TTUB_THET2
ID TTUB_THET2 Reviewed; 65 AA.
AC Q72LF4;
DT 20-DEC-2017, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=Sulfur carrier protein TtuB {ECO:0000303|PubMed:16547008, ECO:0000303|PubMed:28439027};
DE AltName: Full=2-thiouridine synthesis sulfur carrier protein TtuB {ECO:0000303|PubMed:28439027};
DE AltName: Full=Ubiquitin-like S-donor protein TtuB {ECO:0000303|PubMed:28439027};
DE AltName: Full=Ubiquitin-like protein modifier TtuB {ECO:0000303|PubMed:22467871};
DE AltName: Full=tRNA two-thiouridine-synthesizing protein B {ECO:0000303|PubMed:16547008};
GN Name=ttuB {ECO:0000303|PubMed:16547008};
GN OrderedLocusNames=TT_C0105 {ECO:0000312|EMBL:AAS80453.1};
OS Thermus thermophilus (strain ATCC BAA-163 / DSM 7039 / HB27).
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=262724;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-163 / DSM 7039 / HB27;
RX PubMed=15064768; DOI=10.1038/nbt956;
RA Henne A., Brueggemann H., Raasch C., Wiezer A., Hartsch T., Liesegang H.,
RA Johann A., Lienard T., Gohl O., Martinez-Arias R., Jacobi C.,
RA Starkuviene V., Schlenczeck S., Dencker S., Huber R., Klenk H.-P.,
RA Kramer W., Merkl R., Gottschalk G., Fritz H.-J.;
RT "The genome sequence of the extreme thermophile Thermus thermophilus.";
RL Nat. Biotechnol. 22:547-553(2004).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, TRNA-BINDING, DISRUPTION
RP PHENOTYPE, PATHWAY, AND SUBUNIT.
RC STRAIN=ATCC BAA-163 / DSM 7039 / HB27;
RX PubMed=16547008; DOI=10.1074/jbc.m511675200;
RA Shigi N., Sakaguchi Y., Suzuki T., Watanabe K.;
RT "Identification of two tRNA thiolation genes required for cell growth at
RT extremely high temperatures.";
RL J. Biol. Chem. 281:14296-14306(2006).
RN [3]
RP FUNCTION, THIOCARBOXYLATION AT GLY-65, AMPYLATION AT GLY-65, CROSS-LINKING
RP TO ADENYLYLTRANSFERASE TTUC, AND 3D-STRUCTURE MODELING.
RC STRAIN=ATCC BAA-163 / DSM 7039 / HB27;
RX PubMed=19037260; DOI=10.1038/emboj.2008.246;
RA Shigi N., Sakaguchi Y., Asai S., Suzuki T., Watanabe K.;
RT "Common thiolation mechanism in the biosynthesis of tRNA thiouridine and
RT sulphur-containing cofactors.";
RL EMBO J. 27:3267-3278(2008).
RN [4]
RP FUNCTION AS A PROTEIN MODIFIER, AND MUTAGENESIS OF GLY-65.
RC STRAIN=ATCC BAA-163 / DSM 7039 / HB27;
RX PubMed=22467871; DOI=10.1074/jbc.m112.359844;
RA Shigi N.;
RT "Posttranslational modification of cellular proteins by a ubiquitin-like
RT protein in bacteria.";
RL J. Biol. Chem. 287:17568-17577(2012).
RN [5] {ECO:0007744|PDB:5GHA}
RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF MUTANT CYS-65 IN COMPLEX WITH
RP TTUA PROTEIN, FUNCTION, AND SUBUNIT.
RC STRAIN=ATCC BAA-163 / DSM 7039 / HB27;
RX PubMed=28439027; DOI=10.1073/pnas.1615585114;
RA Chen M., Asai S., Narai S., Nambu S., Omura N., Sakaguchi Y., Suzuki T.,
RA Ikeda-Saito M., Watanabe K., Yao M., Shigi N., Tanaka Y.;
RT "Biochemical and structural characterization of oxygen-sensitive 2-
RT thiouridine synthesis catalyzed by an iron-sulfur protein TtuA.";
RL Proc. Natl. Acad. Sci. U.S.A. 114:4954-4959(2017).
CC -!- FUNCTION: Required for the 2-thiolation of 5-methyluridine residue at
CC position 54 in the T loop of tRNAs, leading to 5-methyl-2-thiouridine
CC (m(5)s(2)U or s(2)T) (PubMed:16547008, PubMed:28439027). This
CC modification allows thermal stabilization of tRNAs in thermophilic
CC microorganisms, and is essential for cell growth at high temperatures
CC (PubMed:16547008). Thiocarboxylated TtuB functions as the sulfur donor
CC in the sulfurtransferase reaction catalyzed by TtuA (PubMed:28439027,
CC PubMed:19037260). TtuB also functions as a protein modifier covalently
CC attached to lysine residues of the target proteins TtuA and TtuC
CC (PubMed:22467871). TtuB conjugation might play a regulatory role to
CC ensure appropriate sulfur transfer in cells (PubMed:22467871).
