TRMO_ECOLI
ID TRMO_ECOLI Reviewed; 235 AA.
AC P28634; Q47676;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 2.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=tRNA (adenine(37)-N6)-methyltransferase {ECO:0000305};
DE EC=2.1.1.- {ECO:0000269|PubMed:25063302};
DE AltName: Full=tRNA (m6t6A37) methyltransferase {ECO:0000303|PubMed:9537379};
DE AltName: Full=tRNA methyltransferase O {ECO:0000303|PubMed:25063302};
GN Name=trmO {ECO:0000303|PubMed:25063302};
GN Synonyms=tsaA {ECO:0000303|PubMed:9537379}, yaeB;
GN OrderedLocusNames=b0195, JW0191;
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;
RA Miyamoto K.;
RL Submitted (APR-1993) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=1459951; DOI=10.1128/jb.174.24.8016-8022.1992;
RA Gervais F.G., Drapeau G.R.;
RT "Identification, cloning, and characterization of rcsF, a new regulator
RT gene for exopolysaccharide synthesis that suppresses the division mutation
RT ftsZ84 in Escherichia coli K-12.";
RL J. Bacteriol. 174:8016-8022(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RA Takemoto K., Mori H., Murayama N., Kataoka K., Yano M., Itoh T.,
RA Yamamoto Y., Inokuchi H., Miki T., Hatada E., Fukuda R., Ichihara S.,
RA Mizuno T., Makino K., Nakata A., Yura T., Sampei G., Mizobuchi K.;
RT "Systematic sequencing of the Escherichia coli genome: analysis of the 4.0
RT - 6.0 min (189,987 - 281,416bp) region.";
RL Submitted (FEB-1996) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RA Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M.,
RA Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D.,
RA Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.;
RT "Sequence of minutes 4-25 of Escherichia coli.";
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN [5]
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 [6]
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 [7]
RP PROBABLE FUNCTION.
RC STRAIN=K12;
RX PubMed=9537379; DOI=10.1128/jb.180.7.1808-1813.1998;
RA Qian Q., Curran J.F., Bjork G.R.;
RT "The methyl group of the N6-methyl-N6-threonylcarbamoyladenosine in tRNA of
RT Escherichia coli modestly improves the efficiency of the tRNA.";
RL J. Bacteriol. 180:1808-1813(1998).
RN [8]
RP FUNCTION, CATALYTIC ACTIVITY, TRNA-BINDING, AND MUTAGENESIS OF ARG-92;
RP LYS-136; ASP-194 AND ARG-196.
RX PubMed=25063302; DOI=10.1093/nar/gku618;
RA Kimura S., Miyauchi K., Ikeuchi Y., Thiaville P.C., Crecy-Lagard V.D.,
RA Suzuki T.;
RT "Discovery of the beta-barrel-type RNA methyltransferase responsible for
RT N6-methylation of N6-threonylcarbamoyladenosine in tRNAs.";
RL Nucleic Acids Res. 42:9350-9365(2014).
CC -!- FUNCTION: S-adenosyl-L-methionine-dependent methyltransferase
CC responsible for the addition of the methyl group in the formation of
CC N6-methyl-N6-threonylcarbamoyladenosine at position 37 (m(6)t(6)A37) of
CC the tRNA anticodon loop of tRNA(Thr)(GGU) that read codons starting
CC with adenosine (PubMed:9537379, PubMed:25063302). The methyl group of
CC m(6)t(6)A37 appears to slightly improve the efficiency of the tRNA
CC decoding ability (PubMed:9537379, PubMed:25063302).
CC {ECO:0000269|PubMed:25063302, ECO:0000269|PubMed:9537379}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N(6)-L-threonylcarbamoyladenosine(37) in tRNA + S-adenosyl-L-
CC methionine = H(+) + N(6)-methyl,N(6)-L-threonylcarbamoyladenosine(37)
CC in tRNA + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:70027, Rhea:RHEA-
CC COMP:10163, Rhea:RHEA-COMP:17808, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:74418,
CC ChEBI:CHEBI:188470; Evidence={ECO:0000269|PubMed:25063302};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70028;
CC Evidence={ECO:0000269|PubMed:25063302};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P44740}.
CC -!- SIMILARITY: Belongs to the tRNA methyltransferase O family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA24509.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; D15061; BAA03655.1; -; Genomic_DNA.
DR EMBL; L04474; AAA24509.1; ALT_FRAME; Genomic_DNA.
DR EMBL; U70214; AAB08623.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73306.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA77871.1; -; Genomic_DNA.
DR PIR; C47040; C47040.
