TRKG_ECOLI
ID TRKG_ECOLI Reviewed; 485 AA.
AC P23849;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1991, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Trk system potassium uptake protein TrkG;
GN Name=trkG; OrderedLocusNames=b1363, JW1358;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND SUBCELLULAR LOCATION.
RC STRAIN=K12;
RX PubMed=2022616; DOI=10.1128/jb.173.10.3170-3176.1991;
RA Schloesser A., Kluttig S., Hamann A., Bakker E.P.;
RT "Subcloning, nucleotide sequence, and expression of trkG, a gene that
RT encodes an integral membrane protein involved in potassium uptake via the
RT Trk system of Escherichia coli.";
RL J. Bacteriol. 173:3170-3176(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9097039; DOI=10.1093/dnares/3.6.363;
RA Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K.,
RA Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S.,
RA Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G.,
RA Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y.,
RA Wada C., Yamamoto Y., Horiuchi T.;
RT "A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 28.0-40.1 min region on the linkage map.";
RL DNA Res. 3:363-377(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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 [4]
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 [5]
RP FUNCTION.
RX PubMed=2674131; DOI=10.1016/s0021-9258(19)84721-x;
RA Bossemeyer D., Borchard A., Dosch D.C., Helmer G.C., Epstein W.,
RA Booth I.R., Bakker E.P.;
RT "K+-transport protein TrkA of Escherichia coli is a peripheral membrane
RT protein that requires other trk gene products for attachment to the
RT cytoplasmic membrane.";
RL J. Biol. Chem. 264:16403-16410(1989).
RN [6]
RP FUNCTION, AND BIOPHYSICOCHEMICAL 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 [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, AND TOPOLOGY [LARGE SCALE ANALYSIS].
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 maximal
CC transport activity, low activity is seen in its absence; no further
CC stimulation is seen with SapF (PubMed:11700350). Transport in the
CC absence of SapD is dependent on a high membrane potential and a high
CC cytoplasmic ATP concentration, suggesting this protein may be able to
CC interact with other ATP-binding proteins (PubMed:11700350). Can
CC transport potassium and rubidium (PubMed:7896723).
CC {ECO:0000269|PubMed:11700350, ECO:0000269|PubMed:2022616,
CC ECO:0000269|PubMed:2674131, ECO:0000269|PubMed:7896723}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1 mM for K(+) {ECO:0000269|PubMed:7896723};
CC KM=0.4 mM for Rb(+) {ECO:0000269|PubMed:7896723};
CC Vmax=300 umol/min/g enzyme with K(+) as substrate
CC {ECO:0000269|PubMed:7896723};
CC Vmax=17 umol/min/g enzyme with Rb(+) as substrate
CC {ECO:0000269|PubMed:7896723};
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:15919996,
CC ECO:0000269|PubMed:2022616}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:2022616}.
CC -!- SIMILARITY: Belongs to the TrkH potassium transport family.
CC {ECO:0000305}.
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DR EMBL; X56783; CAA40103.1; -; Genomic_DNA.
DR EMBL; U00096; AAC74445.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA14960.1; -; Genomic_DNA.
DR PIR; A39408; A39408.
DR RefSeq; NP_415881.1; NC_000913.3.
DR RefSeq; WP_001097895.1; NZ_SSUV01000042.1.
DR AlphaFoldDB; P23849; -.
DR SMR; P23849; -.
DR BioGRID; 4260161; 11.
DR DIP; DIP-11029N; -.
DR IntAct; P23849; 1.
DR STRING; 511145.b1363; -.
DR TCDB; 2.A.38.1.6; the k(+) transporter (trk) family.
DR jPOST; P23849; -.
DR PaxDb; P23849; -.
DR PRIDE; P23849; -.
DR EnsemblBacteria; AAC74445; AAC74445; b1363.
DR EnsemblBacteria; BAA14960; BAA14960; BAA14960.
DR GeneID; 60668599; -.
DR GeneID; 66674797; -.
DR GeneID; 945932; -.
DR KEGG; ecj:JW1358; -.
DR KEGG; eco:b1363; -.
DR PATRIC; fig|511145.12.peg.1422; -.
DR EchoBASE; EB1013; -.
DR eggNOG; COG0168; Bacteria.
DR HOGENOM; CLU_030708_0_2_6; -.
DR InParanoid; P23849; -.
DR OMA; HTARIIW; -.
DR PhylomeDB; P23849; -.
DR BioCyc; EcoCyc:TRKG-MON; -.
DR BioCyc; MetaCyc:TRKG-MON; -.
DR PRO; PR:P23849; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:EcoCyc.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
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:CACAO.
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 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..485
FT /note="Trk system potassium uptake protein TrkG"
FT /id="PRO_0000070474"
FT TOPO_DOM 1..5
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 6..32
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 33..38
FT /note="Periplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 39..60
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 61..68
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 69..93
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 94..?
