UniProt functional annotation for O27564



	UniProt functional annotation for O27564

UniProt code: O27564.

Organism: Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H) (Methanobacterium thermoautotrophicum).

Taxonomy: Archaea; Euryarchaeota; Methanomada group; Methanobacteria; Methanobacteriales; Methanobacteriaceae; Methanothermobacter.

Function: Calcium-gated potassium channel.

Subunit: Homotetramer.

Subcellular location: Cell membrane; Multi-pass membrane protein.

Domain: The channel is composed of 4 repeated units, each containing a transmembrane pore part and a gating ring part. The gating ring is composed of eight identical RCK (Regulators of K conductance) domains, in an alternating arrangement of one domain from each of the four subunits and four from the intracellular solution. Two protein interfaces between dimers of RCK domains from the pore-forming subunit and from the intracellular solution hold the ring together. One is called the fixed interface and the other the flexible interface. The flexible interface forms a cleft where calcium binds. Upon calcium binding the gating ring undergoes a conformational change that enables it to pull open the inner helices of the pore, allowing ion conduction.

Miscellaneous: It is not known whether calcium is the physiological ligand.

Miscellaneous: Inhibited by charybdotoxin (CTX), a protein from scorpion venom.

Annotations taken from UniProtKB at the EBI.


Organism:		Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H) (Methanobacterium thermoautotrophicum).
Taxonomy:		Archaea; Euryarchaeota; Methanomada group; Methanobacteria; Methanobacteriales; Methanobacteriaceae; Methanothermobacter.



Function:		Calcium-gated potassium channel.


Subunit:		Homotetramer.
Subcellular location:		Cell membrane; Multi-pass membrane protein.
Domain:		The channel is composed of 4 repeated units, each containing a transmembrane pore part and a gating ring part. The gating ring is composed of eight identical RCK (Regulators of K conductance) domains, in an alternating arrangement of one domain from each of the four subunits and four from the intracellular solution. Two protein interfaces between dimers of RCK domains from the pore-forming subunit and from the intracellular solution hold the ring together. One is called the fixed interface and the other the flexible interface. The flexible interface forms a cleft where calcium binds. Upon calcium binding the gating ring undergoes a conformational change that enables it to pull open the inner helices of the pore, allowing ion conduction.
Miscellaneous:		It is not known whether calcium is the physiological ligand.
Miscellaneous:		Inhibited by charybdotoxin (CTX), a protein from scorpion venom.