TCDB is operated by the Saier Lab Bioinformatics Group
« See all members of the family


1.A.1.21.1
K+- and Na+-conducting NaK channel, NaK2K of 97 aas and 2 TMSs. The 3-D structure has been solved with Na+ and K+bound (Shi et al., 2006).  It exhibits tight structural and dynamic coupling between the selectivity filter and the channel scaffold (Brettmann et al. 2015). A hydrophobic residue at the bottom of the selectivity filter, Phe92, appears in dual conformations. One of the two conformations of Phe92 restricts the diameter of the exit pore around the selectivity filter, limiting ion flow through the channel, while the other conformation of Phe92 provides a larger-diameter exit pore from the selectivity filter. Thus, Phe92 acts as a hydrophobic gate (Langan et al. 2020).

Accession Number:Q81HW2
Protein Name:Potassium channel protein
Length:114
Molecular Weight:12894.00
Species:Bacillus cereus (strain ATCC 14579 / DSM 31) [226900]
Number of TMSs:2
Location1 / Topology2 / Orientation3: Cell membrane1 / Multi-pass membrane protein2
Substrate K+, Na+

Cross database links:

DIP: DIP-46436N
RefSeq: NP_830482.1   
Entrez Gene ID: 1203020   
Pfam: PF07885   
BioCyc: BCER226900:BC_0669-MONOMER   
KEGG: bce:BC0669   

Gene Ontology

GO:0005216 F:ion channel activity

References (1)

[1] “Genome sequence of Bacillus cereus and comparative analysis with Bacillus anthracis.”  Ivanova N.et.al.   12721630
Structure:
2AHY   2AHZ   2Q67   2Q68   2Q69   2Q6A   3E83   3E86   3E89   3E8B   [...more]

External Searches:

Analyze:

Predict TMSs (Predict number of transmembrane segments)
Window Size: Angle:  
FASTA formatted sequence
1:	MLSFLLTLKR MLRACLRAWK DKEFQVLFVL TILTLISGTI FYSTVEGLRP IDALYFSVVT 
61:	LTTVGDGNFS PQTDFGKIFT ILYIFIGIGL VFGFIHKLAV NVQLPSILSN RKKE