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TRKH_ECO57
ID   TRKH_ECO57              Reviewed;         483 AA.
AC   P0AFZ8; P21166; P76769;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   20-DEC-2005, sequence version 1.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=Trk system potassium uptake protein TrkH;
GN   Name=trkH; OrderedLocusNames=Z5371, ECs4777;
OS   Escherichia coli O157:H7.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83334;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX   PubMed=11206551; DOI=10.1038/35054089;
RA   Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA   Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA   Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA   Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA   Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA   Blattner F.R.;
RT   "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL   Nature 409:529-533(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX   PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA   Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA   Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA   Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA   Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT   genomic comparison with a laboratory strain K-12.";
RL   DNA Res. 8:11-22(2001).
CC   -!- FUNCTION: Low-affinity potassium transport system. Interacts with Trk
CC       system potassium uptake protein TrkA and requires TrkE for transport
CC       activity (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Multi-pass
CC       membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the TrkH potassium transport family.
CC       {ECO:0000305}.
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DR   EMBL; AE005174; AAG59043.1; -; Genomic_DNA.
DR   EMBL; BA000007; BAB38200.1; -; Genomic_DNA.
DR   PIR; A91226; A91226.
DR   PIR; G86072; G86072.
DR   RefSeq; NP_312804.1; NC_002695.1.
DR   RefSeq; WP_000545677.1; NZ_SWKA01000005.1.
DR   AlphaFoldDB; P0AFZ8; -.
DR   SMR; P0AFZ8; -.
DR   STRING; 155864.EDL933_5169; -.
DR   EnsemblBacteria; AAG59043; AAG59043; Z5371.
DR   EnsemblBacteria; BAB38200; BAB38200; ECs_4777.
DR   GeneID; 66672245; -.
DR   GeneID; 915125; -.
DR   KEGG; ece:Z5371; -.
DR   KEGG; ecs:ECs_4777; -.
DR   PATRIC; fig|386585.9.peg.4986; -.
DR   eggNOG; COG0168; Bacteria.
DR   HOGENOM; CLU_030708_0_2_6; -.
DR   OMA; LQWMGGM; -.
DR   Proteomes; UP000000558; Chromosome.
DR   Proteomes; UP000002519; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005267; F:potassium channel activity; ISS:UniProtKB.
DR   GO; GO:0030955; F:potassium ion binding; ISS:UniProtKB.
DR   GO; GO:0015379; F:potassium:chloride symporter activity; IEA:InterPro.
DR   GO; GO:0071805; P:potassium ion transmembrane transport; ISS:UniProtKB.
DR   InterPro; IPR003445; Cat_transpt.
DR   InterPro; IPR004772; TrkH.
DR   Pfam; PF02386; TrkH; 1.
DR   PIRSF; PIRSF006247; TrkH; 1.
DR   TIGRFAMs; TIGR00933; 2a38; 1.
PE   3: Inferred from homology;
KW   Cell inner membrane; Cell membrane; Ion channel; Ion transport; Membrane;
KW   Metal-binding; Potassium; Potassium transport; Reference proteome;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..483
FT                   /note="Trk system potassium uptake protein TrkH"
FT                   /id="PRO_0000070476"
FT   TOPO_DOM        1..2
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        3..29
FT                   /note="Helical"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        30..35
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        36..57
FT                   /note="Helical"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        58..65
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        66..90
FT                   /note="Helical"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        91..?
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000250"
FT   INTRAMEM        ?..97
FT                   /evidence="ECO:0000250"
FT   INTRAMEM        98..109
FT                   /note="Helical; Pore-forming"
FT                   /evidence="ECO:0000250"
FT   INTRAMEM        110..115
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        116..124
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        125..150
FT                   /note="Helical"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        151..177
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        178..202
FT                   /note="Helical"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        203..205
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000250"
FT   INTRAMEM        206
FT                   /evidence="ECO:0000250"
FT   INTRAMEM        207..218
FT                   /note="Helical; Pore-forming"
FT                   /evidence="ECO:0000250"
FT   INTRAMEM        219..224
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        225..234
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000250"
FT   INTRAMEM        235..250
FT                   /note="Helical"
FT                   /evidence="ECO:0000250"
FT   INTRAMEM        251..?
