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2.A.38.4.2
High affinity (Km <50 μM) KtrA binds ATP to a β-α-β-Rossman fold. Other nucleotides bound, but only ATP bound with high affinity and changed the conformation of KtrA so that KtrA and KtrB associate (Kroning et al., 2007) in vivo. Both ATP and ΔΨ were required for transport activity. K+ uptake may occur by a Na+:K+ symport mechanism.  However, one region of KtrB, the transmembrane helix (M(2C); 40aas long) seems to control K+ transport non-coordinately with Na+ symport (Haenelt et al., 2010). M2C2 may form a flexible "gate" controlling K+ translocation at the cytoplasmic side of KtrB (Hänelt et al. 2010).  M(2C2) seems to be required for the interaction between KtrA and KtrB.

Accession Number:O87952
Protein Name:KtrA
Length:220
Molecular Weight:23806.00
Species:Vibrio alginolyticus [663]
Number of TMSs:1
Location1 / Topology2 / Orientation3: Cell inner membrane1 / Single-pass membrane protein2
Substrate sodium(1+), potassium(1+)

Cross database links:

Pfam: PF02080    PF02254   

Gene Ontology

GO:0005886 C:plasma membrane
GO:0005488 F:binding
GO:0003824 F:catalytic activity
GO:0008324 F:cation transmembrane transporter activity
GO:0008152 P:metabolic process
GO:0006813 P:potassium ion transport

References (1)

[1] “KtrAB, a new type of bacterial K(+)-uptake system from Vibrio alginolyticus.”  Nakamura T.et.al.   9642210

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Predict TMSs (Predict number of transmembrane segments)
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FASTA formatted sequence 
1:	MKTGDKQFAV IGLGRFGLAV CKELQDSGSQ VLAVDINEDR VKEAAGFVSQ AIVANCTHEE 
61:	TVAELKLDDY DMVMIAIGAD VNASILATLI AKEAGVKSVW VKANDRFQAR VLQKIGADHI 
121:	IMPERDMGIR VARKMLDKRV LEFHPLGSGL AMTEFVVGSR LMGKTLSDLA LCKVEGVQVL 
181:	GYKRGPEIIK APDMSTTLEI GDLIIVVGPQ DKLANKLKSL