TTUD_THET2
ID TTUD_THET2 Reviewed; 285 AA.
AC Q72JV2;
DT 20-DEC-2017, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Sulfur carrier protein TtuD {ECO:0000303|PubMed:27878988};
DE AltName: Full=Rhodanese-like protein TtuD {ECO:0000303|PubMed:27878988};
DE AltName: Full=tRNA two-thiouridine-synthesizing protein D {ECO:0000303|PubMed:27878988};
GN Name=ttuD {ECO:0000303|PubMed:27878988};
GN OrderedLocusNames=TT_C0666 {ECO:0000312|EMBL:AAS81014.1};
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 FUNCTION, DISRUPTION PHENOTYPE, PATHWAY, MUTAGENESIS OF CYS-240, AND
RP SULFHYDRATION AT CYS-240.
RC STRAIN=ATCC BAA-163 / DSM 7039 / HB27;
RX PubMed=27878988; DOI=10.1002/1873-3468.12499;
RA Shigi N., Asai S.I., Watanabe K.;
RT "Identification of a rhodanese-like protein involved in thiouridine
RT biosynthesis in Thermus thermophilus tRNA.";
RL FEBS Lett. 590:4628-4637(2016).
CC -!- FUNCTION: Required for the efficient 2-thiolation of 5-methyluridine
CC residue at position 54 in the T loop of tRNAs, leading to 5-methyl-2-
CC thiouridine (m(5)s(2)U or s(2)T). TtuD is a sulfur carrier protein that
CC has a role to direct sulfur flow from cysteine desulfurases to
CC m(5)s(2)U synthesis in vivo. It enhances the cysteine desulfurase
CC activity of IscS and SufS, as well as the formation of thiocarboxylated
CC TtuB (TtuB-COSH) in the presence of these desulfurases.
CC {ECO:0000269|PubMed:27878988}.
CC -!- PATHWAY: tRNA modification. {ECO:0000269|PubMed:27878988}.
CC -!- PTM: Cys-240 can accept a sulfur atom as persulfide forms from cysteine
CC desulfurases IscS and SufS. {ECO:0000269|PubMed:27878988}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene have a m(5)s(2)U content
CC in tRNA that is about 40% of that of the wild-type strain. Moreover,
CC TtuB-conjugates in the deletion mutant strain are similar to those in
CC the wild-type strain, suggesting that TtuD is not involved in TtuB-
CC conjugate formation. {ECO:0000269|PubMed:27878988}.
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DR EMBL; AE017221; AAS81014.1; -; Genomic_DNA.
DR RefSeq; WP_008632430.1; NC_005835.1.
DR AlphaFoldDB; Q72JV2; -.
DR SMR; Q72JV2; -.
DR STRING; 262724.TT_C0666; -.
DR EnsemblBacteria; AAS81014; AAS81014; TT_C0666.
DR GeneID; 3170077; -.
DR KEGG; tth:TT_C0666; -.
DR eggNOG; COG2897; Bacteria.
DR HOGENOM; CLU_031618_1_3_0; -.
DR OMA; LLDVRWQ; -.
DR OrthoDB; 1385159at2; -.
DR BioCyc; MetaCyc:MON-20263; -.
DR Proteomes; UP000000592; Chromosome.
DR GO; GO:0004792; F:thiosulfate sulfurtransferase activity; IEA:InterPro.
DR GO; GO:0008033; P:tRNA processing; IEA:UniProtKB-KW.
DR Gene3D; 3.40.250.10; -; 2.
DR InterPro; IPR001763; Rhodanese-like_dom.
DR InterPro; IPR036873; Rhodanese-like_dom_sf.
DR InterPro; IPR001307; Thiosulphate_STrfase_CS.
DR Pfam; PF00581; Rhodanese; 2.
DR SMART; SM00450; RHOD; 2.
DR SUPFAM; SSF52821; SSF52821; 2.
DR PROSITE; PS00380; RHODANESE_1; 1.
DR PROSITE; PS00683; RHODANESE_2; 1.
DR PROSITE; PS50206; RHODANESE_3; 2.
PE 1: Evidence at protein level;
KW Repeat; tRNA processing.
FT CHAIN 1..285
FT /note="Sulfur carrier protein TtuD"
FT /id="PRO_0000442740"
FT DOMAIN 20..127
FT /note="Rhodanese 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00173"
FT DOMAIN 161..281
FT /note="Rhodanese 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00173"
FT MOD_RES 240
FT /note="Cysteine persulfide"
FT /evidence="ECO:0000269|PubMed:27878988"
FT MUTAGEN 240
FT /note="C->S: Loss of persulfidation."
FT /evidence="ECO:0000269|PubMed:27878988"
SQ SEQUENCE 285 AA; 32925 MW; 845757ABCDE6CAD6 CRC64;
MGYAHPEVLV STDWVQEHLE DPKVRVLEVD EDILLYDTGH IPGAQKIDWQ RDFWDPVVRD
FISEEEFAKL MERLGISNDT TVVLYGDKNN WWAAYAFWFF KYNGHKDVRL MNGGRQKWVE
EGRPLTTEVP SYPPGRYEVP YRDESIRAYR DDVLEHIIKV KEGKGALVDV RSPQEYRGEL
THMPDYPQEG ALRAGHIPGA KNIPWAKAVN PDGTFKSAEE LRALYEPLGI TKDKDIVVYC
RIAERSSHSW FVLKYLLGYP HVKNYDGSWT EWGNLVGVPI AKGEE
