TRMJ_PSEAB
ID TRMJ_PSEAB Reviewed; 257 AA.
AC A0A0H2ZF87;
DT 12-SEP-2018, integrated into UniProtKB/Swiss-Prot.
DT 16-SEP-2015, sequence version 1.
DT 03-AUG-2022, entry version 27.
DE RecName: Full=tRNA (cytidine/uridine/adenosine-2'-O-)-methyltransferase TrmJ {ECO:0000305};
DE EC=2.1.1.- {ECO:0000269|PubMed:27683218};
DE EC=2.1.1.200 {ECO:0000269|PubMed:27683218};
DE AltName: Full=tRNA (cytidine(32)/uridine(32)/adenosine(32)-2'-O)-methyltransferase {ECO:0000303|PubMed:27683218};
DE AltName: Full=tRNA Cm32/Um32/Am32 methyltransferase {ECO:0000303|PubMed:27683218};
GN Name=trmJ {ECO:0000303|PubMed:27683218};
GN OrderedLocusNames=PA14_14690 {ECO:0000312|EMBL:ABJ13078.1};
OS Pseudomonas aeruginosa (strain UCBPP-PA14).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208963;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UCBPP-PA14;
RX PubMed=17038190; DOI=10.1186/gb-2006-7-10-r90;
RA Lee D.G., Urbach J.M., Wu G., Liberati N.T., Feinbaum R.L., Miyata S.,
RA Diggins L.T., He J., Saucier M., Deziel E., Friedman L., Li L., Grills G.,
RA Montgomery K., Kucherlapati R., Rahme L.G., Ausubel F.M.;
RT "Genomic analysis reveals that Pseudomonas aeruginosa virulence is
RT combinatorial.";
RL Genome Biol. 7:R90.1-R90.14(2006).
RN [2] {ECO:0007744|PDB:5GM8, ECO:0007744|PDB:5GMB, ECO:0007744|PDB:5GMC}
RP X-RAY CRYSTALLOGRAPHY (1.62 ANGSTROMS) OF 1-167 IN COMPLEX WITH SINEFUNGIN,
RP FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, AND DISRUPTION PHENOTYPE.
RC STRAIN=UCBPP-PA14;
RX PubMed=27683218; DOI=10.1093/nar/gkw870;
RA Jaroensuk J., Atichartpongkul S., Chionh Y.H., Wong Y.H., Liew C.W.,
RA McBee M.E., Thongdee N., Prestwich E.G., DeMott M.S., Mongkolsuk S.,
RA Dedon P.C., Lescar J., Fuangthong M.;
RT "Methylation at position 32 of tRNA catalyzed by TrmJ alters oxidative
RT stress response in Pseudomonas aeruginosa.";
RL Nucleic Acids Res. 44:10834-10848(2016).
CC -!- FUNCTION: Catalyzes the formation of 2'O-methylated cytidine (Cm32),
CC 2'O-methylated uridine (Um32) or 2'O-methylated adenosine (Am32) at
CC position 32 in tRNA. Confers resistance to oxidative stress.
CC {ECO:0000269|PubMed:27683218}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=cytidine(32) in tRNA + S-adenosyl-L-methionine = 2'-O-
CC methylcytidine(32) in tRNA + H(+) + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:42932, Rhea:RHEA-COMP:10288, Rhea:RHEA-COMP:10289,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:74495, ChEBI:CHEBI:82748; EC=2.1.1.200;
CC Evidence={ECO:0000269|PubMed:27683218};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-adenosyl-L-methionine + uridine(32) in tRNA = 2'-O-
CC methyluridine(32) in tRNA + H(+) + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:42936, Rhea:RHEA-COMP:10107, Rhea:RHEA-COMP:10290,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:65315, ChEBI:CHEBI:74478; EC=2.1.1.200;
CC Evidence={ECO:0000269|PubMed:27683218};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=adenosine(32) in tRNA + S-adenosyl-L-methionine = 2'-O-
CC methyladenosine(32) in tRNA + H(+) + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:56884, Rhea:RHEA-COMP:14778, Rhea:RHEA-COMP:14779,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:74411, ChEBI:CHEBI:74477;
CC Evidence={ECO:0000269|PubMed:27683218};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:27683218}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- DISRUPTION PHENOTYPE: Inactivation of the gene abolishes Cm, Um and Am
CC formation in tRNA. Mutant has increased sensitivity to hydrogen
CC peroxide (H(2)O(2)), with reduced expression of oxyR-recG, katB-ankB,
CC and katE. {ECO:0000269|PubMed:27683218}.
