TRMB_BACSU
ID TRMB_BACSU Reviewed; 213 AA.
AC O34522;
DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=tRNA (guanine-N(7)-)-methyltransferase {ECO:0000255|HAMAP-Rule:MF_01057};
DE EC=2.1.1.33 {ECO:0000255|HAMAP-Rule:MF_01057, ECO:0000269|PubMed:16600901};
DE AltName: Full=BsTrmB {ECO:0000303|PubMed:16600901};
DE AltName: Full=tRNA (guanine(46)-N(7))-methyltransferase {ECO:0000255|HAMAP-Rule:MF_01057};
DE AltName: Full=tRNA(m7G46)-methyltransferase {ECO:0000255|HAMAP-Rule:MF_01057, ECO:0000303|PubMed:16600901};
GN Name=trmB {ECO:0000255|HAMAP-Rule:MF_01057, ECO:0000303|PubMed:16600901};
GN Synonyms=ytmQ; OrderedLocusNames=BSU29900;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9387221; DOI=10.1099/00221287-143-11-3431;
RA Lapidus A., Galleron N., Sorokin A., Ehrlich S.D.;
RT "Sequencing and functional annotation of the Bacillus subtilis genes in the
RT 200 kb rrnB-dnaB region.";
RL Microbiology 143:3431-3441(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS), FUNCTION, CATALYTIC ACTIVITY,
RP PATHWAY, AND SUBUNIT.
RC STRAIN=168;
RX PubMed=16600901; DOI=10.1093/nar/gkl116;
RA Zegers I., Gigot D., van Vliet F., Tricot C., Aymerich S., Bujnicki J.M.,
RA Kosinski J., Droogmans L.;
RT "Crystal structure of Bacillus subtilis TrmB, the tRNA (m7G46)
RT methyltransferase.";
RL Nucleic Acids Res. 34:1925-1934(2006).
CC -!- FUNCTION: Catalyzes the formation of N(7)-methylguanine at position 46
CC (m7G46) in tRNA. {ECO:0000255|HAMAP-Rule:MF_01057,
CC ECO:0000269|PubMed:16600901}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=guanosine(46) in tRNA + S-adenosyl-L-methionine = N(7)-
CC methylguanosine(46) in tRNA + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:42708, Rhea:RHEA-COMP:10188, Rhea:RHEA-COMP:10189,
CC ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:74269,
CC ChEBI:CHEBI:74480; EC=2.1.1.33; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01057, ECO:0000269|PubMed:16600901};
CC -!- PATHWAY: tRNA modification; N(7)-methylguanine-tRNA biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_01057, ECO:0000305|PubMed:16600901}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:16600901}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. TrmB family. {ECO:0000255|HAMAP-Rule:MF_01057,
CC ECO:0000305}.
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DR EMBL; AF008220; AAC00285.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB14968.1; -; Genomic_DNA.
DR PIR; B69997; B69997.
DR RefSeq; NP_390868.1; NC_000964.3.
DR RefSeq; WP_004398646.1; NZ_JNCM01000036.1.
DR PDB; 2FCA; X-ray; 2.10 A; A/B=1-213.
DR PDB; 7NYB; X-ray; 2.50 A; A/B=1-213.
DR PDB; 7NZI; X-ray; 3.10 A; A/B=1-213.
DR PDB; 7NZJ; X-ray; 1.98 A; A/B/C/D/E/F=1-213.
DR PDBsum; 2FCA; -.
DR PDBsum; 7NYB; -.
DR PDBsum; 7NZI; -.
DR PDBsum; 7NZJ; -.
DR AlphaFoldDB; O34522; -.
DR SMR; O34522; -.
DR STRING; 224308.BSU29900; -.
DR PaxDb; O34522; -.
DR EnsemblBacteria; CAB14968; CAB14968; BSU_29900.
DR GeneID; 936447; -.
DR KEGG; bsu:BSU29900; -.
DR PATRIC; fig|224308.179.peg.3248; -.
DR eggNOG; COG0220; Bacteria.
DR InParanoid; O34522; -.
DR OMA; WRGAKTA; -.
DR PhylomeDB; O34522; -.
DR BioCyc; BSUB:BSU29900-MON; -.
DR BRENDA; 2.1.1.33; 658.
DR UniPathway; UPA00989; -.
