Database: UniProt
Entry: O05515
LinkDB: O05515
Original site: O05515 
ID   TSAE_BACSU              Reviewed;         158 AA.
AC   O05515;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   29-SEP-2021, entry version 124.
DE   RecName: Full=tRNA threonylcarbamoyladenosine biosynthesis protein TsaE;
DE   AltName: Full=t(6)A37 threonylcarbamoyladenosine biosynthesis protein TsaE;
GN   Name=tsaE; Synonyms=ydiB; OrderedLocusNames=BSU05910;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
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]
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]
RC   STRAIN=168;
RX   PubMed=19246765; DOI=10.1099/mic.0.021543-0;
RA   Karst J.C., Foucher A.-E., Campbell T.L., Di Guilmi A.-M., Stroebel D.,
RA   Mangat C.S., Brown E.D., Jault J.-M.;
RT   "The ATPase activity of an 'essential' Bacillus subtilis enzyme, ydiB, is
RT   required for its cellular function and is modulated by oligomerization.";
RL   Microbiology 155:944-956(2009).
RN   [4]
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 TsaB; this reaction does not require ATP in
CC       vitro. TsaE seems to play an indirect role in the t(6)A biosynthesis
CC       pathway, possibly in regulating the core enzymatic function of TsaD.
CC       Displays ATPase activity in vitro, which is modulated by the oligomeric
CC       status of the protein. {ECO:0000269|PubMed:19246765,
CC       ECO:0000269|PubMed:23072323}.
CC       Kinetic parameters:
CC         KM=62.1 uM for ATP {ECO:0000269|PubMed:19246765};
CC         Vmax=10.5 nmol/min/mg enzyme {ECO:0000269|PubMed:19246765};
CC         Note=Values are given for the monomeric form. The rate of ATP
CC         hydrolysis is about three times higher for the monomeric form as
CC         compared to the homooligomeric forms.;
CC   -!- SUBUNIT: Monomer, homodimer or homotetramer; in equilibrium. Low salt
CC       concentration favors oligomerization, while high salt concentration
CC       favors the monomeric form. {ECO:0000269|PubMed:19246765}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19246765}.
CC       Note=Localized predominantly at the cell poles and at the periphery of
CC       the bacterium.
CC   -!- INDUCTION: Expressed at all stages of growth.
CC       {ECO:0000269|PubMed:19246765}.
CC   -!- DISRUPTION PHENOTYPE: Cells lacking this gene exhibit significantly
CC       reduced growth in rich and minimal medium.
CC       {ECO:0000269|PubMed:19246765}.
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 TsaE family. {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; BAA19715.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB12410.1; -; Genomic_DNA.
DR   PIR; C69786; C69786.
DR   RefSeq; NP_388472.1; NC_000964.3.
DR   RefSeq; WP_003234079.1; NZ_JNCM01000032.1.
DR   PDB; 5MVR; X-ray; 1.76 A; A=2-158.
DR   PDB; 5NP9; X-ray; 2.00 A; A=1-158.
DR   PDBsum; 5MVR; -.
DR   PDBsum; 5NP9; -.
DR   SMR; O05515; -.
DR   STRING; 224308.BSU05910; -.
DR   PaxDb; O05515; -.
DR   EnsemblBacteria; CAB12410; CAB12410; BSU_05910.
DR   GeneID; 938047; -.
DR   KEGG; bsu:BSU05910; -.
DR   PATRIC; fig|224308.179.peg.636; -.
DR   eggNOG; COG0802; Bacteria.
DR   InParanoid; O05515; -.
DR   PhylomeDB; O05515; -.
DR   BioCyc; BSUB:BSU05910-MONOMER; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0002949; P:tRNA threonylcarbamoyladenosine modification; IDA:UniProtKB.
DR   Gene3D;; -; 1.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR003442; T6A_TsaE.
DR   Pfam; PF02367; TsaE; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR00150; T6A_YjeE; 1.
PE   1: Evidence at protein level;
KW   3D-structure; ATP-binding; Cytoplasm; Magnesium; Metal-binding;
KW   Nucleotide-binding; Reference proteome; tRNA processing.
FT   CHAIN           1..158
FT                   /note="tRNA threonylcarbamoyladenosine biosynthesis protein
FT                   TsaE"
FT                   /id="PRO_0000096211"
FT   NP_BIND         38..43
FT                   /note="ATP"
FT                   /evidence="ECO:0000250"
FT   METAL           42
FT                   /note="Magnesium"
FT                   /evidence="ECO:0000250"
FT   METAL           106
FT                   /note="Magnesium"
FT                   /evidence="ECO:0000250"
FT   BINDING         130
FT                   /note="ATP; via carbonyl oxygen"
FT                   /evidence="ECO:0000250"
FT   MUTAGEN         41
FT                   /note="K->A: Severely reduces ATPase activity and growth
FT                   rate."
FT                   /evidence="ECO:0000269|PubMed:19246765"
FT   STRAND          2..10
FT                   /evidence="ECO:0007829|PDB:5MVR"
FT   HELIX           11..23
FT                   /evidence="ECO:0007829|PDB:5MVR"
FT   STRAND          30..34
FT                   /evidence="ECO:0007829|PDB:5MVR"
FT   HELIX           41..51
FT                   /evidence="ECO:0007829|PDB:5MVR"
FT   TURN            62..64
FT                   /evidence="ECO:0007829|PDB:5NP9"
FT   STRAND          65..69
FT                   /evidence="ECO:0007829|PDB:5MVR"
FT   STRAND          71..74
FT                   /evidence="ECO:0007829|PDB:5MVR"
FT   STRAND          76..80
FT                   /evidence="ECO:0007829|PDB:5MVR"
FT   HELIX           84..86
FT                   /evidence="ECO:0007829|PDB:5NP9"
FT   HELIX           94..97
FT                   /evidence="ECO:0007829|PDB:5MVR"
FT   STRAND          99..106
FT                   /evidence="ECO:0007829|PDB:5MVR"
FT   HELIX           108..114
FT                   /evidence="ECO:0007829|PDB:5MVR"
FT   STRAND          119..127
FT                   /evidence="ECO:0007829|PDB:5MVR"
FT   TURN            128..130
FT                   /evidence="ECO:0007829|PDB:5MVR"
FT   STRAND          131..140
FT                   /evidence="ECO:0007829|PDB:5MVR"
FT   HELIX           141..152
FT                   /evidence="ECO:0007829|PDB:5MVR"
SQ   SEQUENCE   158 AA;  17906 MW;  4847502A54A64221 CRC64;
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