KUP_ECOLI
ID KUP_ECOLI Reviewed; 622 AA.
AC P63183; P30016; P76748; Q2M865;
DT 27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2004, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Low affinity potassium transport system protein kup;
DE AltName: Full=Kup system potassium uptake protein;
GN Name=kup; Synonyms=trkD; OrderedLocusNames=b3747, JW5609;
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=8226635; DOI=10.1128/jb.175.21.6925-6931.1993;
RA Schleyer M., Bakker E.P.;
RT "Nucleotide sequence and 3'-end deletion studies indicate that the K(+)-
RT uptake protein kup from Escherichia coli is composed of a hydrophobic core
RT linked to a large and partially essential hydrophilic C-terminus.";
RL J. Bacteriol. 175:6925-6931(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=7686882; DOI=10.1006/geno.1993.1230;
RA Burland V.D., Plunkett G. III, Daniels D.L., Blattner F.R.;
RT "DNA sequence and analysis of 136 kilobases of the Escherichia coli genome:
RT organizational symmetry around the origin of replication.";
RL Genomics 16:551-561(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND SEQUENCE REVISION.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=8265357; DOI=10.1093/nar/21.23.5408;
RA Blattner F.R., Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L.;
RT "Analysis of the Escherichia coli genome. IV. DNA sequence of the region
RT from 89.2 to 92.8 minutes.";
RL Nucleic Acids Res. 21:5408-5417(1993).
RN [4]
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 [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=K12;
RX PubMed=2649491; DOI=10.1128/jb.171.4.2219-2221.1989;
RA Bossemeyer D., Schloesser A., Bakker E.P.;
RT "Specific cesium transport via the Escherichia coli Kup (TrkD) K+ uptake
RT system.";
RL J. Bacteriol. 171:2219-2221(1989).
RN [8]
RP FUNCTION, AND INHIBITION BY CCCP.
RC STRAIN=K12;
RX PubMed=10214935; DOI=10.1016/s0014-5793(99)00288-4;
RA Trchounian A., Kobayashi H.;
RT "Kup is the major K+ uptake system in Escherichia coli upon hyper-osmotic
RT stress at a low pH.";
RL FEBS Lett. 447:144-148(1999).
RN [9]
RP FUNCTION.
RC STRAIN=K12;
RX PubMed=11682179; DOI=10.1111/j.1574-6968.2001.tb10863.x;
RA Zakharyan E., Trchounian A.;
RT "K+ influx by Kup in Escherichia coli is accompanied by a decrease in H+
RT efflux.";
RL FEMS Microbiol. Lett. 204:61-64(2001).
RN [10]
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: Responsible for the low-affinity transport of potassium into
CC the cell, with the probable concomitant uptake of protons (symport
CC system). Can also transport cesium. {ECO:0000269|PubMed:10214935,
CC ECO:0000269|PubMed:11682179, ECO:0000269|PubMed:2649491}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000269|PubMed:15919996}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:15919996}.
CC -!- MISCELLANEOUS: Kup is probably the major potassium uptake system upon
CC hyper-osmotic stress at a low pH.
CC -!- MISCELLANEOUS: Uptake is inhibited by protonophores such as CCCP.
CC -!- SIMILARITY: Belongs to the HAK/KUP transporter (TC 2.A.72) family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA62100.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; X68551; CAA48555.1; -; Genomic_DNA.
DR EMBL; L10328; AAA62100.1; ALT_FRAME; Genomic_DNA.
DR EMBL; U00096; AAT48204.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77541.1; -; Genomic_DNA.
DR PIR; A49345; A49345.
DR RefSeq; WP_000102319.1; NZ_STEB01000015.1.
DR RefSeq; YP_026244.1; NC_000913.3.
DR AlphaFoldDB; P63183; -.
DR BioGRID; 4263467; 29.
DR STRING; 511145.b3747; -.
DR TCDB; 2.A.72.1.1; the k(+) uptake permease (kup) family.
DR PaxDb; P63183; -.
