ID   TSAB_BACSU              Reviewed;         229 AA.
AC   O05516; Q797D5;
DT   03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   03-AUG-2022, entry version 122.
DE   RecName: Full=tRNA threonylcarbamoyladenosine biosynthesis protein TsaB;
DE   AltName: Full=t(6)A37 threonylcarbamoyladenosine biosynthesis protein TsaB;
GN   Name=tsaB; Synonyms=ydiC; OrderedLocusNames=BSU05920;
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=9202461; DOI=10.1099/00221287-143-6-1861;
RA   Sadaie Y., Yata K., Fujita M., Sagai H., Itaya M., Kasahara Y.,
RA   Ogasawara N.;
RT   "Nucleotide sequence and analysis of the phoB-rrnE-groESL region of the
RT   Bacillus subtilis chromosome.";
RL   Microbiology 143:1861-1866(1997).
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   SUBUNIT.
RC   STRAIN=168;
RX   PubMed=21285948; DOI=10.1038/emboj.2010.363;
RA   El Yacoubi B., Hatin I., Deutsch C., Kahveci T., Rousset J.P.,
RA   Iwata-Reuyl D., Murzin A.G., de Crecy-Lagard V.;
RT   "A role for the universal Kae1/Qri7/YgjD (COG0533) family in tRNA
RT   modification.";
RL   EMBO J. 30:882-893(2011).
RN   [4]
RP   SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=168;
RX   PubMed=17005971; DOI=10.1099/mic.0.29152-0;
RA   Hunt A., Rawlins J.P., Thomaides H.B., Errington J.;
RT   "Functional analysis of 11 putative essential genes in Bacillus subtilis.";
RL   Microbiology 152:2895-2907(2006).
RN   [5]
RP   FUNCTION.
RC   STRAIN=168;
RX   PubMed=23072323; DOI=10.1021/bi301233d;
RA   Lauhon C.T.;
RT   "Mechanism of N6-threonylcarbamoyladenosine (t(6)A) biosynthesis: isolation
RT   and characterization of the intermediate threonylcarbamoyl-AMP.";
RL   Biochemistry 51:8950-8963(2012).
CC   -!- FUNCTION: Required for the formation of a threonylcarbamoyl group on
CC       adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning
CC       with adenine. Is involved in the transfer of the threonylcarbamoyl
CC       moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37,
CC       together with TsaD and TsaE; this reaction does not require ATP in
CC       vitro. TsaB seems to play an indirect role in the t(6)A biosynthesis
CC       pathway, possibly in regulating the core enzymatic function of TsaD.
CC       {ECO:0000269|PubMed:23072323}.
CC   -!- SUBUNIT: Forms a heterodimer with TsaE. {ECO:0000305|PubMed:21285948}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17005971}.
CC   -!- DISRUPTION PHENOTYPE: Cells lacking this gene display a slow growth
CC       phenotype. Cell size, shape and nucleoid morphology remain unchanged.
CC       {ECO:0000269|PubMed:17005971}.
CC   -!- MISCELLANEOUS: The four proteins YwlC, TsaD, TsaB and TsaE are
CC       necessary and sufficient for tRNA(NNU) t(6)A37
CC       threonylcarbamoyladenosine biosynthesis in vitro in B.subtilis.
CC       {ECO:0000305|PubMed:23072323}.
CC   -!- SIMILARITY: Belongs to the KAE1 / TsaD family. TsaB subfamily.
CC       {ECO:0000305}.
CC   -!- CAUTION: The well-known t(6)A modification appears to be a hydrolyzed
CC       artifact of natural cyclic t(6)A (ct(6)A) that occurs during the
CC       preparation and handling of tRNA in B.subtilis and many other species
CC       (PubMed:23242255). In these species, the t(6)A modification is
CC       processed further by dehydration into ct(6)A, a reaction catalyzed by
CC       TcdA. {ECO:0000305}.
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DR   EMBL; D88802; BAA19716.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB12411.1; -; Genomic_DNA.
DR   PIR; D69786; D69786.
DR   RefSeq; NP_388473.1; NC_000964.3.
DR   RefSeq; WP_003234078.1; NZ_JNCM01000032.1.
DR   AlphaFoldDB; O05516; -.
DR   SMR; O05516; -.
DR   STRING; 224308.BSU05920; -.
DR   PaxDb; O05516; -.
DR   PRIDE; O05516; -.
DR   EnsemblBacteria; CAB12411; CAB12411; BSU_05920.
DR   GeneID; 939874; -.
DR   KEGG; bsu:BSU05920; -.
DR   PATRIC; fig|224308.179.peg.637; -.
DR   eggNOG; COG1214; Bacteria.
DR   InParanoid; O05516; -.
DR   OMA; PFYLKDF; -.
DR   PhylomeDB; O05516; -.
DR   BioCyc; BSUB:BSU05920-MON; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0002949; P:tRNA threonylcarbamoyladenosine modification; IDA:UniProtKB.
DR   InterPro; IPR043129; ATPase_NBD.
DR   InterPro; IPR000905; Gcp-like_dom.
DR   InterPro; IPR022496; T6A_TsaB.
DR   PANTHER; PTHR11735; PTHR11735; 1.
DR   PANTHER; PTHR11735:SF11; PTHR11735:SF11; 1.
DR   Pfam; PF00814; TsaD; 1.
DR   SUPFAM; SSF53067; SSF53067; 2.
DR   TIGRFAMs; TIGR03725; T6A_YeaZ; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Reference proteome; tRNA processing.
FT   CHAIN           1..229
FT                   /note="tRNA threonylcarbamoyladenosine biosynthesis protein
FT                   TsaB"
FT                   /id="PRO_0000387461"
SQ   SEQUENCE   229 AA;  25243 MW;  CC70715EEA5C1A2D CRC64;
     MTILAIDTSN YTLGIALLRE DTVIAEYITY LKKNHSVRAM PAVHSLLNDC DMAPQDLSKI
     VVAKGPGSYT GVRIGVTLAK TLAWSLDIPI SAVSSLETLA ANGRHFDGLI SPIFDARRGQ
     VYTGLYQYKN GLLEQVVPDQ NVMLADWLEM LKEKDRPVLF LGHDTSLHKQ MIEDVLGTKG
     FIGTAAQHNP RPSELAFLGK EKEAADVHGL VPDYLRLAEA EAKWIESQK