DR PIR; C64744; C64744.
DR RefSeq; NP_414737.1; NC_000913.3.
DR RefSeq; WP_000094011.1; NZ_STEB01000032.1.
DR AlphaFoldDB; P28634; -.
DR SMR; P28634; -.
DR BioGRID; 4259756; 15.
DR BioGRID; 853352; 1.
DR DIP; DIP-11195N; -.
DR IntAct; P28634; 6.
DR STRING; 511145.b0195; -.
DR jPOST; P28634; -.
DR PaxDb; P28634; -.
DR PRIDE; P28634; -.
DR EnsemblBacteria; AAC73306; AAC73306; b0195.
DR EnsemblBacteria; BAA77871; BAA77871; BAA77871.
DR GeneID; 66671515; -.
DR GeneID; 949112; -.
DR KEGG; ecj:JW0191; -.
DR KEGG; eco:b0195; -.
DR PATRIC; fig|1411691.4.peg.2083; -.
DR EchoBASE; EB1466; -.
DR eggNOG; COG1720; Bacteria.
DR HOGENOM; CLU_013458_3_0_6; -.
DR InParanoid; P28634; -.
DR OMA; CFKEKFA; -.
DR PhylomeDB; P28634; -.
DR BioCyc; EcoCyc:EG11503-MON; -.
DR BioCyc; MetaCyc:EG11503-MON; -.
DR PRO; PR:P28634; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0000049; F:tRNA binding; IDA:UniProtKB.
DR GO; GO:0089715; F:tRNA m6t6A37 methyltransferase activity; IDA:EcoCyc.
DR GO; GO:0030488; P:tRNA methylation; IMP:EcoCyc.
DR CDD; cd09281; UPF0066; 1.
DR Gene3D; 2.40.30.70; -; 1.
DR InterPro; IPR023370; TrmO-like_N.
DR InterPro; IPR041369; TrmO_C.
DR InterPro; IPR023368; UPF0066_cons_site.
DR InterPro; IPR040372; YaeB-like.
DR InterPro; IPR036413; YaeB-like_sf.
DR InterPro; IPR036414; YaeB_N_sf.
DR PANTHER; PTHR12818; PTHR12818; 1.
DR Pfam; PF01980; TrmO; 1.
DR Pfam; PF18389; TrmO_C; 1.
DR SUPFAM; SSF118196; SSF118196; 1.
DR TIGRFAMs; TIGR00104; tRNA_TsaA; 1.
DR PROSITE; PS01318; TSAA_1; 1.
DR PROSITE; PS51668; TSAA_2; 1.
PE 1: Evidence at protein level;
KW Methyltransferase; Reference proteome; RNA-binding;
KW S-adenosyl-L-methionine; Transferase; tRNA processing.
FT CHAIN 1..235
FT /note="tRNA (adenine(37)-N6)-methyltransferase"
FT /id="PRO_0000155617"
FT DOMAIN 6..147
FT /note="TsaA-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01003"
FT BINDING 23..25
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:O29998"
FT BINDING 64..65
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:O29998"
FT BINDING 92
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:O29998"
FT BINDING 127..130
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:O29998"
FT MUTAGEN 92
FT /note="R->A: Inhibits tRNA m(6)t(6)A37 formation."
FT /evidence="ECO:0000269|PubMed:25063302"
FT MUTAGEN 136
FT /note="K->A: Inhibits tRNA m(6)t(6)A37 formation."
FT /evidence="ECO:0000269|PubMed:25063302"
FT MUTAGEN 194
FT /note="D->A: Inhibits tRNA m(6)t(6)A37 formation; when
FT associated with A-196."
FT /evidence="ECO:0000269|PubMed:25063302"
FT MUTAGEN 196
FT /note="R->A: Inhibits tRNA m(6)t(6)A37 formation; when
FT associated with A-194."
FT /evidence="ECO:0000269|PubMed:25063302"
SQ SEQUENCE 235 AA; 26362 MW; B19F8D50DECCB572 CRC64;
MSSFQFEQIG VIRSPYKEKF AVPRQPGLVK SANGELHLIA PYNQADAVRG LEAFSHLWIL
FVFHQTMEGG WRPTVRPPRL GGNARMGVFA TRSTFRPNPI GMSLVELKEV VCHKDSVILK
LGSLDLVDGT PVVDIKPYLP FAESLPDASA SYAQSAPAAE MAVSFTAEVE KQLLTLEKRY
PQLTLFIREV LAQDPRPAYR KGEETGKTYA VWLHDFNVRW RVTDAGFEVF ALEPR