CC {ECO:0000269|PubMed:16547008, ECO:0000269|PubMed:19037260,
CC ECO:0000269|PubMed:22467871, ECO:0000269|PubMed:28439027}.
CC -!- PATHWAY: tRNA modification. {ECO:0000269|PubMed:16547008}.
CC -!- SUBUNIT: Is able to form a heterocomplex with TtuA.
CC {ECO:0000269|PubMed:16547008, ECO:0000269|PubMed:28439027}.
CC -!- PTM: The C-terminal glycine residue of TtuB is first activated by TtuC
CC as an acyl-adenylate (TtuB-COAMP), and then converted to the
CC thiocarboxylate form (TtuB-COSH) by the cysteine desulfurases IscS or
CC SufS. {ECO:0000269|PubMed:19037260}.
CC -!- DISRUPTION PHENOTYPE: Disruption of this gene completely abolishes the
CC presence of m(5)s(2)U in tRNAs, although its precursor, 5-methyluridine
CC (ribothymidine) is present; other nucleoside modifications remain
CC unchanged. These deletion mutants exhibit a temperature-sensitive
CC phenotype, they are unable to grow above 80 degrees Celsius.
CC {ECO:0000269|PubMed:16547008}.
CC -!- SIMILARITY: Belongs to the TtuB family. {ECO:0000305}.
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DR EMBL; AE017221; AAS80453.1; -; Genomic_DNA.
DR RefSeq; WP_011172562.1; NC_005835.1.
DR PDB; 5GHA; X-ray; 2.50 A; E/F/G/H=1-64.
DR PDBsum; 5GHA; -.
DR AlphaFoldDB; Q72LF4; -.
DR SMR; Q72LF4; -.
DR STRING; 262724.TT_C0105; -.
DR EnsemblBacteria; AAS80453; AAS80453; TT_C0105.
DR GeneID; 3169172; -.
DR KEGG; tth:TT_C0105; -.
DR eggNOG; COG2104; Bacteria.
DR HOGENOM; CLU_114601_9_5_0; -.
DR OMA; NNEVKEM; -.
DR OrthoDB; 2083208at2; -.
DR BioCyc; MetaCyc:MON-20126; -.
DR Proteomes; UP000000592; Chromosome.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0008033; P:tRNA processing; IEA:UniProtKB-KW.
DR Gene3D; 3.10.20.30; -; 1.
DR InterPro; IPR012675; Beta-grasp_dom_sf.
DR InterPro; IPR016155; Mopterin_synth/thiamin_S_b.
DR InterPro; IPR003749; ThiS/MoaD-like.
DR Pfam; PF02597; ThiS; 1.
DR SUPFAM; SSF54285; SSF54285; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Isopeptide bond; Nucleotide-binding; Phosphoprotein;
KW Thioester bond; tRNA processing; Ubl conjugation pathway.
FT CHAIN 1..65
FT /note="Sulfur carrier protein TtuB"
FT /id="PRO_0000442738"
FT MOD_RES 65
FT /note="1-thioglycine; alternate"
FT /evidence="ECO:0000269|PubMed:19037260,
FT ECO:0000305|PubMed:28439027"
FT MOD_RES 65
FT /note="Glycyl adenylate; alternate"
FT /evidence="ECO:0000269|PubMed:19037260"
FT CROSSLNK 65
FT /note="Glycyl cysteine thioester (Gly-Cys) (interchain with
FT C-192 in TtuC); alternate"
FT /evidence="ECO:0000269|PubMed:19037260"
FT CROSSLNK 65
FT /note="Glycyl lysine isopeptide (Gly-Lys) (interchain with
FT K-? in acceptor proteins); alternate"
FT /evidence="ECO:0000269|PubMed:22467871"
FT MUTAGEN 65
FT /note="Missing: Loss of formation of TtuB conjugates."
FT /evidence="ECO:0000269|PubMed:22467871"
FT STRAND 3..13
FT /evidence="ECO:0007829|PDB:5GHA"
FT STRAND 18..20
FT /evidence="ECO:0007829|PDB:5GHA"
FT HELIX 21..27
FT /evidence="ECO:0007829|PDB:5GHA"
FT HELIX 32..34
FT /evidence="ECO:0007829|PDB:5GHA"
FT STRAND 35..39
FT /evidence="ECO:0007829|PDB:5GHA"
FT STRAND 56..60
FT /evidence="ECO:0007829|PDB:5GHA"
SQ SEQUENCE 65 AA; 7310 MW; 63F1E103D64FBFDB CRC64;
MRVVLRLPER KEVEVKGNRP LREVLEELGL NPETVVAVRG EELLTLEDEV REEDTLEVLS
AISGG
