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Protein

Tellurite methyltransferase

Gene

tehB

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

S-adenosyl-L-methionine dependent methyltransferase that catalyzes the methylation of tellurite and is responsible for tellurite resistance when present in high copy number. Can also methylate selenite and selenium dioxide. Is thus able to detoxify different chalcogens. Cannot methylate arsenic compounds.2 Publications

Catalytic activityi

S-adenosyl-L-methionine + tellurite = S-adenosyl-L-homocysteine + methanetelluronate.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei38S-adenosyl-L-methionine; via carbonyl oxygen1
Binding sitei43S-adenosyl-L-methionine1
Binding sitei59S-adenosyl-L-methionine1
Binding sitei102S-adenosyl-L-methionine1
Binding sitei177SubstrateCurated1

GO - Molecular functioni

  • S-adenosylmethionine-dependent methyltransferase activity Source: EcoCyc

GO - Biological processi

  • response to antibiotic Source: UniProtKB-KW
  • response to tellurium ion Source: EcoCyc
  • response to toxic substance Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Methyltransferase, Transferase

Keywords - Biological processi

Antibiotic resistance, Detoxification, Tellurium resistance

Keywords - Ligandi

S-adenosyl-L-methionine

Enzyme and pathway databases

BioCyciEcoCyc:EG11884-MONOMER.
ECOL316407:JW1426-MONOMER.
MetaCyc:EG11884-MONOMER.
BRENDAi2.1.1.265. 2026.

Names & Taxonomyi

Protein namesi
Recommended name:
Tellurite methyltransferase (EC:2.1.1.265)
Alternative name(s):
Chalcogen-detoxifying protein TehB
Selenite methyltransferase
Tellurite resistance protein TehB
Gene namesi
Name:tehB
Ordered Locus Names:b1430, JW1426
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG11884. tehB.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: EcoCyc
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi36D → A or N: Loss of tellurite resistance. 1 Publication1
Mutagenesisi59D → A: Loss of tellurite resistance. 1 Publication1
Mutagenesisi96Y → A: Decrease in tellurite resistance. 1 Publication1
Mutagenesisi97D → E: No effect on tellurite resistance. 1 Publication1
Mutagenesisi97D → N: Decrease in tellurite resistance. 1 Publication1
Mutagenesisi98F → A or Y: Loss of tellurite resistance. 1 Publication1
Mutagenesisi176H → A: 95% of wild-type methyltransferase activity on tellurite. 1 Publication1
Mutagenesisi177R → A: 35% of wild-type methyltransferase activity on tellurite. 1 Publication1
Mutagenesisi184R → A: 74% of wild-type methyltransferase activity on tellurite. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000724811 – 197Tellurite methyltransferaseAdd BLAST197

Proteomic databases

PaxDbiP25397.
PRIDEiP25397.

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

BioGridi4259401. 4 interactors.
DIPiDIP-10978N.
IntActiP25397. 7 interactors.
MINTiMINT-1274665.
STRINGi511145.b1430.

Structurei

Secondary structure

1197
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi8 – 13Combined sources6
Helixi20 – 25Combined sources6
Turni26 – 28Combined sources3
Beta strandi33 – 38Combined sources6
Helixi43 – 50Combined sources8
Beta strandi54 – 60Combined sources7
Helixi62 – 75Combined sources14
Beta strandi80 – 84Combined sources5
Helixi87 – 89Combined sources3
Beta strandi96 – 103Combined sources8
Helixi105 – 107Combined sources3
Helixi110 – 112Combined sources3
Helixi113 – 122Combined sources10
Beta strandi124 – 136Combined sources13
Beta strandi139 – 141Combined sources3
Helixi155 – 159Combined sources5
Turni160 – 162Combined sources3
Beta strandi163 – 169Combined sources7
Beta strandi172 – 178Combined sources7
Beta strandi184 – 195Combined sources12

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2XVAX-ray1.90A/B/C/D1-197[»]
2XVMX-ray1.48A/B1-197[»]
ProteinModelPortaliP25397.
SMRiP25397.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP25397.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni86 – 87S-adenosyl-L-methionine2