FT /note="Periplasmic"
FT /evidence="ECO:0000250"
FT INTRAMEM ?..100
FT /evidence="ECO:0000250"
FT INTRAMEM 101..112
FT /note="Helical; Pore-forming"
FT /evidence="ECO:0000250"
FT INTRAMEM 113..118
FT /evidence="ECO:0000250"
FT TOPO_DOM 119..127
FT /note="Periplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 128..153
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 154..180
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 181..205
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 206..208
FT /note="Periplasmic"
FT /evidence="ECO:0000250"
FT INTRAMEM 209
FT /evidence="ECO:0000250"
FT INTRAMEM 210..221
FT /note="Helical; Pore-forming"
FT /evidence="ECO:0000250"
FT INTRAMEM 222..227
FT /evidence="ECO:0000250"
FT TOPO_DOM 228..237
FT /note="Periplasmic"
FT /evidence="ECO:0000250"
FT INTRAMEM 238..253
FT /note="Helical"
FT /evidence="ECO:0000250"
FT INTRAMEM 254..?
FT /evidence="ECO:0000250"
FT TOPO_DOM ?..276
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 277..297
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 298..?
FT /note="Periplasmic"
FT /evidence="ECO:0000250"
FT INTRAMEM ?..302
FT /evidence="ECO:0000250"
FT INTRAMEM 303..318
FT /note="Helical; Pore-forming"
FT /evidence="ECO:0000250"
FT INTRAMEM 319..324
FT /evidence="ECO:0000250"
FT TOPO_DOM 325..332
FT /note="Periplasmic"
FT /evidence="ECO:0000250"
FT INTRAMEM 333..344
FT /note="Helical"
FT /evidence="ECO:0000250"
FT INTRAMEM 345..357
FT /note="Note=Loop between two helices"
FT /evidence="ECO:0000250"
FT INTRAMEM 358..?
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM ?..391
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 392..419
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 420..421
FT /note="Periplasmic"
FT /evidence="ECO:0000250"
FT INTRAMEM 422..423
FT /evidence="ECO:0000250"
FT INTRAMEM 424..434
FT /note="Helical; Pore-forming"
FT /evidence="ECO:0000250"
FT INTRAMEM 435..441
FT /evidence="ECO:0000250"
FT TOPO_DOM 442..453
FT /note="Periplasmic"
FT /evidence="ECO:0000250"
FT INTRAMEM 454..465
FT /note="Helical"
FT /evidence="ECO:0000250"
FT INTRAMEM 466..?
FT /evidence="ECO:0000250"
FT TOPO_DOM ?..485
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250, ECO:0000269|PubMed:15919996"
FT REGION 113..118
FT /note="Selectivity filter part 1"
FT /evidence="ECO:0000250"
FT REGION 222..227
FT /note="Selectivity filter part 2"
FT /evidence="ECO:0000250"
FT REGION 319..324
FT /note="Selectivity filter part 3"
FT /evidence="ECO:0000250"
FT REGION 436..441
FT /note="Selectivity filter part 4"
FT /evidence="ECO:0000250"
FT BINDING 114
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250|UniProtKB:Q87TN7"
FT BINDING 115
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250|UniProtKB:Q87TN7"
FT BINDING 223
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250|UniProtKB:Q87TN7"
FT BINDING 224
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250|UniProtKB:Q87TN7"
FT BINDING 320
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250|UniProtKB:Q87TN7"
FT BINDING 321
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250|UniProtKB:Q87TN7"
FT BINDING 437
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250|UniProtKB:Q87TN7"
FT BINDING 438
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250|UniProtKB:Q87TN7"
SQ SEQUENCE 485 AA; 53944 MW; 87E19BEC3B50B458 CRC64;
MNTSHVRVVT HMCGFLVWLY SLSMLPPMVV ALFYKEKSLF VFFITFVIFF CIGGGAWYTT
KKSGIQLRTR DGFIIIVMFW ILFSVISAFP LWIDSELNLT FIDALFEGVS GITTTGATVI
DDVSSLPRAY LYYRSQLNFI GGLGVIVLAV AVLPLLGIGG AKLYQSEMPG PFKDDKLTPR
LADTSRTLWI TYSLLGIACI VCYRLAGMPL FDAICHGIST VSLGGFSTHS ESIGYFNNYL
VELVAGSFSL LSAFNFTLWY IVISRKTIKP LIRDIELRFF LLIALGVIIV TSFQVWHIGM
YDLHGSFIHS FFLASSMLTD NGLATQDYAS WPTHTIVFLL LSSFFGGCIG STCGGIKSLR
FLILFKQSKH EINQLSHPRA LLSVNVGGKI VTDRVMRSVW SFFFLYTLFT VFFILVLNGM
GYDFLTSFAT VAACINNMGL GFGATASSFG VLNDIAKCLM CIAMILGRLE IYPVIILFSG
FFWRS
