ID   TSAB_ECOLI              Reviewed;         231 AA.
AC   P76256; O08476; O08477;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   02-SEP-2026, entry version 176.
DE   RecName: Full=tRNA threonylcarbamoyladenosine biosynthesis protein TsaB;
DE   AltName: Full=t(6)A37 threonylcarbamoyladenosine biosynthesis protein TsaB;
GN   Name=tsaB; Synonyms=yeaZ; OrderedLocusNames=b1807, JW1796;
OS   Escherichia coli (strain K12).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Enterobacterales; Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=9097040; DOI=10.1093/dnares/3.6.379;
RA   Itoh T., Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K.,
RA   Kasai H., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T.,
RA   Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S., Nakamura Y.,
RA   Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y.,
RA   Sivasundaram S., Tagami H., Takeda J., Takemoto K., Wada C., Yamamoto Y.,
RA   Horiuchi T.;
RT   "A 460-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT   the 40.1-50.0 min region on the linkage map.";
RL   DNA Res. 3:379-392(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA   Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1462(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT   and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [4]
RP   PROTEASE ACTIVITY, FUNCTION, DISRUPTION PHENOTYPE, SUBUNIT, INTERACTION
RP   WITH TSAD AND TSAE, LACK OF GLYCOPROTEASE ACTIVITY, AND SUBCELLULAR
RP   LOCATION.
RC   STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX   PubMed=19376873; DOI=10.1128/jb.00136-09;
RA   Handford J.I., Ize B., Buchanan G., Butland G.P., Greenblatt J., Emili A.,
RA   Palmer T.;
RT   "Conserved network of proteins essential for bacterial viability.";
RL   J. Bacteriol. 191:4732-4749(2009).
RN   [5]
RP   INTERACTION WITH TSAD AND TSAE.
RC   STRAIN=K12;
RX   PubMed=20701780; DOI=10.1186/1471-2164-11-470;
RA   Rajagopala S.V., Yamamoto N., Zweifel A.E., Nakamichi T., Huang H.K.,
RA   Mendez-Rios J.D., Franca-Koh J., Boorgula M.P., Fujita K., Suzuki K.,
RA   Hu J.C., Wanner B.L., Mori H., Uetz P.;
RT   "The Escherichia coli K-12 ORFeome: a resource for comparative molecular
RT   microbiology.";
RL   BMC Genomics 11:470-470(2010).
RN   [6]
RP   FUNCTION IN T(6)A37 FORMATION, GENE NAME, AND INTERACTION WITH TSAE; TSAD
RP   AND TSAC.
RC   STRAIN=K12;
RX   PubMed=22378793; DOI=10.1074/jbc.m112.344028;
RA   Deutsch C., El Yacoubi B., de Crecy-Lagard V., Iwata-Reuyl D.;
RT   "Biosynthesis of threonylcarbamoyl adenosine (t6A), a universal tRNA
RT   nucleoside.";
RL   J. Biol. Chem. 287:13666-13673(2012).
RN   [7]
RP   X-RAY CRYSTALLOGRAPHY (2.28 ANGSTROMS) OF 2-231, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
RX   PubMed=16511176; DOI=10.1107/s1744309105025856;
RA   Jeudy S., Stelter M., Coutard B., Kahn R., Abergel C.;
RT   "Preliminary crystallographic analysis of the Escherichia coli YeaZ protein
RT   using the anomalous signal of a gadolinium derivative.";
RL   Acta Crystallogr. F 61:848-851(2005).
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 probably involved in the transfer of the
CC       threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6
CC       group of A37, together with TsaD and TsaE. TsaB seems to play an
CC       indirect role in the t(6)A biosynthesis pathway, possibly in regulating
CC       the core enzymatic function of TsaD. In fact, can act as a protease
CC       that specifically degrades TsaD in vitro; therefore TsaB may post-
CC       translationally regulate cellular pools of TsaD via proteolytic
CC       degradation. Does not show sialoglycoprotease activity against
CC       glycophorin A. {ECO:0000269|PubMed:19376873,
CC       ECO:0000269|PubMed:22378793}.