DR PRIDE; P63183; -.
DR DNASU; 948255; -.
DR EnsemblBacteria; AAT48204; AAT48204; b3747.
DR EnsemblBacteria; BAE77541; BAE77541; BAE77541.
DR GeneID; 948255; -.
DR KEGG; ecj:JW5609; -.
DR KEGG; eco:b3747; -.
DR PATRIC; fig|1411691.4.peg.2953; -.
DR EchoBASE; EB1503; -.
DR eggNOG; COG3158; Bacteria.
DR HOGENOM; CLU_008142_4_2_6; -.
DR InParanoid; P63183; -.
DR OMA; AADQFEI; -.
DR PhylomeDB; P63183; -.
DR BioCyc; EcoCyc:KUP-MON; -.
DR BioCyc; MetaCyc:KUP-MON; -.
DR PRO; PR:P63183; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; ISM:EcoCyc.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0015079; F:potassium ion transmembrane transporter activity; IDA:EcoCyc.
DR GO; GO:0015387; F:potassium:proton symporter activity; IDA:EcoCyc.
DR GO; GO:0071278; P:cellular response to cesium ion; IDA:EcoCyc.
DR GO; GO:0071805; P:potassium ion transmembrane transport; IDA:EcoCyc.
DR GO; GO:0006813; P:potassium ion transport; IBA:GO_Central.
DR HAMAP; MF_01522; Kup; 1.
DR InterPro; IPR003855; K+_transporter.
DR InterPro; IPR023051; K+_uptake_low_affin.
DR PANTHER; PTHR30540; PTHR30540; 1.
DR Pfam; PF02705; K_trans; 1.
DR TIGRFAMs; TIGR00794; kup; 1.
PE 3: Inferred from homology;
KW Cell inner membrane; Cell membrane; Ion transport; Membrane; Potassium;
KW Potassium transport; Reference proteome; Symport; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..622
FT /note="Low affinity potassium transport system protein kup"
FT /id="PRO_0000209011"
FT TOPO_DOM 1..8
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 9..29
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 30..48
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 49..69
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 70..102
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 103..123
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 124..136
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 137..157
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 158..164
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 165..185
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 186..212
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 213..233
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 234..246
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 247..267
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 268..275
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 276..296
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 297..336
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 337..357
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 358..362
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 363..383
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 384..395
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 396..416
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 417..418
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 419..439
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 440..622
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
SQ SEQUENCE 622 AA; 69294 MW; E556791ABF9B8D25 CRC64;
MSTDNKQSLP AITLAAIGVV YGDIGTSPLY TLRECLSGQF GFGVERDAVF GFLSLIFWLL
IFVVSIKYLT FVMRADNAGE GGILTLMSLA GRNTSARTTS MLVIMGLIGG SFFYGEVVIT
PAISVMSAIE GLEIVAPQLD TWIVPLSIIV LTLLFMIQKH GTAMVGKLFA PIMLTWFLIL
AGLGLRSIIA NPEVLHALNP MWAVHFFLEY KTVSFIALGA VVLSITGVEA LYADMGHFGK
FPIRLAWFTV VLPSLTLNYF GQGALLLKNP EAIKNPFFLL APDWALIPLL IIAALATVIA
SQAVISGVFS LTRQAVRLGY LSPMRIIHTS EMESGQIYIP FVNWMLYVAV VIVIVSFEHS
SNLAAAYGIA VTGTMVLTSI LSTTVARQNW HWNKYFVALI LIAFLCVDIP LFTANLDKLL
SGGWLPLSLG TVMFIVMTTW KSERFRLLRR MHEHGNSLEA MIASLEKSPP VRVPGTAVYM
SRAINVIPFA LMHNLKHNKV LHERVILLTL RTEDAPYVHN VRRVQIEQLS PTFWRVVASY
GWRETPNVEE VFHRCGLEGL SCRMMETSFF MSHESLILGK RPWYLRLRGK LYLLLQRNAL
RAPDQFEIPP NRVIELGTQV EI
