TEHB_ECOLI
ID TEHB_ECOLI Reviewed; 197 AA.
AC P25397; P76866;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1992, sequence version 1.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Tellurite methyltransferase;
DE EC=2.1.1.265;
DE AltName: Full=Chalcogen-detoxifying protein TehB;
DE AltName: Full=Selenite methyltransferase;
DE AltName: Full=Tellurite resistance protein TehB;
GN Name=tehB; OrderedLocusNames=b1430, JW1426;
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 FUNCTION, SAM-BINDING, SUBUNIT, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP ASP-36; ASP-59; TYR-96; ASP-97 AND PHE-98.
RX PubMed=11053398; DOI=10.1128/jb.182.22.6509-6513.2000;
RA Liu M., Turner R.J., Winstone T.L., Saetre A., Dyllick-Brenzinger M.,
RA Jickling G., Tari L.W., Weiner J.H., Taylor D.E.;
RT "Escherichia coli TehB requires S-adenosylmethionine as a cofactor to
RT mediate tellurite resistance.";
RL J. Bacteriol. 182:6509-6513(2000).
RN [7]
RP CRYSTALLIZATION, AND SAM-BINDING.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=21045305; DOI=10.1107/s1744309110036043;
RA Choudhury H.G., Beis K.;
RT "Crystallization and initial X-ray diffraction analysis of the tellurite-
RT resistance S-adenosyl-L-methionine transferase protein TehB from
RT Escherichia coli.";
RL Acta Crystallogr. F 66:1496-1499(2010).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (1.48 ANGSTROMS) OF 3-197 IN COMPLEXES WITH
RP S-ADENOSYL-L-HOMOCYSTEINE AND A SAM ANALOG, FUNCTION, CATALYTIC ACTIVITY,
RP SUBSTRATE SPECIFICITY, MUTAGENESIS OF HIS-176; ARG-177 AND ARG-184, AND
RP REACTION MECHANISM.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=21244361; DOI=10.1042/bj20102014;
RA Choudhury H.G., Cameron A.D., Iwata S., Beis K.;
RT "Structure and mechanism of the chalcogen-detoxifying protein TehB from
RT Escherichia coli.";
RL Biochem. J. 435:85-91(2011).
CC -!- FUNCTION: S-adenosyl-L-methionine dependent methyltransferase that
CC catalyzes the methylation of tellurite and is responsible for tellurite
CC resistance when present in high copy number. Can also methylate
CC selenite and selenium dioxide. Is thus able to detoxify different
CC chalcogens. Cannot methylate arsenic compounds.
CC {ECO:0000269|PubMed:11053398, ECO:0000269|PubMed:21244361}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-adenosyl-L-methionine + tellurite = methanetellurite + S-
CC adenosyl-L-homocysteine; Xref=Rhea:RHEA:34539, ChEBI:CHEBI:30477,
CC ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:71624;
CC EC=2.1.1.265; Evidence={ECO:0000269|PubMed:21244361};
CC -!- SUBUNIT: Homodimer. {ECO:0000305|PubMed:11053398}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:11053398}.
CC Note=Probably a peripheral membrane protein that interacts with TehA.
CC -!- SIMILARITY: Belongs to the TehB family. {ECO:0000305}.
CC -!- CAUTION: Was originally thought to be plasmid encoded.
CC {ECO:0000305|PubMed:2060788}.
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DR EMBL; M74072; AAA19564.1; -; Unassigned_DNA.
DR EMBL; U00096; AAC74512.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA15059.1; -; Genomic_DNA.
DR PIR; A64895; A64895.
DR RefSeq; NP_415947.1; NC_000913.3.
DR RefSeq; WP_000586732.1; NZ_SSZK01000021.1.
DR PDB; 2XVA; X-ray; 1.90 A; A/B/C/D=1-197.
DR PDB; 2XVM; X-ray; 1.48 A; A/B=1-197.
DR PDBsum; 2XVA; -.
DR PDBsum; 2XVM; -.
DR AlphaFoldDB; P25397; -.
DR SMR; P25397; -.
DR BioGRID; 4259401; 6.
DR DIP; DIP-10978N; -.
DR IntAct; P25397; 7.
DR STRING; 511145.b1430; -.
DR jPOST; P25397; -.
DR PaxDb; P25397; -.
DR PRIDE; P25397; -.
DR EnsemblBacteria; AAC74512; AAC74512; b1430.
DR EnsemblBacteria; BAA15059; BAA15059; BAA15059.
DR GeneID; 945979; -.
DR KEGG; ecj:JW1426; -.
DR KEGG; eco:b1430; -.
DR PATRIC; fig|1411691.4.peg.841; -.
DR eggNOG; COG0500; Bacteria.
DR HOGENOM; CLU_056435_2_0_6; -.
DR InParanoid; P25397; -.
DR OMA; VFMFLNR; -.
DR PhylomeDB; P25397; -.
DR BioCyc; EcoCyc:EG11884-MON; -.
