TEHA_HAEIN
ID TEHA_HAEIN Reviewed; 328 AA.
AC P44741;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Tellurite resistance protein TehA homolog;
GN Name=tehA; OrderedLocusNames=HI_0511;
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 X-RAY CRYSTALLOGRAPHY (1.15 ANGSTROMS) OF 15-328, SUBUNIT, SUBCELLULAR
RP LOCATION, TRANSMEMBRANE TOPOLOGY, AND MUTAGENESIS OF GLY-29 AND PHE-276.
RX PubMed=20981093; DOI=10.1038/nature09487;
RA Chen Y.H., Hu L., Punta M., Bruni R., Hillerich B., Kloss B., Rost B.,
RA Love J., Siegelbaum S.A., Hendrickson W.A.;
RT "Homologue structure of the SLAC1 anion channel for closing stomata in
RT leaves.";
RL Nature 467:1074-1080(2010).
CC -!- FUNCTION: Ion channel involved in potassium tellurite resistance.
CC {ECO:0000305}.
CC -!- SUBUNIT: Homotrimer. Each subunit forms a channel.
CC {ECO:0000269|PubMed:20981093}.
CC -!- INTERACTION:
CC P44741; P44741: tehA; NbExp=4; IntAct=EBI-15888134, EBI-15888134;
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Multi-pass
CC membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the tellurite-resistance/dicarboxylate
CC transporter (TDT) family. {ECO:0000305}.
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DR EMBL; L42023; AAC22169.1; -; Genomic_DNA.
DR PIR; D64073; D64073.
DR RefSeq; NP_438669.1; NC_000907.1.
DR PDB; 3M71; X-ray; 1.20 A; A=15-328.
DR PDB; 3M72; X-ray; 1.70 A; A=15-328.
DR PDB; 3M73; X-ray; 1.15 A; A=15-328.
DR PDB; 3M74; X-ray; 1.65 A; A=15-328.
DR PDB; 3M75; X-ray; 1.60 A; A=15-328.
DR PDB; 3M76; X-ray; 1.50 A; A=15-328.
DR PDB; 3M77; X-ray; 1.50 A; A=15-328.
DR PDB; 3M78; X-ray; 2.60 A; A=15-328.
DR PDB; 3M7B; X-ray; 1.50 A; A=15-328.
DR PDB; 3M7C; X-ray; 1.70 A; A=15-328.
DR PDB; 3M7E; X-ray; 1.80 A; A=15-328.
DR PDB; 3M7L; X-ray; 1.50 A; A=15-328.
DR PDB; 4YCR; X-ray; 2.30 A; A=22-320.
DR PDBsum; 3M71; -.
DR PDBsum; 3M72; -.
DR PDBsum; 3M73; -.
DR PDBsum; 3M74; -.
DR PDBsum; 3M75; -.
DR PDBsum; 3M76; -.
DR PDBsum; 3M77; -.
DR PDBsum; 3M78; -.
DR PDBsum; 3M7B; -.
DR PDBsum; 3M7C; -.
DR PDBsum; 3M7E; -.
DR PDBsum; 3M7L; -.
DR PDBsum; 4YCR; -.
DR AlphaFoldDB; P44741; -.
DR SMR; P44741; -.
DR DIP; DIP-59222N; -.
DR STRING; 71421.HI_0511; -.
DR TCDB; 2.A.16.1.2; the telurite-resistance/dicarboxylate transporter (tdt) family.
DR DNASU; 950588; -.
DR EnsemblBacteria; AAC22169; AAC22169; HI_0511.
DR KEGG; hin:HI_0511; -.
DR PATRIC; fig|71421.8.peg.530; -.
DR eggNOG; COG1275; Bacteria.
DR HOGENOM; CLU_044414_1_0_6; -.
DR OMA; EVRAEYH; -.
DR PhylomeDB; P44741; -.
DR BioCyc; HINF71421:G1GJ1-524-MON; -.
DR EvolutionaryTrace; P44741; -.
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:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0006811; P:ion transport; IEA:UniProtKB-KW.
DR GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR GO; GO:0046690; P:response to tellurium ion; IEA:UniProtKB-KW.
DR GO; GO:0055085; P:transmembrane transport; IEA:InterPro.
