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Database: UniProt
Entry: E6Z0B2_BARSR
LinkDB: E6Z0B2_BARSR
Original site: E6Z0B2_BARSR 
ID   E6Z0B2_BARSR            Unreviewed;       462 AA.
AC   E6Z0B2;
DT   08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT   08-MAR-2011, sequence version 1.
DT   24-JAN-2024, entry version 36.
DE   RecName: Full=Trk system potassium uptake protein {ECO:0000256|PIRNR:PIRNR006247};
GN   Name=trkH {ECO:0000313|EMBL:CBI82550.1};
GN   ORFNames=B11C_40405 {ECO:0000313|EMBL:CBI82550.1};
OS   Bartonella schoenbuchensis (strain DSM 13525 / NCTC 13165 / R1).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Bartonellaceae; Bartonella.
OX   NCBI_TaxID=687861 {ECO:0000313|EMBL:CBI82550.1};
RN   [1] {ECO:0000313|EMBL:CBI82550.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=R1 {ECO:0000313|EMBL:CBI82550.1};
RX   PubMed=21347280; DOI=10.1371/journal.pgen.1001296;
RA   Engel P., Salzburger W., Liesch M., Chang C.C., Maruyama S., Lanz C.,
RA   Calteau A., Lajus A., Medigue C., Schuster S.C., Dehio C.;
RT   "Parallel evolution of a type IV secretion system in radiating lineages of
RT   the host-restricted bacterial pathogen Bartonella.";
RL   PLoS Genet. 7:E1001296-E1001296(2011).
CC   -!- FUNCTION: Low-affinity potassium transport system. Interacts with Trk
CC       system potassium uptake protein TrkA. {ECO:0000256|PIRNR:PIRNR006247}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane
CC       {ECO:0000256|PIRNR:PIRNR006247}; Multi-pass membrane protein
CC       {ECO:0000256|PIRNR:PIRNR006247}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the TrkH potassium transport family.
CC       {ECO:0000256|PIRNR:PIRNR006247}.
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DR   EMBL; FN645509; CBI82550.1; -; Genomic_DNA.
DR   AlphaFoldDB; E6Z0B2; -.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0015379; F:potassium:chloride symporter activity; IEA:InterPro.
DR   InterPro; IPR003445; Cat_transpt.
DR   InterPro; IPR004772; TrkH.
DR   PANTHER; PTHR32024:SF3; TRK SYSTEM POTASSIUM UPTAKE PROTEIN; 1.
DR   PANTHER; PTHR32024; TRK SYSTEM POTASSIUM UPTAKE PROTEIN TRKG-RELATED; 1.
DR   Pfam; PF02386; TrkH; 1.
DR   PIRSF; PIRSF006247; TrkH; 1.
PE   3: Inferred from homology;
KW   Cell inner membrane {ECO:0000256|PIRNR:PIRNR006247};
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475,
KW   ECO:0000256|PIRNR:PIRNR006247};
KW   Ion transport {ECO:0000256|ARBA:ARBA00023065,
KW   ECO:0000256|PIRNR:PIRNR006247};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PIRNR:PIRNR006247};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR006247-1};
KW   Potassium {ECO:0000256|ARBA:ARBA00022958, ECO:0000256|PIRNR:PIRNR006247};
KW   Potassium transport {ECO:0000256|ARBA:ARBA00022538,
KW   ECO:0000256|PIRNR:PIRNR006247};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|PIRNR:PIRNR006247}.
FT   TRANSMEM        16..36
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        48..70
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        107..129
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        158..180
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        215..239
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        251..269
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        275..292
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        304..326
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        372..392
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        433..456
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   BINDING         90
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006247-1"
FT   BINDING         91
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006247-1"
FT   BINDING         294
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006247-1"
FT   BINDING         295
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006247-1"
FT   BINDING         411
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006247-1"
SQ   SEQUENCE   462 AA;  50370 MW;  3E6A1E72570BA57F CRC64;
     MLLPALADLR DGNHNWAAFL YSCVITTMLA TLILLATRGA SCRFSARLGF TLTLCLWLTG
     SIVGALPLYL SPLPISLAGA IFESVSGITT TGSTVITGLD NLSRSILLWR SLICWIGGIG
     FIGLALLLLP SLRVGGVQLF HMESSDKSEK ILPRINQIAN GIIIAYIGLT LACMLSYFAA
     GMTLFDAINH AMSTIATAGF STHDASFGYF SDKPAILIVS TIFMLLSALP FVLYVKLVLP
     GQSKRSIDPQ VIVFLNIVFF FSFALAVWLR SQDHLTFHWA FLDVIFHFVS IISTTGYSAE
     NYQLWGPFAF GVFFIVSFTG GCAGSTSGGI KINRLIILWR IAQTNMAKLL SPNAVVKVRY
     DHSNISNDIA QSVLLFVCLY MFCLLIGTTL LLTTGLDFTS AFTGVLTALS NIGPGFGEII
     GPSGNFMTIN DNALWILSFL MLAGRLEIIT IFVFFIPTFW RE
//
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