DR BioCyc; MetaCyc:EG11884-MON; -.
DR BRENDA; 2.1.1.265; 2026.
DR EvolutionaryTrace; P25397; -.
DR PRO; PR:P25397; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0008168; F:methyltransferase activity; IBA:GO_Central.
DR GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IDA:EcoCyc.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
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:0009636; P:response to toxic substance; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR015985; TehB-like_dom.
DR InterPro; IPR004537; Tellurite-R_MeTrfase_TehB.
DR Pfam; PF03848; TehB; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR TIGRFAMs; TIGR00477; tehB; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antibiotic resistance; Cytoplasm; Detoxification;
KW Methyltransferase; Reference proteome; S-adenosyl-L-methionine;
KW Tellurium resistance; Transferase.
FT CHAIN 1..197
FT /note="Tellurite methyltransferase"
FT /id="PRO_0000072481"
FT REGION 86..87
FT /note="S-adenosyl-L-methionine"
FT BINDING 38
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT BINDING 43
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT BINDING 59
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT BINDING 102
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT BINDING 177
FT /ligand="substrate"
FT /evidence="ECO:0000305"
FT MUTAGEN 36
FT /note="D->A,N: Loss of tellurite resistance."
FT /evidence="ECO:0000269|PubMed:11053398"
FT MUTAGEN 59
FT /note="D->A: Loss of tellurite resistance."
FT /evidence="ECO:0000269|PubMed:11053398"
FT MUTAGEN 96
FT /note="Y->A: Decrease in tellurite resistance."
FT /evidence="ECO:0000269|PubMed:11053398"
FT MUTAGEN 97
FT /note="D->E: No effect on tellurite resistance."
FT /evidence="ECO:0000269|PubMed:11053398"
FT MUTAGEN 97
FT /note="D->N: Decrease in tellurite resistance."
FT /evidence="ECO:0000269|PubMed:11053398"
FT MUTAGEN 98
FT /note="F->A,Y: Loss of tellurite resistance."
FT /evidence="ECO:0000269|PubMed:11053398"
FT MUTAGEN 176
FT /note="H->A: 95% of wild-type methyltransferase activity on
FT tellurite."
FT /evidence="ECO:0000269|PubMed:21244361"
FT MUTAGEN 177
FT /note="R->A: 35% of wild-type methyltransferase activity on
FT tellurite."
FT /evidence="ECO:0000269|PubMed:21244361"
FT MUTAGEN 184
FT /note="R->A: 74% of wild-type methyltransferase activity on
FT tellurite."
FT /evidence="ECO:0000269|PubMed:21244361"
FT HELIX 8..13
FT /evidence="ECO:0007829|PDB:2XVM"
FT HELIX 20..25
FT /evidence="ECO:0007829|PDB:2XVM"
FT TURN 26..28
FT /evidence="ECO:0007829|PDB:2XVM"
FT STRAND 33..38
FT /evidence="ECO:0007829|PDB:2XVM"
FT HELIX 43..50
FT /evidence="ECO:0007829|PDB:2XVM"
FT STRAND 54..60
FT /evidence="ECO:0007829|PDB:2XVM"
FT HELIX 62..75
FT /evidence="ECO:0007829|PDB:2XVM"
FT STRAND 80..84
FT /evidence="ECO:0007829|PDB:2XVM"
FT HELIX 87..89
FT /evidence="ECO:0007829|PDB:2XVM"
FT STRAND 96..103
FT /evidence="ECO:0007829|PDB:2XVM"
FT HELIX 105..107
FT /evidence="ECO:0007829|PDB:2XVM"
FT HELIX 110..112
FT /evidence="ECO:0007829|PDB:2XVM"
FT HELIX 113..122
FT /evidence="ECO:0007829|PDB:2XVM"
FT STRAND 124..136
FT /evidence="ECO:0007829|PDB:2XVM"
FT STRAND 139..141
FT /evidence="ECO:0007829|PDB:2XVM"
FT HELIX 155..159
FT /evidence="ECO:0007829|PDB:2XVM"
FT TURN 160..162
FT /evidence="ECO:0007829|PDB:2XVM"
FT STRAND 163..169
FT /evidence="ECO:0007829|PDB:2XVM"
FT STRAND 172..178
FT /evidence="ECO:0007829|PDB:2XVM"
FT STRAND 184..195
FT /evidence="ECO:0007829|PDB:2XVM"
SQ SEQUENCE 197 AA; 22531 MW; BF0D2D64F9B9C2E8 CRC64;
MIIRDENYFT DKYELTRTHS EVLEAVKVVK PGKTLDLGCG NGRNSLYLAA NGYDVDAWDK
NAMSIANVER IKSIENLDNL HTRVVDLNNL TFDRQYDFIL STVVLMFLEA KTIPGLIANM
QRCTKPGGYN LIVAAMDTAD YPCTVGFPFA FKEGELRRYY EGWERVKYNE DVGELHRTDA
NGNRIKLRFA TMLARKK
