TRKH_HAEIN
ID TRKH_HAEIN Reviewed; 487 AA.
AC P44843;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-1998, sequence version 2.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Trk system potassium uptake protein TrkH;
GN Name=trkH; OrderedLocusNames=HI_0723;
OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=71421;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=7542800; DOI=10.1126/science.7542800;
RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT Rd.";
RL Science 269:496-512(1995).
RN [2]
RP SEQUENCE REVISION.
RA White O., Clayton R.A., Kerlavage A.R., Fleischmann R.D., Peterson J.,
RA Hickey E., Dodson R., Gwinn M.;
RL Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases.
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; L42023; AAC22381.1; -; Genomic_DNA.
DR RefSeq; NP_438881.1; NC_000907.1.
DR RefSeq; WP_005694630.1; NC_000907.1.
DR AlphaFoldDB; P44843; -.
DR SMR; P44843; -.
DR STRING; 71421.HI_0723; -.
DR EnsemblBacteria; AAC22381; AAC22381; HI_0723.
DR KEGG; hin:HI_0723; -.
DR PATRIC; fig|71421.8.peg.755; -.
DR eggNOG; COG0168; Bacteria.
DR HOGENOM; CLU_030708_0_2_6; -.
DR OMA; LQWMGGM; -.
DR PhylomeDB; P44843; -.
DR BioCyc; HINF71421:G1GJ1-757-MON; -.
DR Proteomes; UP000000579; 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..487
FT /note="Trk system potassium uptake protein TrkH"
FT /id="PRO_0000070477"
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 ?..277
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 278..298
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 299..?
FT /note="Periplasmic"
FT /evidence="ECO:0000250"
FT INTRAMEM ?..304
FT /evidence="ECO:0000250"
FT INTRAMEM 305..320
FT /note="Helical; Pore-forming"
FT /evidence="ECO:0000250"
FT INTRAMEM 321..326
FT /evidence="ECO:0000250"
FT TOPO_DOM 327..334
FT /note="Periplasmic"
FT /evidence="ECO:0000250"
FT INTRAMEM 335..346
FT /note="Helical"
FT /evidence="ECO:0000250"
FT INTRAMEM 347..359
FT /note="Note=Loop between two helices"
FT /evidence="ECO:0000250"
FT INTRAMEM 360..?
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM ?..393
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 394..421
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 422..423
FT /note="Periplasmic"
FT /evidence="ECO:0000250"
FT INTRAMEM 424..425
FT /evidence="ECO:0000250"
FT INTRAMEM 426..436
FT /note="Helical; Pore-forming"
FT /evidence="ECO:0000250"
FT INTRAMEM 437..443
FT /evidence="ECO:0000250"
FT TOPO_DOM 444..455
FT /note="Periplasmic"
FT /evidence="ECO:0000250"
FT INTRAMEM 456..467
FT /note="Helical"
FT /evidence="ECO:0000250"
FT INTRAMEM 468..?
FT /evidence="ECO:0000250"
FT TOPO_DOM ?..487
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 321..326
FT /note="Selectivity filter part 3"
FT /evidence="ECO:0000250"
FT REGION 438..443
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 322
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250|UniProtKB:Q87TN7"
FT BINDING 323
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250|UniProtKB:Q87TN7"
FT BINDING 439
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250|UniProtKB:Q87TN7"
FT BINDING 440
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250|UniProtKB:Q87TN7"
SQ SEQUENCE 487 AA; 53469 MW; 91A8F38C37F4540A CRC64;
MRILSIIRII GILVMCFSGT MLVPAFVALI YGDGGGKAFM QAFMLSLIAG TLLWWPCHHH
KQELRSRDGF LIVVAFWLVL GSLATLPLLL FDSPHLTIAS AVFEAFSGLT TTGATVMTGL
DNLPKSILFY RQFLQWLGGM GIIVLAVAII PLLGIGGTQL YRAESSGPLK DQKSLPKISE
VAKALWIIYA SLTVLCAIAY WLSGMNLFDA IGHSFSTISN GGFSTHDASI GYFNQASIYW
VTTIFMLIGG VNFSLHISAF LALGKRNIWR NYWKDPEFRF FLTMQIIFIG IVSLSLYGYG
LVSDINEAVT KGALQLTSMS MTAGYTIFDI DNLPPFIGLL LVISAVIGGC GGSTTGGLKA
IRTLILWKQI DRELHSLIHP NLVQPIRIGK NRLAPRMIES IWAFFIIFIL VYWGCVFAVI
LCGMNTFDAM GAVFATLTNA GPGLGFIHES FIGVPESAKL VFSFAMICGR LEMFSLIVLF
IPSYWKK