CC -!- SIMILARITY: Belongs to the class IV-like SAM-binding methyltransferase
CC superfamily. RNA methyltransferase TrmH family. {ECO:0000305}.
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DR EMBL; CP000438; ABJ13078.1; -; Genomic_DNA.
DR RefSeq; WP_003092842.1; NZ_CP034244.1.
DR PDB; 5GM8; X-ray; 2.20 A; A/B/C/D=1-167.
DR PDB; 5GMB; X-ray; 1.62 A; A=1-167.
DR PDB; 5GMC; X-ray; 1.70 A; A/B/C/D=1-167.
DR PDBsum; 5GM8; -.
DR PDBsum; 5GMB; -.
DR PDBsum; 5GMC; -.
DR AlphaFoldDB; A0A0H2ZF87; -.
DR SMR; A0A0H2ZF87; -.
DR EnsemblBacteria; ABJ13078; ABJ13078; PA14_14690.
DR KEGG; pau:PA14_14690; -.
DR HOGENOM; CLU_056931_0_1_6; -.
DR OMA; PIMNLSH; -.
DR BioCyc; PAER208963:G1G74-1205-MON; -.
DR BRENDA; 2.1.1.200; 5087.
DR Proteomes; UP000000653; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0008173; F:RNA methyltransferase activity; IEA:InterPro.
DR GO; GO:0008033; P:tRNA processing; IEA:UniProtKB-KW.
DR Gene3D; 3.40.1280.10; -; 1.
DR InterPro; IPR029028; Alpha/beta_knot_MTases.
DR InterPro; IPR004384; RNA_MeTrfase_TrmJ/LasT.
DR InterPro; IPR001537; SpoU_MeTrfase.
DR InterPro; IPR029026; tRNA_m1G_MTases_N.
DR PANTHER; PTHR42786; PTHR42786; 1.
DR Pfam; PF00588; SpoU_methylase; 1.
DR PIRSF; PIRSF004808; LasT; 1.
DR SUPFAM; SSF75217; SSF75217; 1.
DR TIGRFAMs; TIGR00050; rRNA_methyl_1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Methyltransferase; S-adenosyl-L-methionine;
KW Transferase; tRNA processing.
FT CHAIN 1..257
FT /note="tRNA (cytidine/uridine/adenosine-2'-O-)-
FT methyltransferase TrmJ"
FT /id="PRO_0000445018"
FT BINDING 79..82
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000305|PubMed:27683218"
FT BINDING 115..117
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000305|PubMed:27683218"
FT BINDING 135
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000305|PubMed:27683218"
FT BINDING 142..144
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000305|PubMed:27683218"
SQ SEQUENCE 257 AA; 28486 MW; 3360B51B30E39A9B CRC64;
MLDRIRVVLV NTSHPGNIGG AARAMKNMGL SQLVLVQPES FPHGDAVARA SGATDILDAA
RVVDTLEEAL SGCSVVLGTS ARDRRIPWPL LDPRECATTC LEHLEANGEV ALVFGREYAG
LTNEELQRCQ FHVHIPSDPE FGSLNLAAAV QVLTYEVRMA WLAAQGKPTK MEKFESTSML
NTELVTADEL ELYYAHLERT LIDIGFLDPE KPRHLMSRLR RLYGRSAISK LEMNILRGIL
TETQKVARGL SYKRSDD
