TEHB_HAEIN
ID TEHB_HAEIN Reviewed; 286 AA.
AC P45134;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 115.
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=HI_1275;
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 INDUCTION.
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=16855256; DOI=10.1128/jb.00417-06;
RA Whitby P.W., Vanwagoner T.M., Seale T.W., Morton D.J., Stull T.L.;
RT "Transcriptional profile of Haemophilus influenzae: effects of iron and
RT heme.";
RL J. Bacteriol. 188:5640-5645(2006).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS).
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RA Chen Y.-H., Hendrickson W.A.;
RT "Crystal structure of TehB from Haemophilus influenzae.";
RL Submitted (MAY-2010) to the PDB data bank.
CC -!- FUNCTION: Probable S-adenosyl-L-methionine-dependent methyltransferase.
CC Plays a role in both resistance to oxidative damage and heme
CC uptake/utilization. Also protects H.influenzae from tellurite exposure
CC in vitro; however, since H.influenzae grows only in humans, it is
CC unlikely to encounter tellurite in its natural environment, and it is
CC thus probable that tellurite resistance does not represent a
CC biologically relevant role of TehB (By similarity). {ECO:0000250}.
CC -!- INDUCTION: Transcription is significantly up-regulated during growth in
CC iron/heme-restricted conditions. {ECO:0000269|PubMed:16855256}.
CC -!- SIMILARITY: Belongs to the TehB family. {ECO:0000305}.
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DR EMBL; L42023; AAC22923.1; -; Genomic_DNA.
DR PIR; H64113; H64113.
DR RefSeq; NP_439428.1; NC_000907.1.
DR RefSeq; WP_005694518.1; NC_000907.1.
DR PDB; 3M70; X-ray; 1.95 A; A=1-286.
DR PDBsum; 3M70; -.
DR AlphaFoldDB; P45134; -.
DR SMR; P45134; -.
DR STRING; 71421.HI_1275; -.
DR EnsemblBacteria; AAC22923; AAC22923; HI_1275.
DR KEGG; hin:HI_1275; -.
DR PATRIC; fig|71421.8.peg.1326; -.
DR eggNOG; COG0500; Bacteria.
DR eggNOG; COG3615; Bacteria.
DR HOGENOM; CLU_084458_0_0_6; -.
DR OMA; VFMFLNR; -.
DR PhylomeDB; P45134; -.
DR BioCyc; HINF71421:G1GJ1-1300-MON; -.
DR EvolutionaryTrace; P45134; -.
DR Proteomes; UP000000579; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0008168; F:methyltransferase activity; IBA:GO_Central.
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 1: Evidence at protein level;
KW 3D-structure; Methyltransferase; Reference proteome;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..286
FT /note="Probable S-adenosyl-L-methionine-dependent
FT methyltransferase TehB"
FT /id="PRO_0000072482"
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"
FT TURN 2..4
FT /evidence="ECO:0007829|PDB:3M70"
FT STRAND 5..10
FT /evidence="ECO:0007829|PDB:3M70"
FT TURN 16..18
FT /evidence="ECO:0007829|PDB:3M70"
FT HELIX 21..24
FT /evidence="ECO:0007829|PDB:3M70"
FT STRAND 25..27
FT /evidence="ECO:0007829|PDB:3M70"
FT STRAND 34..42
FT /evidence="ECO:0007829|PDB:3M70"
FT STRAND 44..49
FT /evidence="ECO:0007829|PDB:3M70"
FT STRAND 55..61
FT /evidence="ECO:0007829|PDB:3M70"
FT STRAND 76..82
FT /evidence="ECO:0007829|PDB:3M70"
FT STRAND 86..94
FT /evidence="ECO:0007829|PDB:3M70"
FT HELIX 95..97
FT /evidence="ECO:0007829|PDB:3M70"
FT HELIX 98..103
FT /evidence="ECO:0007829|PDB:3M70"
FT HELIX 110..118
FT /evidence="ECO:0007829|PDB:3M70"
FT STRAND 123..128
FT /evidence="ECO:0007829|PDB:3M70"
FT HELIX 133..140
FT /evidence="ECO:0007829|PDB:3M70"
FT STRAND 144..150
FT /evidence="ECO:0007829|PDB:3M70"
FT HELIX 152..164
FT /evidence="ECO:0007829|PDB:3M70"
FT STRAND 169..173
FT /evidence="ECO:0007829|PDB:3M70"
FT HELIX 176..178
FT /evidence="ECO:0007829|PDB:3M70"
FT STRAND 185..190
FT /evidence="ECO:0007829|PDB:3M70"
FT HELIX 194..196
FT /evidence="ECO:0007829|PDB:3M70"
FT HELIX 199..201
FT /evidence="ECO:0007829|PDB:3M70"
FT HELIX 202..211
FT /evidence="ECO:0007829|PDB:3M70"
FT STRAND 213..225
FT /evidence="ECO:0007829|PDB:3M70"
FT STRAND 228..230
FT /evidence="ECO:0007829|PDB:3M70"
FT HELIX 244..248
FT /evidence="ECO:0007829|PDB:3M70"
FT TURN 249..251
FT /evidence="ECO:0007829|PDB:3M70"
FT STRAND 252..258
FT /evidence="ECO:0007829|PDB:3M70"
FT STRAND 261..267
FT /evidence="ECO:0007829|PDB:3M70"
FT STRAND 273..284
FT /evidence="ECO:0007829|PDB:3M70"
SQ SEQUENCE 286 AA; 33020 MW; 69D7647E97CC74FA CRC64;
MKNELICYKQ MPVWTKDNLP QMFQEKHNTK VGTWGKLTVL KGKLKFYELT ENGDVIAEHI
FTPESHIPFV EPQAWHRVEA LSDDLECTLG FYCKKEDYFS KKYNTTAIHG DVVDAAKIIS
PCKVLDLGCG QGRNSLYLSL LGYDVTSWDH NENSIAFLNE TKEKENLNIS TALYDINAAN
IQENYDFIVS TVVFMFLNRE RVPSIIKNMK EHTNVGGYNL IVAAMSTDDV PCPLPFSFTF
AENELKEYYK DWEFLEYNEN MGELHKTDEN GNRIKMKFAT MLARKK
