ID   TEHB_HAEI1              Reviewed;         286 AA.
AC   E1X791;
DT   06-FEB-2013, integrated into UniProtKB/Swiss-Prot.
DT   30-NOV-2010, sequence version 1.
DT   03-AUG-2022, entry version 50.
DE   RecName: Full=Probable S-adenosyl-L-methionine-dependent methyltransferase TehB;
DE            EC=2.1.1.-;
DE   AltName: Full=Tellurite resistance protein TehB homolog;
GN   Name=tehB; OrderedLocusNames=HIB_14270;
OS   Haemophilus influenzae (strain 10810).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=862964;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=10810;
RA   Crook D., Hood D., Moxon R., Bentley S.D., Aslett M., Parkhill J.;
RT   "The genome sequence of Haemophilus influenzae 10810.";
RL   Submitted (JUL-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   FUNCTION, INDUCTION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=10810;
RX   PubMed=20075041; DOI=10.1099/mic.0.036400-0;
RA   Whitby P.W., Seale T.W., Morton D.J., VanWagoner T.M., Stull T.L.;
RT   "Characterization of the Haemophilus influenzae tehB gene and its role in
RT   virulence.";
RL   Microbiology 156:1188-1200(2010).
CC   -!- FUNCTION: Probable S-adenosyl-L-methionine-dependent methyltransferase.
CC       Plays a role in both resistance to oxidative damage and heme
CC       uptake/utilization, and is important for virulence of this organism in
CC       an animal model of invasive disease. Also protects H.influenzae from
CC       tellurite exposure in vitro; however, since H.influenzae grows only in
CC       humans, it is unlikely to encounter tellurite in its natural
CC       environment, and it is thus probable that tellurite resistance does not
CC       represent a biologically relevant role of TehB.
CC       {ECO:0000269|PubMed:20075041}.
CC   -!- INDUCTION: Transcription of tehB is independent of both tellurite
CC       exposure and oxidative stress. {ECO:0000269|PubMed:20075041}.
CC   -!- DISRUPTION PHENOTYPE: Deletion of tehB leads to an increase in
CC       sensitivity both to tellurite and to the oxidizing agents cumene
CC       hydroperoxide, tert-butyl hydroperoxide and hydrogen peroxide. The tehB
CC       mutant additionally shows a significantly reduced ability to utilize
CC       free heme as well as several heme-containing moieties including heme-
CC       human serum albumin, hemoglobin and hemoglobin-haptoglobin, to support
CC       aerobic growth. Virulence of the mutant strain is reduced compared to
CC       the wild-type strain in the infant rat. {ECO:0000269|PubMed:20075041}.
CC   -!- SIMILARITY: Belongs to the TehB family. {ECO:0000305}.
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DR   EMBL; FQ312006; CBW29614.1; -; Genomic_DNA.
DR   RefSeq; WP_015702159.1; NC_016809.1.
DR   AlphaFoldDB; E1X791; -.
DR   SMR; E1X791; -.
DR   KEGG; hiu:HIB_14270; -.
DR   PATRIC; fig|862964.3.peg.1480; -.
DR   HOGENOM; CLU_084458_0_0_6; -.
DR   OMA; VFMFLNR; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IEA:InterPro.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   GO; GO:0046690; P:response to tellurium ion; IEA:InterPro.
DR   Gene3D; 2.60.120.10; -; 1.
DR   Gene3D; 3.40.50.150; -; 1.
DR   InterPro; IPR015392; DUF1971.
DR   InterPro; IPR014710; RmlC-like_jellyroll.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR015985; TehB-like_dom.
DR   InterPro; IPR004537; Tellurite-R_MeTrfase_TehB.
DR   InterPro; IPR014431; Tellurite-R_TehB-2.
DR   Pfam; PF09313; DUF1971; 1.
DR   Pfam; PF03848; TehB; 1.
DR   PIRSF; PIRSF005215; TehB; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   TIGRFAMs; TIGR00477; tehB; 1.
PE   2: Evidence at transcript level;
KW   Methyltransferase; S-adenosyl-L-methionine; Transferase; Virulence.
FT   CHAIN           1..286
FT                   /note="Probable S-adenosyl-L-methionine-dependent
FT                   methyltransferase TehB"
FT                   /id="PRO_0000421105"
FT   BINDING         128
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         133
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         149
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         175..176
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         191
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   286 AA;  33050 MW;  DFC140B068C6F7CD CRC64;
     MKNELICYKQ MPVWTKDKLP QMFQEKHNTK VGTWGKLTVL KGKIKFYELT ENGDVVAEHI
     FTPESHIPFV EPQAWHRVEA LSDDLECTLG FYCKKEDYFS KKYNMTAIHG DVVDAAKIIS
     PCKVLDLGCG QGRNSLYLSL LGYDVTSWDH NENSIAFLNE TKEKENLNIS TALYDINAAN
     IQENYDFIVS TVVFMFLNRE RVPSIIKNMQ EHTNVGGYNL IVAAMSTDDV PCPLPFSFTF
     AENELKEYYK DWEFLEYNEN MGELHKTDEN GNRIKMKFAT MLARKK