BarA was demonstrated to play a crucial role in the observed multicopy suppression. Histidine 22-31 hypothetical protein Escherichia coli 35-39 7957084-6 1994 Furthermore, it was demonstrated in vivo and in vitro for ArcB that the C-terminal domain containing the histidine can function as an alternative phosphodonor (or transmitter). Histidine 105-114 hypothetical protein Escherichia coli 58-62