ID   TSAB_BUCBP              Reviewed;         221 AA.
AC   Q89AI5;
DT   13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 91.
DE   RecName: Full=tRNA threonylcarbamoyladenosine biosynthesis protein TsaB;
DE   AltName: Full=t(6)A37 threonylcarbamoyladenosine biosynthesis protein TsaB;
GN   Name=tsaB; OrderedLocusNames=bbp_301;
OS   Buchnera aphidicola subsp. Baizongia pistaciae (strain Bp).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=224915;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bp;
RX   PubMed=12522265; DOI=10.1073/pnas.0235981100;
RA   van Ham R.C.H.J., Kamerbeek J., Palacios C., Rausell C., Abascal F.,
RA   Bastolla U., Fernandez J.M., Jimenez L., Postigo M., Silva F.J.,
RA   Tamames J., Viguera E., Latorre A., Valencia A., Moran F., Moya A.;
RT   "Reductive genome evolution in Buchnera aphidicola.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:581-586(2003).
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 (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the KAE1 / TsaD family. TsaB subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AE016826; AAO27026.1; -; Genomic_DNA.
DR   RefSeq; WP_011091427.1; NC_004545.1.
DR   AlphaFoldDB; Q89AI5; -.
DR   SMR; Q89AI5; -.
DR   STRING; 224915.bbp_301; -.
DR   EnsemblBacteria; AAO27026; AAO27026; bbp_301.
DR   GeneID; 56470841; -.
DR   KEGG; bab:bbp_301; -.
DR   eggNOG; COG1214; Bacteria.
DR   HOGENOM; CLU_064886_2_0_6; -.
DR   OMA; FIGVRIG; -.
DR   OrthoDB; 1826274at2; -.
DR   Proteomes; UP000000601; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0002949; P:tRNA threonylcarbamoyladenosine modification; IEA:InterPro.
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   3: Inferred from homology;
KW   Cytoplasm; Reference proteome; tRNA processing.
FT   CHAIN           1..221
FT                   /note="tRNA threonylcarbamoyladenosine biosynthesis protein
FT                   TsaB"
FT                   /id="PRO_0000096994"
SQ   SEQUENCE   221 AA;  25185 MW;  7C4B62DFC674DEED CRC64;
     MLKTILAFDT SMSVCSISLL HKNRKYNIQK ECRNNHTLYL LPMIHEILKK NHVSLNEINI
     IATSKGPGSF SGVRIALAVA QGISLGLNLP HVISLSTILI MAEQVWNNHK ISKVLAIITV
     NKTSVYWIQY SRNFHGLWIK KSKAIILNLS KALEKILSLK KQWALVGNGW DKFPKNILKK
     IFITNITFPN SKYIISLISA NSIYQKKEVL HKIIPIYLNE R