Sequence similaritiesi

Belongs to the TehB family.Curated

Phylogenomic databases

eggNOGiENOG41088CC. Bacteria.
COG0500. LUCA.
HOGENOMiHOG000120596.
InParanoidiP25397.
KOiK16868.
OMAiWDKNPMS.
PhylomeDBiP25397.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
InterProiIPR029063. SAM-dependent_MTases.
IPR015985. TehB-like_dom.
IPR004537. Tellurite-R_MeTrfase_TehB.
[Graphical view]
PfamiPF03848. TehB. 1 hit.
[Graphical view]
SUPFAMiSSF53335. SSF53335. 1 hit.
TIGRFAMsiTIGR00477. tehB. 1 hit.

Sequencei

Sequence statusi: Complete.

P25397-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MIIRDENYFT DKYELTRTHS EVLEAVKVVK PGKTLDLGCG NGRNSLYLAA
60 70 80 90 100
NGYDVDAWDK NAMSIANVER IKSIENLDNL HTRVVDLNNL TFDRQYDFIL
110 120 130 140 150
STVVLMFLEA KTIPGLIANM QRCTKPGGYN LIVAAMDTAD YPCTVGFPFA
160 170 180 190
FKEGELRRYY EGWERVKYNE DVGELHRTDA NGNRIKLRFA TMLARKK
Length:197
Mass (Da):22,531
Last modified:May 1, 1992 - v1
Checksum:iBF0D2D64F9B9C2E8
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M74072 Unassigned DNA. Translation: AAA19564.1.
U00096 Genomic DNA. Translation: AAC74512.1.
AP009048 Genomic DNA. Translation: BAA15059.1.
PIRiA64895.
RefSeqiNP_415947.1. NC_000913.3.
WP_000586732.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC74512; AAC74512; b1430.
BAA15059; BAA15059; BAA15059.
GeneIDi945979.
KEGGiecj:JW1426.
eco:b1430.
PATRICi32118144. VBIEscCol129921_1492.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M74072 Unassigned DNA. Translation: AAA19564.1.
U00096 Genomic DNA. Translation: AAC74512.1.
AP009048 Genomic DNA. Translation: BAA15059.1.
PIRiA64895.
RefSeqiNP_415947.1. NC_000913.3.
WP_000586732.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2XVAX-ray1.90A/B/C/D1-197[»]
2XVMX-ray1.48A/B1-197[»]
ProteinModelPortaliP25397.
SMRiP25397.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4259401. 4 interactors.
DIPiDIP-10978N.
IntActiP25397. 7 interactors.
MINTiMINT-1274665.
STRINGi511145.b1430.

Proteomic databases

PaxDbiP25397.
PRIDEiP25397.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC74512; AAC74512; b1430.
BAA15059; BAA15059; BAA15059.
GeneIDi945979.
KEGGiecj:JW1426.
eco:b1430.
PATRICi32118144. VBIEscCol129921_1492.

Organism-specific databases

EcoGeneiEG11884. tehB.

Phylogenomic databases

eggNOGiENOG41088CC. Bacteria.
COG0500. LUCA.
HOGENOMiHOG000120596.
InParanoidiP25397.
KOiK16868.
OMAiWDKNPMS.
PhylomeDBiP25397.

Enzyme and pathway databases

BioCyciEcoCyc:EG11884-MONOMER.
ECOL316407:JW1426-MONOMER.
MetaCyc:EG11884-MONOMER.
BRENDAi2.1.1.265. 2026.

Miscellaneous databases

EvolutionaryTraceiP25397.
PROiP25397.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
InterProiIPR029063. SAM-dependent_MTases.
IPR015985. TehB-like_dom.
IPR004537. Tellurite-R_MeTrfase_TehB.
[Graphical view]
PfamiPF03848. TehB. 1 hit.
[Graphical view]
SUPFAMiSSF53335. SSF53335. 1 hit.
TIGRFAMsiTIGR00477. tehB. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiTEHB_ECOLI
AccessioniPrimary (citable) accession number: P25397
Secondary accession number(s): P76866
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: May 1, 1992
Last modified: November 2, 2016
This is version 128 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Caution

Was originally thought to be plasmid encoded.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.