TSAB_ECOLI
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 03-AUG-2022, entry version 163.
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; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC 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_SSZK01000001.1.
DR PDB; 1OKJ; X-ray; 2.28 A; A/B/C/D=2-231.
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 PDBsum; 1OKJ; -.
DR PDBsum; 4WQ4; -.
DR PDBsum; 4WQ5; -.
DR PDBsum; 4YDU; -.
DR PDBsum; 6Z81; -.
DR AlphaFoldDB; P76256; -.
DR SMR; P76256; -.
DR BioGRID; 4260340; 15.
DR BioGRID; 850661; 5.
DR ComplexPortal; CPX-1094; YgjD-YeaZ-YjeE complex.
DR DIP; DIP-11804N; -.
DR IntAct; P76256; 12.
DR STRING; 511145.b1807; -.
DR jPOST; P76256; -.
DR PaxDb; P76256; -.
DR PRIDE; P76256; -.
DR EnsemblBacteria; AAC74877; AAC74877; b1807.
DR EnsemblBacteria; BAA15611; BAA15611; BAA15611.
DR GeneID; 946304; -.
DR KEGG; ecj:JW1796; -.
DR KEGG; eco:b1807; -.
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 PhylomeDB; P76256; -.
DR BioCyc; EcoCyc:G6991-MON; -.
DR BioCyc; MetaCyc:G6991-MON; -.
DR EvolutionaryTrace; P76256; -.
DR PRO; PR:P76256; -.
DR Proteomes; UP000000318; Chromosome.
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; IC:ComplexPortal.
DR GO; GO:0002949; P:tRNA threonylcarbamoyladenosine modification; IDA:ComplexPortal.
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 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"
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
