TRMK_BACSU
ID TRMK_BACSU Reviewed; 238 AA.
AC P54471;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 03-MAY-2011, sequence version 2.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=tRNA (adenine(22)-N(1))-methyltransferase;
DE EC=2.1.1.217;
DE AltName: Full=TrMet(m1A22);
DE AltName: Full=tRNA(m1A22)-methyltransferase;
DE Short=tRNA(m1A22)MTase;
GN Name=trmK; Synonyms=yqfN; OrderedLocusNames=BSU25180;
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 / JH642;
RX PubMed=8969508; DOI=10.1099/13500872-142-11-3103;
RA Mizuno M., Masuda S., Takemaru K., Hosono S., Sato T., Takeuchi M.,
RA Kobayashi Y.;
RT "Systematic sequencing of the 283 kb 210 degrees-232 degrees region of the
RT Bacillus subtilis genome containing the skin element and many sporulation
RT genes.";
RL Microbiology 142:3103-3111(1996).
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-70, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC STRAIN=168;
RX PubMed=17218307; DOI=10.1074/mcp.m600464-mcp200;
RA Macek B., Mijakovic I., Olsen J.V., Gnad F., Kumar C., Jensen P.R.,
RA Mann M.;
RT "The serine/threonine/tyrosine phosphoproteome of the model bacterium
RT Bacillus subtilis.";
RL Mol. Cell. Proteomics 6:697-707(2007).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, AND IDENTIFICATION OF START CODON.
RC STRAIN=168;
RX PubMed=18420655; DOI=10.1093/nar/gkn169;
RA Roovers M., Kaminska K.H., Tkaczuk K.L., Gigot D., Droogmans L.,
RA Bujnicki J.M.;
RT "The YqfN protein of Bacillus subtilis is the tRNA: m1A22 methyltransferase
RT (TrmK).";
RL Nucleic Acids Res. 36:3252-3262(2008).
CC -!- FUNCTION: Catalyzes the S-adenosyl-L-methionine-dependent formation of
CC N(1)-methyladenine at position 22 (m1A22) in tRNA.
CC {ECO:0000269|PubMed:18420655}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=adenosine(22) in tRNA + S-adenosyl-L-methionine = H(+) + N(1)-
CC methyladenosine(22) in tRNA + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:43144, Rhea:RHEA-COMP:10361, Rhea:RHEA-COMP:10362,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:74411, ChEBI:CHEBI:74491; EC=2.1.1.217;
CC Evidence={ECO:0000269|PubMed:18420655};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the TrmK family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA12491.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAB14448.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; D84432; BAA12491.1; ALT_INIT; Genomic_DNA.
DR EMBL; AL009126; CAB14448.1; ALT_INIT; Genomic_DNA.
DR PIR; H69953; H69953.
DR RefSeq; NP_390397.1; NC_000964.3.
DR RefSeq; WP_003246178.1; NC_000964.3.
DR PDB; 6Q56; X-ray; 2.00 A; A/B/C/D=1-238.
DR PDBsum; 6Q56; -.
DR AlphaFoldDB; P54471; -.
DR SMR; P54471; -.
DR STRING; 224308.BSU25180; -.
DR iPTMnet; P54471; -.
DR jPOST; P54471; -.
DR PaxDb; P54471; -.
DR PRIDE; P54471; -.
DR DNASU; 937898; -.
DR EnsemblBacteria; CAB14448; CAB14448; BSU_25180.
DR GeneID; 937898; -.
DR KEGG; bsu:BSU25180; -.
DR PATRIC; fig|224308.43.peg.2625; -.
DR eggNOG; COG2384; Bacteria.
DR InParanoid; P54471; -.
DR BioCyc; BSUB:BSU25180-MON; -.
DR BioCyc; MetaCyc:BSU25180-MON; -.
DR BRENDA; 2.1.1.217; 658.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016429; F:tRNA (adenine-N1-)-methyltransferase activity; IDA:UniProtKB.
DR GO; GO:0030488; P:tRNA methylation; IDA:UniProtKB.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR006901; TrmK.
DR Pfam; PF04816; TrmK; 1.
DR PIRSF; PIRSF018637; TrmK; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Methyltransferase; Phosphoprotein;
KW Reference proteome; S-adenosyl-L-methionine; Transferase; tRNA processing.
FT CHAIN 1..238
FT /note="tRNA (adenine(22)-N(1))-methyltransferase"
FT /id="PRO_0000049798"
FT MOD_RES 70
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17218307"
FT HELIX 8..14
FT /evidence="ECO:0007829|PDB:6Q56"
FT STRAND 21..26
FT /evidence="ECO:0007829|PDB:6Q56"
FT HELIX 32..39
FT /evidence="ECO:0007829|PDB:6Q56"
FT STRAND 42..52
FT /evidence="ECO:0007829|PDB:6Q56"
FT HELIX 53..65
FT /evidence="ECO:0007829|PDB:6Q56"
FT TURN 69..71
FT /evidence="ECO:0007829|PDB:6Q56"
FT STRAND 72..78
FT /evidence="ECO:0007829|PDB:6Q56"
FT HELIX 79..82
FT /evidence="ECO:0007829|PDB:6Q56"
FT STRAND 89..96
FT /evidence="ECO:0007829|PDB:6Q56"
FT HELIX 98..107
FT /evidence="ECO:0007829|PDB:6Q56"
FT HELIX 109..111
FT /evidence="ECO:0007829|PDB:6Q56"
FT STRAND 116..124
FT /evidence="ECO:0007829|PDB:6Q56"
FT HELIX 127..135
FT /evidence="ECO:0007829|PDB:6Q56"
FT STRAND 139..148
FT /evidence="ECO:0007829|PDB:6Q56"
FT STRAND 151..161
FT /evidence="ECO:0007829|PDB:6Q56"
FT HELIX 165..167
FT /evidence="ECO:0007829|PDB:6Q56"
FT HELIX 172..178
FT /evidence="ECO:0007829|PDB:6Q56"
FT HELIX 180..185
FT /evidence="ECO:0007829|PDB:6Q56"
FT HELIX 188..210
FT /evidence="ECO:0007829|PDB:6Q56"
FT HELIX 215..234
FT /evidence="ECO:0007829|PDB:6Q56"
SQ SEQUENCE 238 AA; 26162 MW; F59DA3FB5091C0C9 CRC64;
MNELKLSKRL QTVAEYIPNG AVMADIGSDH AYLPCYAVLN HKASGAIAGE ITDGPFLSAK
RQVEKSGLNS HISVRQGDGL EVIKKGEADA ITIAGMGGAL IAHILEAGKD KLTGKERLIL
QPNIHAVHIR EWLYKERYAL IDEVILEEDG KCYEVLVAEA GDRDAAYDGI SLSAGMLVGP
FLAKEKNAVF LKKWTQELQH TQSIYEQISQ AADTEQNKQK LKELADRMEL LKEVIDHG