CC   -!- SUBUNIT: Homodimer. Interacts with TsaD and TsaE in a mutually
CC       exclusive manner; TsaD is the preferred partner. Also interacts with
CC       TsaC. {ECO:0000269|PubMed:19376873, ECO:0000269|PubMed:20701780,
CC       ECO:0000269|PubMed:22378793}.
CC   -!- INTERACTION:
CC       P76256; P05852: tsaD; NbExp=8; IntAct=EBI-560669, EBI-561994;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19376873}.
CC   -!- DISRUPTION PHENOTYPE: Appears essential for growth, since no null
CC       mutants can be obtained. Conditional depletion of this gene leads to
CC       enlarged cells, which display highly condensed nucleoids. The TsaB
CC       depletion phenotype is suppressed by overexpressing the response
CC       regulator RstA. {ECO:0000269|PubMed:19376873}.
CC   -!- MISCELLANEOUS: TsaBCDE are necessary and sufficient for tRNA(NNU)
CC       t(6)A37 threonylcarbamoyladenosine modification in vitro in E.coli.
CC       {ECO:0000305|PubMed:22378793}.
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 E.coli 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; U00096; AAC74877.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAA15611.1; -; Genomic_DNA.
DR   PIR; G64941; G64941.
DR   RefSeq; NP_416321.1; NC_000913.3.
DR   RefSeq; WP_001220966.1; NZ_CP009789.1.
DR   PDB; 1OKJ; X-ray; 2.28 A; A/B/C/D=1-231.
DR   PDB; 4WQ4; X-ray; 2.33 A; C/D=1-231.
DR   PDB; 4WQ5; X-ray; 2.33 A; C/D=1-231.
DR   PDB; 4YDU; X-ray; 2.33 A; C/D=1-231.
DR   PDB; 6Z81; X-ray; 2.31 A; C/D=1-231.
DR   AlphaFoldDB; P76256; -.
DR   SMR; P76256; -.
DR   BioGRID; 4260340; 22.
DR   BioGRID; 850661; 5.
DR   ComplexPortal; CPX-1094; YgjD-YeaZ-YjeE complex.
DR   DIP; DIP-11804N; -.
DR   FunCoup; P76256; 496.
DR   IntAct; P76256; 12.
DR   STRING; 511145.b1807; -.
DR   jPOST; P76256; -.
DR   PaxDb; 511145-b1807; -.
DR   EnsemblBacteria; AAC74877; AAC74877; b1807.
DR   GeneID; 946304; -.
DR   KEGG; ecj:JW1796; -.
DR   KEGG; eco:b1807; -.
DR   KEGG; ecoc:C3026_10295; -.
DR   PATRIC; fig|1411691.4.peg.446; -.
DR   EchoBASE; EB3285; -.
DR   eggNOG; COG1214; Bacteria.
DR   HOGENOM; CLU_064886_2_0_6; -.
DR   InParanoid; P76256; -.
DR   OMA; DEVYWGC; -.
DR   OrthoDB; 9809995at2; -.
DR   PhylomeDB; P76256; -.
DR   BioCyc; EcoCyc:G6991-MONOMER; -.
DR   BioCyc; MetaCyc:G6991-MONOMER; -.
DR   EvolutionaryTrace; P76256; -.
DR   PRO; PR:P76256; -.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR   GO; GO:0000408; C:EKC/KEOPS complex; IPI:ComplexPortal.
DR   GO; GO:0042802; F:identical protein binding; IDA:EcoCyc.
DR   GO; GO:0008237; F:metallopeptidase activity; IDA:EcoCyc.
DR   GO; GO:1990145; P:maintenance of translational fidelity; NAS:ComplexPortal.
DR   GO; GO:0002949; P:tRNA threonylcarbamoyladenosine modification; IDA:ComplexPortal.
DR   CDD; cd24032; ASKHA_NBD_TsaB; 1.
DR   FunFam; 3.30.420.40:FF:000119; tRNA threonylcarbamoyladenosine biosynthesis protein TsaB; 1.
DR   Gene3D; 3.30.420.40; -; 2.
DR   InterPro; IPR043129; ATPase_NBD.
DR   InterPro; IPR000905; Gcp-like_dom.
DR   InterPro; IPR022496; T6A_TsaB.
DR   NCBIfam; TIGR03725; T6A_YeaZ; 1.