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        ?..273
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        274..294
FT                   /note="Helical"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        295..?
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000250"
FT   INTRAMEM        ?..300
FT                   /evidence="ECO:0000250"
FT   INTRAMEM        301..316
FT                   /note="Helical; Pore-forming"
FT                   /evidence="ECO:0000250"
FT   INTRAMEM        317..322
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        323..330
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000250"
FT   INTRAMEM        331..342
FT                   /note="Helical"
FT                   /evidence="ECO:0000250"
FT   INTRAMEM        343..355
FT                   /note="Note=Loop between two helices"
FT                   /evidence="ECO:0000250"
FT   INTRAMEM        356..?
FT                   /note="Helical"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        ?..389
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        390..417
FT                   /note="Helical"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        418..419
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000250"
FT   INTRAMEM        420..421
FT                   /evidence="ECO:0000250"
FT   INTRAMEM        422..432
FT                   /note="Helical; Pore-forming"
FT                   /evidence="ECO:0000250"
FT   INTRAMEM        433..439
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        440..451
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000250"
FT   INTRAMEM        452..463
FT                   /note="Helical"
FT                   /evidence="ECO:0000250"
FT   INTRAMEM        464..?
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        ?..483
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   REGION          110..115
FT                   /note="Selectivity filter part 1"
FT                   /evidence="ECO:0000250"
FT   REGION          219..224
FT                   /note="Selectivity filter part 2"
FT                   /evidence="ECO:0000250"
FT   REGION          317..322
FT                   /note="Selectivity filter part 3"
FT                   /evidence="ECO:0000250"
FT   REGION          434..439
FT                   /note="Selectivity filter part 4"
FT                   /evidence="ECO:0000250"
FT   BINDING         111
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /evidence="ECO:0000250|UniProtKB:Q87TN7"
FT   BINDING         112
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /evidence="ECO:0000250|UniProtKB:Q87TN7"
FT   BINDING         220
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /evidence="ECO:0000250|UniProtKB:Q87TN7"
FT   BINDING         221
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /evidence="ECO:0000250|UniProtKB:Q87TN7"
FT   BINDING         318
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /evidence="ECO:0000250|UniProtKB:Q87TN7"
FT   BINDING         319
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /evidence="ECO:0000250|UniProtKB:Q87TN7"
FT   BINDING         435
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /evidence="ECO:0000250|UniProtKB:Q87TN7"
FT   BINDING         436
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /evidence="ECO:0000250|UniProtKB:Q87TN7"
SQ   SEQUENCE   483 AA;  52960 MW;  1AA9CC2F83EB509A CRC64;
     MHFRAITRIV GLLVILFSGT MIIPGLVALI YRDGAGRAFT QTFFVALAIG SMLWWPNRKE
     KGELKSREGF LIVVLFWTVL GSVGALPFIF SESPNLTITD AFFESFSGLT TTGATTLVGL
     DSLPHAILFY RQMLQWFGGM GIIVLAVAIL PILGVGGMQL YRAEMPGPLK DNKMRPRIAE
     TAKTLWLIYV LLTVACALAL WFAGMDAFDA IGHSFATIAI GGFSTHDASI GYFDSPTINT
     IIAIFLLISG CNYGLHFSLL SGRSLKVYWR DPEFRMFIGV QFTLVVICTL VLWFHNVYSS
     ALMTINQAFF QVVSMATTAG FTTDSIARWP LFLPVLLLCS AFIGGCAGST GGGLKVIRIL
     LLFKQGNREL KRLVHPNAVY SIKLGNRALP ERILEAVWGF FSAYALVFIV SMLAIIATGV
     DDFSAFASVV ATLNNLGPGL GVVADNFTSM NPVAKWILIA NMLFGRLEVF TLLVLFTPTF
     WRE
 
 
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