MTAB_BACSU
ID MTAB_BACSU Reviewed; 451 AA.
AC P54462;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Threonylcarbamoyladenosine tRNA methylthiotransferase MtaB;
DE EC=2.8.4.5 {ECO:0000269|PubMed:20584901};
DE AltName: Full=tRNA-t(6)A37 methylthiotransferase;
GN Name=mtaB; Synonyms=tmtB, yqeV; OrderedLocusNames=BSU25430;
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 [GENOMIC DNA].
RC STRAIN=168 / JH642;
RX PubMed=9023197; DOI=10.1128/jb.179.4.1153-1164.1997;
RA Homuth G., Masuda S., Mogk A., Kobayashi Y., Schumann W.;
RT "The dnaK operon of Bacillus subtilis is heptacistronic.";
RL J. Bacteriol. 179:1153-1164(1997).
RN [3]
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 [4]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBCELLULAR LOCATION, AND GENE
RP NAME.
RX PubMed=20584901; DOI=10.1074/jbc.m110.106831;
RA Arragain S., Handelman S.K., Forouhar F., Wei F.Y., Tomizawa K., Hunt J.F.,
RA Douki T., Fontecave M., Mulliez E., Atta M.;
RT "Identification of eukaryotic and prokaryotic methylthiotransferase for
RT biosynthesis of 2-methylthio-N6-threonylcarbamoyladenosine in tRNA.";
RL J. Biol. Chem. 285:28425-28433(2010).
RN [5]
RP FUNCTION AS A METHYLTHIOTRANSFERASE, AND GENE NAME.
RC STRAIN=168;
RX PubMed=20472640; DOI=10.1093/nar/gkq364;
RA Anton B.P., Russell S.P., Vertrees J., Kasif S., Raleigh E.A.,
RA Limbach P.A., Roberts R.J.;
RT "Functional characterization of the YmcB and YqeV tRNA
RT methylthiotransferases of Bacillus subtilis.";
RL Nucleic Acids Res. 38:6195-6205(2010).
CC -!- FUNCTION: Catalyzes the methylthiolation of N6-
CC threonylcarbamoyladenosine (t(6)A), leading to the formation of 2-
CC methylthio-N6-threonylcarbamoyladenosine (ms(2)t(6)A) at position 37 in
CC tRNAs that read codons beginning with adenine.
CC {ECO:0000269|PubMed:20472640, ECO:0000269|PubMed:20584901}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[sulfur carrier]-SH + AH2 + N(6)-L-
CC threonylcarbamoyladenosine(37) in tRNA + 2 S-adenosyl-L-methionine =
CC 2-methylsulfanyl-N(6)-L-threonylcarbamoyladenosine(37) in tRNA + 5'-
CC deoxyadenosine + [sulfur carrier]-H + A + 2 H(+) + L-methionine + S-
CC adenosyl-L-homocysteine; Xref=Rhea:RHEA:37075, Rhea:RHEA-COMP:10163,
CC Rhea:RHEA-COMP:11092, Rhea:RHEA-COMP:14737, Rhea:RHEA-COMP:14739,
CC ChEBI:CHEBI:13193, ChEBI:CHEBI:15378, ChEBI:CHEBI:17319,
CC ChEBI:CHEBI:17499, ChEBI:CHEBI:29917, ChEBI:CHEBI:57844,
CC ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:64428,
CC ChEBI:CHEBI:74418, ChEBI:CHEBI:74420; EC=2.8.4.5;
CC Evidence={ECO:0000269|PubMed:20584901};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000305|PubMed:20584901};
CC Note=Binds 2 [4Fe-4S] clusters. One cluster is coordinated with 3
CC cysteines and an exchangeable S-adenosyl-L-methionine.
CC {ECO:0000305|PubMed:20584901};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|PROSITE-ProRule:PRU00780,
CC ECO:0000269|PubMed:20584901}.
CC -!- SIMILARITY: Belongs to the methylthiotransferase family. MtaB
CC subfamily. {ECO:0000305}.
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DR EMBL; D84432; BAA12468.1; -; Genomic_DNA.
DR EMBL; D83717; BAA12080.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB14485.1; -; Genomic_DNA.
DR PIR; E69952; E69952.
DR RefSeq; NP_390421.1; NC_000964.3.
DR RefSeq; WP_003230017.1; NZ_JNCM01000036.1.
DR AlphaFoldDB; P54462; -.
DR SMR; P54462; -.
DR STRING; 224308.BSU25430; -.
DR PaxDb; P54462; -.
