(data stored in SCRATCH zone)

SWISSPROT: 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   11-DEC-2019, entry version 131.
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}.
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   SMR; P54462; -.
DR   STRING; 224308.BSU25430; -.
DR   PaxDb; P54462; -.
DR   PRIDE; P54462; -.
DR   EnsemblBacteria; CAB14485; CAB14485; BSU25430.
DR   GeneID; 937857; -.
DR   KEGG; bsu:BSU25430; -.
DR   PATRIC; fig|224308.179.peg.2764; -.
DR   eggNOG; ENOG4105CIW; Bacteria.
DR   eggNOG; COG0621; LUCA.
DR   HOGENOM; HOG000224765; -.
DR   InParanoid; P54462; -.
DR   KO; K18707; -.
DR   OMA; HFHIPLQ; -.
DR   PhylomeDB; P54462; -.
DR   BioCyc; BSUB:BSU25430-MONOMER; -.
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; SFLDF00295; threonylcarbamoyladenosine_tRN; 1.
DR   SFLD; SFLDS00029; Radical_SAM; 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; PS50926; TRAM; 1.
PE   1: Evidence at protein level;
DR   PRODOM; P54462.
DR   SWISS-2DPAGE; P54462.
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          372..437
FT                   /note="TRAM"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00208"
FT   METAL           11
FT                   /note="Iron-sulfur (4Fe-4S)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00780"
FT   METAL           47
FT                   /note="Iron-sulfur (4Fe-4S)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00780"
FT   METAL           78
FT                   /note="Iron-sulfur (4Fe-4S)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00780"
FT   METAL           153
FT                   /note="Iron-sulfur (4Fe-4S-S-AdoMet)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00780"
FT   METAL           157
FT                   /note="Iron-sulfur (4Fe-4S-S-AdoMet)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00780"
FT   METAL           160
FT                   /note="Iron-sulfur (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
//

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