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 3D-structure; Antibiotic resistance; Cell inner membrane; Cell membrane;
KW Ion channel; Ion transport; Membrane; Reference proteome;
KW Tellurium resistance; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..328
FT /note="Tellurite resistance protein TehA homolog"
FT /id="PRO_0000072480"
FT TOPO_DOM 1..21
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 22..42
FT /note="Helical"
FT TOPO_DOM 43..49
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 50..73
FT /note="Helical"
FT TOPO_DOM 74..93
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 94..112
FT /note="Helical"
FT TOPO_DOM 113..115
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 116..141
FT /note="Helical"
FT TOPO_DOM 142..153
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 154..174
FT /note="Helical"
FT TOPO_DOM 175..176
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 177..204
FT /note="Helical"
FT TOPO_DOM 205..208
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 209..232
FT /note="Helical"
FT TOPO_DOM 233..238
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 239..262
FT /note="Helical"
FT TOPO_DOM 263..268
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 269..289
FT /note="Helical"
FT TOPO_DOM 290..294
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 295..321
FT /note="Helical"
FT TOPO_DOM 322..328
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT SITE 276
FT /note="Important for gating; obstructs channel and prevents
FT ion flux in the closed conformation"
FT MUTAGEN 29
FT /note="G->D: Blocks channel. Abolishes ion flux; when
FT associated with A-276."
FT /evidence="ECO:0000269|PubMed:20981093"
FT MUTAGEN 276
FT /note="F->A,G: Constitutively open channel. Abolishes ion
FT flux; when associated with D-29."
FT /evidence="ECO:0000269|PubMed:20981093"
FT MUTAGEN 276
FT /note="F->L,V: No ion flux while channel is in closed
FT conformation."
FT /evidence="ECO:0000269|PubMed:20981093"
FT MUTAGEN 276
FT /note="F->T: Small constitutive ion flux."
FT /evidence="ECO:0000269|PubMed:20981093"
FT HELIX 25..28
FT /evidence="ECO:0007829|PDB:3M73"
FT HELIX 29..42
FT /evidence="ECO:0007829|PDB:3M73"
FT TURN 43..47
FT /evidence="ECO:0007829|PDB:3M73"
FT HELIX 51..79
FT /evidence="ECO:0007829|PDB:3M73"
FT HELIX 81..89
FT /evidence="ECO:0007829|PDB:3M73"
FT HELIX 93..98
FT /evidence="ECO:0007829|PDB:3M73"
FT HELIX 99..111
FT /evidence="ECO:0007829|PDB:3M73"
FT TURN 112..114
FT /evidence="ECO:0007829|PDB:3M73"
FT HELIX 116..137
FT /evidence="ECO:0007829|PDB:3M73"
FT HELIX 139..143
FT /evidence="ECO:0007829|PDB:3M73"
FT STRAND 145..147
FT /evidence="ECO:0007829|PDB:3M73"
FT HELIX 149..151
FT /evidence="ECO:0007829|PDB:3M73"
FT HELIX 154..156
FT /evidence="ECO:0007829|PDB:3M73"
FT HELIX 157..160
FT /evidence="ECO:0007829|PDB:3M73"
FT HELIX 162..173
FT /evidence="ECO:0007829|PDB:3M73"
FT HELIX 177..204
FT /evidence="ECO:0007829|PDB:3M73"
FT HELIX 209..212
FT /evidence="ECO:0007829|PDB:3M73"
FT HELIX 213..219
FT /evidence="ECO:0007829|PDB:3M73"
FT HELIX 220..232
FT /evidence="ECO:0007829|PDB:3M73"
FT TURN 233..235
FT /evidence="ECO:0007829|PDB:3M73"
FT HELIX 239..262
FT /evidence="ECO:0007829|PDB:3M73"
FT TURN 263..265
FT /evidence="ECO:0007829|PDB:3M73"
FT HELIX 269..274
FT /evidence="ECO:0007829|PDB:3M73"
FT HELIX 275..290
FT /evidence="ECO:0007829|PDB:3M73"
FT HELIX 295..321
FT /evidence="ECO:0007829|PDB:3M73"
SQ SEQUENCE 328 AA; 36934 MW; 8F5BA175AD817CE0 CRC64;
MLHFAHIFQN KVHTMNITKP FPLPTGYFGI PLGLAALSLA WFHLENLFPA ARMVSDVLGI
VASAVWILFI LMYAYKLRYY FEEVRAEYHS PVRFSFIALI PITTMLVGDI LYRWNPLIAE
VLIWIGTIGQ LLFSTLRVSE LWQGGVFEQK STHPSFYLPA VAANFTSASS LALLGYHDLG
YLFFGAGMIA WIIFEPVLLQ HLRISSLEPQ FRATMGIVLA PAFVCVSAYL SINHGEVDTL
AKILWGYGFL QLFFLLRLFP WIVEKGLNIG LWAFSFGLAS MANSATAFYH GNVLQGVSIF
AFVFSNVMIG LLVLMTIYKL TKGQFFLK
