TEHA_ECOLI
ID TEHA_ECOLI Reviewed; 330 AA.
AC P25396; P76864;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1992, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Tellurite resistance protein TehA;
GN Name=tehA; OrderedLocusNames=b1429, JW1425;
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=2060788; DOI=10.1016/0378-1119(91)90217-y;
RA Walter E.G., Weiner J.H., Taylor D.E.;
RT "Nucleotide sequence and overexpression of the tellurite-resistance
RT determinant from the IncHII plasmid pHH1508a.";
RL Gene 101:1-7(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 GENE MAPPING.
RC STRAIN=K12;
RX PubMed=8169225; DOI=10.1128/jb.176.9.2740-2742.1994;
RA Taylor D.E., Hou Y., Turner R.J., Weiner J.H.;
RT "Location of a potassium tellurite resistance operon (tehA tehB) within the
RT terminus of Escherichia coli K-12.";
RL J. Bacteriol. 176:2740-2742(1994).
RN [6]
RP 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: Responsible for potassium tellurite resistance when present
CC in high copy number. Ion channel involved in potassium tellurite
CC resistance (By similarity). Otherwise, phenotypically silent.
CC {ECO:0000250}.
CC -!- SUBUNIT: Homotrimer. Each subunit forms a channel (By similarity).
CC {ECO:0000250}.
CC -!- INTERACTION:
CC P25396; P25396: tehA; NbExp=2; IntAct=EBI-15888098, EBI-15888098;
CC -!- SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein.
CC -!- SIMILARITY: Belongs to the tellurite-resistance/dicarboxylate
CC transporter (TDT) family. {ECO:0000305}.
CC -!- CAUTION: Was originally thought to be plasmid encoded.
CC {ECO:0000305|PubMed:2060788}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M74072; AAA19563.1; -; Unassigned_DNA.
DR EMBL; U00096; AAC74511.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA15058.1; -; Genomic_DNA.
DR PIR; H64894; H64894.
DR RefSeq; NP_415946.1; NC_000913.3.
DR RefSeq; WP_001301046.1; NZ_LN832404.1.
DR AlphaFoldDB; P25396; -.
DR SMR; P25396; -.
DR BioGRID; 4261847; 4.
DR DIP; DIP-10977N; -.
DR STRING; 511145.b1429; -.
DR TCDB; 2.A.16.1.1; the telurite-resistance/dicarboxylate transporter (tdt) family.
DR PaxDb; P25396; -.
DR PRIDE; P25396; -.
DR DNASU; 945852; -.
DR EnsemblBacteria; AAC74511; AAC74511; b1429.
DR EnsemblBacteria; BAA15058; BAA15058; BAA15058.
DR GeneID; 945852; -.
DR KEGG; ecj:JW1425; -.
DR KEGG; eco:b1429; -.
DR PATRIC; fig|1411691.4.peg.842; -.
DR EchoBASE; EB1829; -.
DR eggNOG; COG1275; Bacteria.
DR HOGENOM; CLU_044414_1_0_6; -.
DR InParanoid; P25396; -.
DR OMA; EVRAEYH; -.
DR PhylomeDB; P25396; -.
DR BioCyc; EcoCyc:TEHA-MON; -.
DR BioCyc; MetaCyc:TEHA-MON; -.
DR PRO; PR:P25396; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0046583; F:cation efflux transmembrane transporter activity; IDA:EcoCyc.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0006812; P:cation transport; IDA:EcoCyc.
DR GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR GO; GO:0046690; P:response to tellurium ion; IMP:EcoCyc.
DR GO; GO:0055085; P:transmembrane transport; IDA:EcoCyc.
DR CDD; cd09324; TDT_TehA; 1.
DR Gene3D; 1.50.10.150; -; 1.
DR InterPro; IPR004695; SLAC1/Mae1/Ssu1/TehA.
DR InterPro; IPR039264; TehA.
DR InterPro; IPR011552; TehA/Mae1.
DR InterPro; IPR038665; Voltage-dep_anion_channel_sf.
DR Pfam; PF03595; SLAC1; 1.
DR TIGRFAMs; TIGR00816; tdt; 1.
PE 1: Evidence at protein level;
KW Antibiotic resistance; Cell inner membrane; Cell membrane; Ion channel;
KW Ion transport; Membrane; Reference proteome; Tellurium resistance;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..330
FT /note="Tellurite resistance protein TehA"
FT /id="PRO_0000072479"
FT TOPO_DOM 1..7
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 8..28
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 29..35
FT /note="Periplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 36..59
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 60..79
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 80..98
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 99..101
FT /note="Periplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 102..127
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 128..138
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 139..159
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 160..161
FT /note="Periplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 162..189
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 190..194
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 195..218
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 219..224
FT /note="Periplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 225..248
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 249..254
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 255..275
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 276..283
FT /note="Periplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 284..310
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 311..330
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT SITE 262
FT /note="Important for gating; obstructs channel and prevents
FT ion flux in the closed conformation"
FT /evidence="ECO:0000250"
SQ SEQUENCE 330 AA; 35932 MW; BC592152A2D2FFF5 CRC64;
MQSDKVLNLP AGYFGIVLGT IGMGFAWRYA SQVWQVSHWL GDGLVILAMI IWGLLTSAFI
ARLIRFPHSV LAEVRHPVLS SFVSLFPATT MLVAIGFVPW FRPLAVCLFS FGVVVQLAYA
AWQTAGLWRG SHPEEATTPG LYLPTVANNF ISAMACGALG YTDAGLVFLG AGVFSWLSLE
PVILQRLRSS GELPTALRTS LGIQLAPALV ACSAWLSVNG GEGDTLAKML FGYGLLQLLF
MLRLMPWYLS QPFNASFWSF SFGVSALATT GLHLGSGSDN GFFHTLAVPL FIFTNFIIAI
LLIRTFALLM QGKLLVRTER AVLMKAEDKE