DR   PANTHER; PTHR11735; TRNA N6-ADENOSINE THREONYLCARBAMOYLTRANSFERASE; 1.
DR   PANTHER; PTHR11735:SF11; TRNA THREONYLCARBAMOYLADENOSINE BIOSYNTHESIS PROTEIN TSAB; 1.
DR   Pfam; PF00814; TsaD; 1.
DR   SUPFAM; SSF53067; Actin-like ATPase domain; 2.
DR   PDBsum; 1OKJ; -.
DR   PDBsum; 4WQ4; -.
DR   PDBsum; 4WQ5; -.
DR   PDBsum; 4YDU; -.
DR   PDBsum; 6Z81; -.
PE   1: Evidence at protein level;
KW   3D-structure; Cytoplasm; Reference proteome; tRNA processing.
FT   CHAIN           1..231
FT                   /note="tRNA threonylcarbamoyladenosine biosynthesis protein
FT                   TsaB"
FT                   /id="PRO_0000096990"
FT   STRAND          2..7
FT                   /evidence="ECO:0007829|PDB:1OKJ"
FT   STRAND          9..19
FT                   /evidence="ECO:0007829|PDB:1OKJ"
FT   STRAND          22..29
FT                   /evidence="ECO:0007829|PDB:1OKJ"
FT   TURN            31..33
FT                   /evidence="ECO:0007829|PDB:6Z81"
FT   TURN            34..37
FT                   /evidence="ECO:0007829|PDB:1OKJ"
FT   HELIX           38..48
FT                   /evidence="ECO:0007829|PDB:1OKJ"
FT   HELIX           53..55
FT                   /evidence="ECO:0007829|PDB:1OKJ"
FT   STRAND          58..66
FT                   /evidence="ECO:0007829|PDB:1OKJ"
FT   HELIX           68..84
FT                   /evidence="ECO:0007829|PDB:1OKJ"
FT   STRAND          89..93
FT                   /evidence="ECO:0007829|PDB:1OKJ"
FT   HELIX           94..105
FT                   /evidence="ECO:0007829|PDB:1OKJ"
FT   STRAND          109..116
FT                   /evidence="ECO:0007829|PDB:1OKJ"
FT   STRAND          118..120
FT                   /evidence="ECO:0007829|PDB:1OKJ"
FT   STRAND          122..129
FT                   /evidence="ECO:0007829|PDB:1OKJ"
FT   HELIX           138..140
FT                   /evidence="ECO:0007829|PDB:1OKJ"
FT   STRAND          142..144
FT                   /evidence="ECO:0007829|PDB:1OKJ"
FT   HELIX           146..153
FT                   /evidence="ECO:0007829|PDB:1OKJ"
FT   STRAND          158..164
FT                   /evidence="ECO:0007829|PDB:1OKJ"
FT   HELIX           165..169
FT                   /evidence="ECO:0007829|PDB:1OKJ"
FT   TURN            171..176
FT                   /evidence="ECO:0007829|PDB:6Z81"
FT   STRAND          178..183
FT                   /evidence="ECO:0007829|PDB:1OKJ"
FT   HELIX           191..193
FT                   /evidence="ECO:0007829|PDB:1OKJ"
FT   HELIX           194..204
FT                   /evidence="ECO:0007829|PDB:1OKJ"
FT   HELIX           210..212
FT                   /evidence="ECO:0007829|PDB:1OKJ"
FT   HELIX           224..227
FT                   /evidence="ECO:0007829|PDB:6Z81"
SQ   SEQUENCE   231 AA;  25181 MW;  5163E6A5342DC276 CRC64;
     MRILAIDTAT EACSVALWND GTVNAHFELC PREHTQRILP MVQDILTTSG TSLTDINALA
     YGRGPGSFTG VRIGIGIAQG LALGAELPMI GVSTLMTMAQ GAWRKNGATR VLAAIDARMG
     EVYWAEYQRD ENGIWHGEET EAVLKPEIVH ERMQQLSGEW VTVGTGWQAW PDLGKESGLV
     LRDGEVLLPA AEDMLPIACQ MFAEGKTVAV EHAEPVYLRN NVAWKKLPGK E
//