-
DVU_0413 is annotated as TrkH-family K+ uptake membrane subunit containing TrkH (PF02386) and Cat_transpt (IPR003445) domains
"Target verification: The UniProt record provided maps Q72F05 to DVU_0413 from Desulfovibrio vulgaris Hildenborough and annotates it as a TrkH-family potassium uptake protein with TrkH (PF02386) and cation transporter/cation transpt (IPR003445) domains"
-
TrkH/KtrB-family pores are selective for K+ and operate as low-affinity, membrane-potential-driven channels
"TrkH/KtrB-family pores are selective for K+ and operate as low-affinity, membrane-potential-driven channels rather than primary active transporters; ATP acts as a ligand for the cytosolic RCK ring (not as a direct energy source for pumping)"
-
TrkH/KtrB homologs are integral inner-membrane proteins forming the K+ conductance pathway
"Cellular localization: TrkH/KtrB homologs are integral inner-membrane proteins forming the K+ conductance pathway; DVU_0413's TrkH domain architecture and transmembrane nature support inner-membrane localization"
-
Trk/Ktr systems exploit membrane potential for inward K+ flux when extracellular K+ is high
"Trk/Ktr systems are generally ATP-gated channels that exploit the membrane potential for inward K+ flux when extracellular K+ is relatively high (mM range)"
-
KtrAB-type complexes are gated by RCK octameric rings with ATP/ADP-dependent activation
"KtrAB-type complexes are gated by RCK octameric rings (KtrA/TrkA); ATP binding (vs ADP) adopts an activating conformation"
-
Trk-type K+ transporters are key features associated with salinity adaptation
"Trk-type K+ transporter ranked as the top genomic feature linked to high salinity, highlighting the ecological importance of TrkH-mediated salt-in strategies"