DR EvolutionaryTrace; O34522; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0043527; C:tRNA methyltransferase complex; IBA:GO_Central.
DR GO; GO:0008176; F:tRNA (guanine-N7-)-methyltransferase activity; IBA:GO_Central.
DR GO; GO:0036265; P:RNA (guanine-N7)-methylation; IBA:GO_Central.
DR GO; GO:0030488; P:tRNA methylation; IBA:GO_Central.
DR Gene3D; 3.40.50.150; -; 1.
DR HAMAP; MF_01057; tRNA_methyltr_TrmB; 1.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR003358; tRNA_(Gua-N-7)_MeTrfase_Trmb.
DR PANTHER; PTHR23417; PTHR23417; 1.
DR Pfam; PF02390; Methyltransf_4; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR TIGRFAMs; TIGR00091; TIGR00091; 1.
DR PROSITE; PS51625; SAM_MT_TRMB; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Methyltransferase; Reference proteome;
KW S-adenosyl-L-methionine; Transferase; tRNA processing.
FT CHAIN 1..213
FT /note="tRNA (guanine-N(7)-)-methyltransferase"
FT /id="PRO_0000171295"
FT REGION 124..129
FT /note="Interaction with RNA"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01057"
FT ACT_SITE 118
FT /evidence="ECO:0000250|UniProtKB:Q12009"
FT BINDING 44
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01057"
FT BINDING 69
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01057"
FT BINDING 96
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01057"
FT BINDING 118
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01057"
FT BINDING 122
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01057"
FT BINDING 154
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01057"
FT BINDING 191..194
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01057"
FT HELIX 9..15
FT /evidence="ECO:0007829|PDB:7NZJ"
FT TURN 16..19
FT /evidence="ECO:0007829|PDB:7NZJ"
FT HELIX 24..27
FT /evidence="ECO:0007829|PDB:7NZJ"
FT HELIX 31..35
FT /evidence="ECO:0007829|PDB:7NZJ"
FT STRAND 41..45
FT /evidence="ECO:0007829|PDB:7NZJ"
FT STRAND 48..50
FT /evidence="ECO:0007829|PDB:7NZI"
FT HELIX 51..59
FT /evidence="ECO:0007829|PDB:7NZJ"
FT STRAND 63..68
FT /evidence="ECO:0007829|PDB:7NZJ"
FT HELIX 72..85
FT /evidence="ECO:0007829|PDB:7NZJ"
FT STRAND 88..93
FT /evidence="ECO:0007829|PDB:7NZJ"
FT HELIX 97..99
FT /evidence="ECO:0007829|PDB:7NZJ"
FT HELIX 100..103
FT /evidence="ECO:0007829|PDB:7NZJ"
FT STRAND 111..116
FT /evidence="ECO:0007829|PDB:7NZJ"
FT HELIX 123..128
FT /evidence="ECO:0007829|PDB:7NZJ"
FT HELIX 133..143
FT /evidence="ECO:0007829|PDB:7NZJ"
FT STRAND 148..154
FT /evidence="ECO:0007829|PDB:7NZJ"
FT HELIX 156..169
FT /evidence="ECO:0007829|PDB:7NZJ"
FT STRAND 172..179
FT /evidence="ECO:0007829|PDB:7NZJ"
FT HELIX 180..182
FT /evidence="ECO:0007829|PDB:7NZJ"
FT HELIX 192..195
FT /evidence="ECO:0007829|PDB:7NZJ"
FT TURN 196..200
FT /evidence="ECO:0007829|PDB:7NZJ"
FT STRAND 205..210
FT /evidence="ECO:0007829|PDB:7NZJ"
SQ SEQUENCE 213 AA; 24504 MW; 28C34F163EB2DD69 CRC64;
MRMRHKPWAD DFLAENADIA ISNPADYKGK WNTVFGNDNP IHIEVGTGKG QFISGMAKQN
PDINYIGIEL FKSVIVTAVQ KVKDSEAQNV KLLNIDADTL TDVFEPGEVK RVYLNFSDPW
PKKRHEKRRL TYSHFLKKYE EVMGKGGSIH FKTDNRGLFE YSLKSFSEYG LLLTYVSLDL
HNSNLEGNIM TEYEEKFSAL GQPIYRAEVE WRT
