TRMA_SALTY
ID TRMA_SALTY Reviewed; 366 AA.
AC P22038;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 13-DEC-2001, sequence version 2.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=tRNA/tmRNA (uracil-C(5))-methyltransferase {ECO:0000255|HAMAP-Rule:MF_01011};
DE EC=2.1.1.- {ECO:0000255|HAMAP-Rule:MF_01011};
DE EC=2.1.1.35 {ECO:0000255|HAMAP-Rule:MF_01011};
DE AltName: Full=tRNA (uracil(54)-C(5))-methyltransferase {ECO:0000255|HAMAP-Rule:MF_01011};
DE AltName: Full=tRNA(m5U54)-methyltransferase {ECO:0000255|HAMAP-Rule:MF_01011};
DE Short=RUMT {ECO:0000255|HAMAP-Rule:MF_01011};
DE AltName: Full=tmRNA (uracil(341)-C(5))-methyltransferase {ECO:0000255|HAMAP-Rule:MF_01011};
GN Name=trmA {ECO:0000255|HAMAP-Rule:MF_01011}; OrderedLocusNames=STM4129;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-101.
RX PubMed=1999392; DOI=10.1128/jb.173.5.1757-1764.1991;
RA Gustafsson C., Lindstroem P.H.R., Hagervall T.G., Esberg K.B., Bjoerk G.R.;
RT "The trmA promoter has regulatory features and sequence elements in common
RT with the rRNA P1 promoter family of Escherichia coli.";
RL J. Bacteriol. 173:1757-1764(1991).
CC -!- FUNCTION: Catalyzes the formation of 5-methyl-uridine at position 54
CC (m5U54) in all tRNAs.
CC -!- FUNCTION: Dual-specificity methyltransferase that catalyzes the
CC formation of 5-methyluridine at position 54 (m5U54) in all tRNAs, and
CC that of position 341 (m5U341) in tmRNA (transfer-mRNA).
CC {ECO:0000255|HAMAP-Rule:MF_01011}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-adenosyl-L-methionine + uridine(54) in tRNA = 5-
CC methyluridine(54) in tRNA + H(+) + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:42712, Rhea:RHEA-COMP:10167, Rhea:RHEA-COMP:10193,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:65315, ChEBI:CHEBI:74447; EC=2.1.1.35;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01011};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-adenosyl-L-methionine + uridine(341) in tmRNA = 5-
CC methyluridine(341) in tmRNA + H(+) + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:43612, Rhea:RHEA-COMP:10630, Rhea:RHEA-COMP:10631,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:65315, ChEBI:CHEBI:74447; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01011};
CC -!- INDUCTION: Growth rate-dependent regulation of transcription. Is a
CC novel example of a mRNA regulated through a mechanism similar to that
CC of a stable RNA (rRNA).
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. RNA M5U methyltransferase family. TrmA subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_01011}.
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DR EMBL; AE006468; AAL22967.1; -; Genomic_DNA.
DR EMBL; M57569; AAA27233.1; -; Genomic_DNA.
DR RefSeq; NP_463008.1; NC_003197.2.
DR RefSeq; WP_000186981.1; NC_003197.2.
DR AlphaFoldDB; P22038; -.
DR SMR; P22038; -.
DR STRING; 99287.STM4129; -.
DR PaxDb; P22038; -.
DR EnsemblBacteria; AAL22967; AAL22967; STM4129.
DR GeneID; 1255655; -.
DR KEGG; stm:STM4129; -.
DR PATRIC; fig|99287.12.peg.4350; -.
DR HOGENOM; CLU_043022_0_0_6; -.
DR OMA; DHMESGV; -.
DR PhylomeDB; P22038; -.
DR BioCyc; SENT99287:STM4129-MON; -.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0019843; F:rRNA binding; IBA:GO_Central.
DR GO; GO:0030697; F:S-adenosylmethionine-dependent tRNA (m5U54) methyltransferase activity; IBA:GO_Central.
DR GO; GO:0000049; F:tRNA binding; IBA:GO_Central.
DR Gene3D; 3.40.50.150; -; 1.
DR HAMAP; MF_01011; RNA_methyltr_TrmA; 1.
DR InterPro; IPR030390; MeTrfase_TrmA_AS.
DR InterPro; IPR030391; MeTrfase_TrmA_CS.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR011869; TrmA_MeTrfase.
DR InterPro; IPR010280; U5_MeTrfase_fam.
DR PANTHER; PTHR47790; PTHR47790; 1.
DR Pfam; PF05958; tRNA_U5-meth_tr; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR TIGRFAMs; TIGR02143; trmA_only; 1.
DR PROSITE; PS51687; SAM_MT_RNA_M5U; 1.
DR PROSITE; PS01230; TRMA_1; 1.
DR PROSITE; PS01231; TRMA_2; 1.
PE 2: Evidence at transcript level;
KW Methyltransferase; Reference proteome; S-adenosyl-L-methionine;
KW Transferase; tRNA processing.
FT CHAIN 1..366
FT /note="tRNA/tmRNA (uracil-C(5))-methyltransferase"
FT /id="PRO_0000161877"
FT ACT_SITE 324
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01011"
FT ACT_SITE 358
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01011"
FT BINDING 190
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01011"
FT BINDING 218
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01011"
FT BINDING 223
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01011"
FT BINDING 239
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01011"
FT BINDING 299
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01011"
FT CONFLICT 38..39
FT /note="RS -> QLM (in Ref. 2; AAA27233)"
FT /evidence="ECO:0000305"
FT CONFLICT 69..70
FT /note="KS -> FC (in Ref. 2; AAA27233)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 366 AA; 41896 MW; 27BC2A68075CCA31 CRC64;
MTPEHLPTEQ YEAQLAEKVA RLQSMMAPFS GLVPEVFRSP VSHYRMRAEF RLWHDGDDLY
HIMFDQQTKS RIRVDTFPAA SQLINTLMKA MIAGVRDNHA LRHKLFQIDY LTTLSNQAVV
SLLYHKKLDE EWREAATALR DALRAQGLNV HLIGRATKTK IELDQDYIDE RLPVAGKEMI
YRQVENSFTQ PNAAMNIQML EWALEVTKDS KGDLLELYCG NGNFSLALAR NFNRVLATEI
AKPSVAAAQY NIAANHIDNV QIIRMAAEEF TQAMNGVREF NRLQGIDLKR YQCETIFVDP
PRSGLDSETE KMVQAYPRIL YISCNPETLC KNLETLSQTH TVSRLALFDQ FPYTHHMECG
VLLTAR
