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2.A.38.4.3
Low affinity (1 mM) K+ uptake transporter, KtrAB. Evidence for structural similarities between potassium channels and KtrB proteins in the extracellular half of the molecule and differences in the cytoplasmic regions has been obtained (Albright et al., 2007). This system is responsible for K+ accumulation in the cell cytoplasm, allowing oscillatory release of K+ from a biofilm through the BikC (YugO) K+ channel for the attraction of other bacteria (both of the same and different species) to the biofilm (Humphries et al. 2017).

Accession Number:O32080
Protein Name:KtrA aka YuaA
Length:222
Molecular Weight:24882.00
Species:Bacillus subtilis [1423]
Location1 / Topology2 / Orientation3: Cell membrane1 / Peripheral membrane protein2 / Cytoplasmic side3
Substrate potassium(1+)

Cross database links:

RefSeq: NP_390987.1   
Entrez Gene ID: 937145   
Pfam: PF02080    PF02254   
BioCyc: SUBTI:BSU31090-MONOMER   
KEGG: bsu:BSU31090   

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 (4)

[1] “The complete genome sequence of the Gram-positive bacterium Bacillus subtilis.”  Kunst F.et.al.   9384377
[2] “KtrAB and KtrCD: two K+ uptake systems in Bacillus subtilis and their role in adaptation to hypertonicity.”  Holtmann G.et.al.   12562800
[3] “A mechanism of regulating transmembrane potassium flux through a ligand-mediated conformational switch.”  Roosild T.P.et.al.   12086676
[4] “The RCK domain of the KtrAB K+ transporter: multiple conformations of an octameric ring.”  Albright R.A.et.al.   16990138
Structure:
1LSU   2HMS   2HMT   2HMU   2HMV   2HMW   4J7C   4J90   4J91   5BUT   [...more]

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Predict TMSs (Predict number of transmembrane segments)
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FASTA formatted sequence
1:	MGRIKNKQFA VIGLGRFGGS ICKELHRMGH EVLAVDINEE KVNAYASYAT HAVIANATEE 
61:	NELLSLGIRN FEYVIVAIGA NIQASTLTTL LLKELDIPNI WVKAQNYYHH KVLEKIGADR 
121:	IIHPEKDMGV KIAQSLSDEN VLNYIDLSDE YSIVELLATR KLDSKSIIDL NVRAKYGCTI 
181:	LAIKHHGDIC LSPAPEDIIR EQDCLVIMGH KKDIKRFENE GM