Gene Ontology annotation through association of InterPro records with GO terms
Gene Ontology annotation based on UniProtKB/Swiss-Prot keyword mapping
-
Keyword propagation resulted in over-annotation of nucleotide binding and hydrolase activity to KdpC
-
These keywords apply to the KdpFABC complex or specifically to KdpB, not to KdpC
TreeGrafter-generated GO annotations
Combined Automated Annotation using Multiple IEA Methods
-
Some annotations conflate complex-level function with individual subunit function
-
ATP binding, P-type transporter activity, and hydrolase activity belong to KdpB, not KdpC
Method traceable to sequence similarity
Deep research report on KdpC function in D. vulgaris Hildenborough
-
KdpC is a catalytic chaperone that increases ATP-binding affinity of KdpB
"KdpC is not the catalytic ATPase; rather, it is a periplasmic single-spanning subunit thought to modulate ion access in the periplasmic vestibule and help stabilize the KdpA–KdpB interface"
-
KdpC forms transient KdpB/KdpC/ATP ternary complex
"This subunit acts as a catalytic chaperone that increases the ATP-binding affinity of the ATP-hydrolyzing subunit KdpB by the formation of a transient KdpB/KdpC/ATP ternary complex"
-
KdpC is periplasmically oriented and single-pass
"Periplasmically oriented, single-pass membrane protein embedded with KdpA/KdpB/KdpF in the cytoplasmic membrane"
-
KdpC role is non-catalytic but essential for complex function
"Contemporary models assign KdpC a non-catalytic but essential structural/modulatory role"
UniProt entry for Q725T8 (KdpC)
-
KdpC acts as a catalytic chaperone for KdpB
"This subunit acts as a catalytic chaperone that increases the ATP-binding affinity of the ATP-hydrolyzing subunit KdpB by the formation of a transient KdpB/KdpC/ATP ternary complex"
-
KdpC is a single-pass membrane protein in the cell inner membrane
"Cell inner membrane"
-
KdpC is part of the KdpFABC complex
"The system is composed of three essential subunits: KdpA, KdpB and KdpC"
Fast-forward on P-type ATPases: recent advances on structure and function
KdpD is a tandem serine histidine kinase that controls K(+) pump KdpFABC transcriptionally and post-translationally.