ID A4Y1B9_SHEPC Unreviewed; 485 AA.
AC A4Y1B9;
DT 29-MAY-2007, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2007, sequence version 1.
DT 27-MAR-2024, entry version 85.
DE RecName: Full=Trk system potassium uptake protein {ECO:0000256|PIRNR:PIRNR006247};
DE Flags: Precursor;
GN OrderedLocusNames=Sputcn32_0016 {ECO:0000313|EMBL:ABP73752.1};
OS Shewanella putrefaciens (strain CN-32 / ATCC BAA-453).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=319224 {ECO:0000313|EMBL:ABP73752.1};
RN [1] {ECO:0000313|EMBL:ABP73752.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CN-32 {ECO:0000313|EMBL:ABP73752.1};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Mikhailova N., Romine M.F., Fredrickson J.,
RA Tiedje J., Richardson P.;
RT "Complete sequence of Shewanella putrefaciens CN-32.";
RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
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|ARBA:ARBA00004429, ECO:0000256|PIRNR:PIRNR006247}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004429,
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|ARBA:ARBA00009137, ECO:0000256|PIRNR:PIRNR006247}.
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DR EMBL; CP000681; ABP73752.1; -; Genomic_DNA.
DR AlphaFoldDB; A4Y1B9; -.
DR STRING; 319224.Sputcn32_0016; -.
DR KEGG; spc:Sputcn32_0016; -.
DR eggNOG; COG0168; Bacteria.
DR HOGENOM; CLU_030708_0_2_6; -.
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 NCBIfam; TIGR00933; 2a38; 1.
DR PANTHER; PTHR32024; TRK SYSTEM POTASSIUM UPTAKE PROTEIN TRKG-RELATED; 1.
DR PANTHER; PTHR32024:SF2; 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|ARBA:ARBA00022519,
KW 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 12..32
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 38..57
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 69..90
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 136..161
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 184..202
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 237..255
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 276..295
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 333..366
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 398..420
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 458..483
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT BINDING 111
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000256|PIRSR:PIRSR006247-1"
FT BINDING 112
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000256|PIRSR:PIRSR006247-1"
FT BINDING 220
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000256|PIRSR:PIRSR006247-1"
FT BINDING 221
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000256|PIRSR:PIRSR006247-1"
FT BINDING 320
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000256|PIRSR:PIRSR006247-1"
FT BINDING 321
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000256|PIRSR:PIRSR006247-1"
FT BINDING 437
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000256|PIRSR:PIRSR006247-1"
FT BINDING 438
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000256|PIRSR:PIRSR006247-1"
SQ SEQUENCE 485 AA; 53264 MW; 4E7ECD90E71D9986 CRC64;
MQYKTIIRII GLLIGLFSIT MLPPALIAIW YNDGGGTAFI QAFFVSLFIG FWLWYPNRRC
KEELRTREGF LIVVLFWTVL GSIGSLPFIF SNQPDLSWTD SFFESFSALT TTGATVIVGL
DSLPKAILFY RHMLQWLGGM GIIVLAVAIL PVLGVGGMQL YRAEIPGPVK DSKMTPRIAE
TAKALWYIYL LLTISCAGAY WLAGMSIFDA ICHSFSTIAI GGFSTHDASM GYFDSPVINL
ICVFFLIVSA VNFSVHFAAF SRRGINVKVY FKDTEFKMLV AIQLILTAIC FLTLYHSGIY
ESPEETLDQA LFQAVSVATT AGFGTDSFHM WPLFLPMLLI FSSFIGGCGG STAGGIKVIR
VILLLLQGSR ELKRLVHPKA MFSIRIGSKA LPDRVVDAVW GFFSAYALVF VICMLALMAM
GLDDITAFSA TAACLNNLGP GLGEVASNYA SIGDGAKWVL VVAMLFGRLE VFTLLILFTP
TFWKN
//
