TRKH_ECOLI
ID TRKH_ECOLI Reviewed; 483 AA.
AC P0AFZ7; P21166; P76769; Q2M8F2;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Trk system potassium uptake protein TrkH;
GN Name=trkH; OrderedLocusNames=b3849, JW5576;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=2243799; DOI=10.1093/nar/18.21.6439;
RA Nakahigashi K., Inokuchi H.;
RT "Nucleotide sequence between the fadB gene and the rrnA operon from
RT Escherichia coli.";
RL Nucleic Acids Res. 18:6439-6439(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RX PubMed=7896723; DOI=10.1128/jb.177.7.1908-1910.1995;
RA Schlosser A., Meldorf M., Stumpe S., Bakker E.P., Epstein W.;
RT "TrkH and its homolog, TrkG, determine the specificity and kinetics of
RT cation transport by the Trk system of Escherichia coli.";
RL J. Bacteriol. 177:1908-1910(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=1379743; DOI=10.1126/science.1379743;
RA Daniels D.L., Plunkett G. III, Burland V.D., Blattner F.R.;
RT "Analysis of the Escherichia coli genome: DNA sequence of the region from
RT 84.5 to 86.5 minutes.";
RL Science 257:771-778(1992).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND SEQUENCE REVISION TO 69.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [5]
RP SEQUENCE REVISION.
RX PubMed=16397293; DOI=10.1093/nar/gkj405;
RA Riley M., Abe T., Arnaud M.B., Berlyn M.K.B., Blattner F.R.,
RA Chaudhuri R.R., Glasner J.D., Horiuchi T., Keseler I.M., Kosuge T.,
RA Mori H., Perna N.T., Plunkett G. III, Rudd K.E., Serres M.H., Thomas G.H.,
RA Thomson N.R., Wishart D., Wanner B.L.;
RT "Escherichia coli K-12: a cooperatively developed annotation snapshot
RT -- 2005.";
RL Nucleic Acids Res. 34:1-9(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [7]
RP FUNCTION.
RC STRAIN=TK1001;
RX PubMed=11700350; DOI=10.1099/00221287-147-11-2991;
RA Harms C., Domoto Y., Celik C., Rahe E., Stumpe S., Schmid R., Nakamura T.,
RA Bakker E.P.;
RT "Identification of the ABC protein SapD as the subunit that confers ATP
RT dependence to the K+-uptake systems Trk(H) and Trk(G) from Escherichia coli
RT K-12.";
RL Microbiology 147:2991-3003(2001).
RN [8]
RP SUBCELLULAR LOCATION.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=15919996; DOI=10.1126/science.1109730;
RA Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.;
RT "Global topology analysis of the Escherichia coli inner membrane
RT proteome.";
RL Science 308:1321-1323(2005).
CC -!- FUNCTION: Low-affinity potassium transport system. Interacts with Trk
CC system potassium uptake protein TrkA. Requires TrkE (sapD) for
CC transport activity, 20% more uptake is seen with both SapD and SapF
CC (PubMed:11700350). Transport in the absence of SapD and SapF is
CC dependent on a high membrane potential and a high cytoplasmic ATP
CC concentration, suggesting this protein may be able to interact with
CC other ATP-binding proteins (PubMed:11700350). Can transport potassium
CC and rubidium (PubMed:7896723). {ECO:0000250,
CC ECO:0000269|PubMed:11700350, ECO:0000269|PubMed:7896723}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=6 mM for K(+) {ECO:0000269|PubMed:7896723};
CC KM=2 mM for Rb(+) {ECO:0000269|PubMed:7896723};
CC Vmax=800 umol/min/g enzyme with K(+) as substrate
CC {ECO:0000269|PubMed:7896723};
CC Vmax=10 umol/min/g enzyme with Rb(+) as substrate
CC {ECO:0000269|PubMed:7896723};
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000269|PubMed:15919996}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:15919996}.
CC -!- SIMILARITY: Belongs to the TrkH potassium transport family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA67646.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=X54687; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; X54687; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; M87049; AAA67646.1; ALT_FRAME; Genomic_DNA.
DR EMBL; U00096; AAT48231.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77454.1; -; Genomic_DNA.
DR PIR; B65190; B65190.
DR RefSeq; WP_000545677.1; NZ_STEB01000021.1.
DR RefSeq; YP_026273.1; NC_000913.3.
DR AlphaFoldDB; P0AFZ7; -.
DR SMR; P0AFZ7; -.
DR BioGRID; 4262619; 7.
DR DIP; DIP-47978N; -.
DR IntAct; P0AFZ7; 2.
DR STRING; 511145.b3849; -.
DR TCDB; 2.A.38.1.1; the k(+) transporter (trk) family.
DR PaxDb; P0AFZ7; -.
DR PRIDE; P0AFZ7; -.
DR EnsemblBacteria; AAT48231; AAT48231; b3849.
DR EnsemblBacteria; BAE77454; BAE77454; BAE77454.
DR GeneID; 66672245; -.
DR GeneID; 948333; -.
DR KEGG; ecj:JW5576; -.
DR KEGG; eco:b3849; -.
DR PATRIC; fig|1411691.4.peg.2861; -.
DR EchoBASE; EB1014; -.
DR eggNOG; COG0168; Bacteria.
DR HOGENOM; CLU_030708_0_2_6; -.
DR InParanoid; P0AFZ7; -.
DR OMA; LQWMGGM; -.
DR PhylomeDB; P0AFZ7; -.
DR BioCyc; EcoCyc:TRKH-MON; -.
DR BioCyc; MetaCyc:TRKH-MON; -.
DR PRO; PR:P0AFZ7; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
DR GO; GO:0005267; F:potassium channel activity; ISS:UniProtKB.
DR GO; GO:0030955; F:potassium ion binding; ISS:UniProtKB.
DR GO; GO:0015079; F:potassium ion transmembrane transporter activity; IMP:EcoCyc.
DR GO; GO:0015379; F:potassium:chloride symporter activity; IEA:InterPro.
DR GO; GO:0071805; P:potassium ion transmembrane transport; IMP:EcoCyc.
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 1: Evidence at protein level;
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_0000070475"
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"
FT CONFLICT 69
FT /note="Missing (in Ref. 3; AAA67646)"
FT /evidence="ECO:0000305"
FT CONFLICT 144
FT /note="V -> IV (in Ref. 1; X54687)"
FT /evidence="ECO:0000305"
FT CONFLICT 196
FT /note="C -> S (in Ref. 1; X54687)"
FT /evidence="ECO:0000305"
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
