TSAE_BACSU
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 03-AUG-2022, entry version 126.
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]
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 FUNCTION, ATPASE ACTIVITY, KINETIC PARAMETERS, SUBUNIT, SUBCELLULAR
RP LOCATION, INDUCTION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF LYS-41.
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]
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 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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
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 AlphaFoldDB; O05515; -.
DR SMR; O05515; -.
DR STRING; 224308.BSU05910; -.
DR PaxDb; O05515; -.
DR PRIDE; 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 OMA; FTDDAIC; -.
DR PhylomeDB; O05515; -.
DR BioCyc; BSUB:BSU05910-MON; -.
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; 3.40.50.300; -; 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 BINDING 38..43
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 42
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 106
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 130
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
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;
MKQLKWRTVN PEETKAIAKL TAAFAKPGDV LTLEGDLGAG KTTFTKGFAE GLGITRIVNS
PTFTIIKEYN DGVLPLYHMD VYRMEDESED LGLDEYFHGQ GVCLVEWAHL IEEQLPQERL
QIVIKRAGDD EREITFTAVG NRYEMLCEEL SRHDNISN