DR PRIDE; P54462; -.
DR EnsemblBacteria; CAB14485; CAB14485; BSU_25430.
DR GeneID; 937857; -.
DR KEGG; bsu:BSU25430; -.
DR PATRIC; fig|224308.179.peg.2764; -.
DR eggNOG; COG0621; Bacteria.
DR InParanoid; P54462; -.
DR OMA; HFHIPLQ; -.
DR PhylomeDB; P54462; -.
DR BioCyc; BSUB:BSU25430-MON; -.
DR BRENDA; 2.8.4.5; 658.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0035598; F:N6-threonylcarbomyladenosine methylthiotransferase activity; IMP:UniProtKB.
DR GO; GO:0061712; F:tRNA (N(6)-L-threonylcarbamoyladenosine(37)-C(2))-methylthiotransferase; IEA:UniProtKB-EC.
DR GO; GO:0035600; P:tRNA methylthiolation; IMP:UniProtKB.
DR Gene3D; 3.40.50.12160; -; 1.
DR Gene3D; 3.80.30.20; -; 1.
DR InterPro; IPR006638; Elp3/MiaB/NifB.
DR InterPro; IPR005839; Methylthiotransferase.
DR InterPro; IPR020612; Methylthiotransferase_CS.
DR InterPro; IPR013848; Methylthiotransferase_N.
DR InterPro; IPR038135; Methylthiotransferase_N_sf.
DR InterPro; IPR006467; MiaB-like_C.
DR InterPro; IPR007197; rSAM.
DR InterPro; IPR023404; rSAM_horseshoe.
DR InterPro; IPR034557; ThrcA_tRNA_MEthiotransferase.
DR InterPro; IPR002792; TRAM_dom.
DR Pfam; PF04055; Radical_SAM; 1.
DR Pfam; PF01938; TRAM; 1.
DR Pfam; PF00919; UPF0004; 1.
DR SFLD; SFLDS00029; Radical_SAM; 1.
DR SFLD; SFLDF00295; threonylcarbamoyladenosine_tRN; 1.
DR SMART; SM00729; Elp3; 1.
DR TIGRFAMs; TIGR01579; MiaB-like-C; 1.
DR TIGRFAMs; TIGR00089; TIGR00089; 1.
DR PROSITE; PS51449; MTTASE_N; 1.
DR PROSITE; PS01278; MTTASE_RADICAL; 1.
DR PROSITE; PS51918; RADICAL_SAM; 1.
DR PROSITE; PS50926; TRAM; 1.
PE 1: Evidence at protein level;
KW 4Fe-4S; Cytoplasm; Iron; Iron-sulfur; Metal-binding; Reference proteome;
KW S-adenosyl-L-methionine; Transferase; tRNA processing.
FT CHAIN 1..451
FT /note="Threonylcarbamoyladenosine tRNA
FT methylthiotransferase MtaB"
FT /id="PRO_0000141729"
FT DOMAIN 2..114
FT /note="MTTase N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00780"
FT DOMAIN 139..369
FT /note="Radical SAM core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01266"
FT DOMAIN 372..437
FT /note="TRAM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00208"
FT BINDING 11
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00780"
FT BINDING 47
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00780"
FT BINDING 78
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00780"
FT BINDING 153
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00780"
FT BINDING 157
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00780"
FT BINDING 160
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00780"
SQ SEQUENCE 451 AA; 51658 MW; 9FD45437F5CE3552 CRC64;
MATVAFHTLG CKVNHYETEA IWQLFKEAGY ERRDFEQTAD VYVINTCTVT NTGDKKSRQV
IRRAIRQNPD GVICVTGCYA QTSPAEIMAI PGVDIVVGTQ DREKMLGYID QYREERQPIN
GVSNIMKARV YEELDVPAFT DRTRASLKIQ EGCNNFCTFC IIPWARGLLR SRDPEEVIKQ
AQQLVDAGYK EIVLTGIHTG GYGEDMKDYN FAKLLSELDT RVEGVKRIRI SSIEASQITD
EVIEVLDRSD KIVNHLHIPI QSGSNTVLKR MRRKYTMEFF ADRLNKLKKA LPGLAVTSDV
IVGFPGETEE EFMETYNFIK EHKFSELHVF PYSKRTGTPA ARMEDQVDEN VKNERVHRLI
ALSDQLAKEY ASQYENEVLE IIPEEAFKET EEENMFVGYT DNYMKVVFKG TEDMIGKIVK
VKILKAGYPY NEGQFVRVVE DEITEHMRLS S
