ID   THIS_THET2              Reviewed;          64 AA.
AC   Q72KL7;
DT   20-DEC-2017, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 96.
DE   RecName: Full=Sulfur carrier protein ThiS {ECO:0000303|PubMed:19037260};
DE   AltName: Full=Thiamine biosynthesis protein ThiS {ECO:0000305};
GN   Name=thiS {ECO:0000303|PubMed:19037260, ECO:0000312|EMBL:AAS80664.1};
GN   OrderedLocusNames=TT_C0316 {ECO:0000312|EMBL:AAS80664.1};
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, THIOCARBOXYLATION AT GLY-64, AND AMPYLATION AT GLY-64.
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).
CC   -!- FUNCTION: Is the sulfur donor in the synthesis of the thiazole
CC       phosphate moiety of thiamine phosphate. {ECO:0000305|PubMed:19037260}.
CC   -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis.
CC       {ECO:0000305}.
CC   -!- PTM: C-terminal thiocarboxylation occurs in 2 steps, it is first acyl-
CC       adenylated (-COAMP) by TtuC, then thiocarboxylated (-COSH) by the
CC       cysteine desulfurases IscS or SufS. {ECO:0000269|PubMed:19037260}.
CC   -!- SIMILARITY: Belongs to the sulfur carrier protein ThiS family.
CC       {ECO:0000305}.
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DR   EMBL; AE017221; AAS80664.1; -; Genomic_DNA.
DR   RefSeq; WP_011172767.1; NC_005835.1.
DR   AlphaFoldDB; Q72KL7; -.
DR   SMR; Q72KL7; -.
DR   STRING; 262724.TT_C0316; -.
DR   EnsemblBacteria; AAS80664; AAS80664; TT_C0316.
DR   GeneID; 3169033; -.
DR   KEGG; tth:TT_C0316; -.
DR   eggNOG; COG2104; Bacteria.
DR   HOGENOM; CLU_174611_1_0_0; -.
DR   OMA; DFYPGAR; -.
DR   OrthoDB; 2084255at2; -.
DR   UniPathway; UPA00060; -.
DR   EvolutionaryTrace; Q72KL7; -.
DR   Proteomes; UP000000592; Chromosome.
DR   GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR   GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.10.20.30; -; 1.
DR   InterPro; IPR012675; Beta-grasp_dom_sf.
DR   InterPro; IPR016155; Mopterin_synth/thiamin_S_b.
DR   InterPro; IPR010035; Thi_S.
DR   InterPro; IPR003749; ThiS/MoaD-like.
DR   Pfam; PF02597; ThiS; 1.
DR   SUPFAM; SSF54285; SSF54285; 1.
DR   TIGRFAMs; TIGR01683; thiS; 1.
PE   1: Evidence at protein level;
KW   Nucleotide-binding; Phosphoprotein; Thiamine biosynthesis; Thioester bond.
FT   CHAIN           1..64
FT                   /note="Sulfur carrier protein ThiS"
FT                   /id="PRO_0000442741"
FT   MOD_RES         64
FT                   /note="1-thioglycine; alternate"
FT                   /evidence="ECO:0000269|PubMed:19037260"
FT   MOD_RES         64
FT                   /note="Glycyl adenylate; alternate"
FT                   /evidence="ECO:0000269|PubMed:19037260"
FT   CROSSLNK        64
FT                   /note="Glycyl cysteine thioester (Gly-Cys) (interchain with
FT                   C-192 in TtuC); alternate"
FT                   /evidence="ECO:0000305|PubMed:19037260"
SQ   SEQUENCE   64 AA;  6986 MW;  6B8FCBEE9C755414 CRC64;
     MVWLNGEPRP LEGKTLKEVL EEMGVELKGV AVLLNEEAFL GLEVPDRPLR DGDVVEVVAL
     MQGG