THIS_BACSU
ID THIS_BACSU Reviewed; 66 AA.
AC O31617;
DT 02-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Sulfur carrier protein ThiS;
DE AltName: Full=Thiamine biosynthesis protein ThiS;
GN Name=thiS; Synonyms=yjbS; OrderedLocusNames=BSU11680;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [2]
RP CHARACTERIZATION.
RC STRAIN=168 / CU1065;
RX PubMed=14567704; DOI=10.1021/bi034902z;
RA Park J.-H., Dorrestein P.C., Zhai H., Kinsland C., McLafferty F.W.,
RA Begley T.P.;
RT "Biosynthesis of the thiazole moiety of thiamin pyrophosphate (vitamin
RT B1).";
RL Biochemistry 42:12430-12438(2003).
RN [3]
RP FUNCTION IN SULFUR TRANSFER TO THIAZOLE.
RX PubMed=15489164; DOI=10.1016/j.chembiol.2004.08.009;
RA Dorrestein P.C., Zhai H., McLafferty F.W., Begley T.P.;
RT "The biosynthesis of the thiazole phosphate moiety of thiamin: the sulfur
RT transfer mediated by the sulfur carrier protein ThiS.";
RL Chem. Biol. 11:1373-1381(2004).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (3.15 ANGSTROMS) IN COMPLEX WITH THIG, AND SUBUNIT.
RX PubMed=15362849; DOI=10.1021/bi0488911;
RA Settembre E.C., Dorrestein P.C., Zhai H., Chatterjee A., McLafferty F.W.,
RA Begley T.P., Ealick S.E.;
RT "Thiamin biosynthesis in Bacillus subtilis: structure of the thiazole
RT synthase/sulfur carrier protein complex.";
RL Biochemistry 43:11647-11657(2004).
CC -!- FUNCTION: Is the sulfur donor in the synthesis of the thiazole
CC phosphate moiety of thiamine phosphate. {ECO:0000269|PubMed:15489164}.
CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis.
CC -!- SUBUNIT: Forms heterodimers with ThiG. {ECO:0000269|PubMed:15362849}.
CC -!- PTM: C-terminal thiocarboxylation occurs in 2 steps, it is first acyl-
CC adenylated (-COAMP) by ThiF, then thiocarboxylated (-COSH) by ThiI.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the sulfur carrier protein ThiS family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AL009126; CAB13025.1; -; Genomic_DNA.
DR PIR; C69845; C69845.
DR RefSeq; NP_389050.1; NC_000964.3.
DR RefSeq; WP_010886482.1; NZ_JNCM01000035.1.
DR PDB; 1TYG; X-ray; 3.15 A; B/G=1-66.
DR PDBsum; 1TYG; -.
DR AlphaFoldDB; O31617; -.
DR SMR; O31617; -.
DR IntAct; O31617; 1.
DR STRING; 224308.BSU11680; -.
DR PaxDb; O31617; -.
DR EnsemblBacteria; CAB13025; CAB13025; BSU_11680.
DR GeneID; 939811; -.
DR KEGG; bsu:BSU11680; -.
DR eggNOG; COG2104; Bacteria.
DR InParanoid; O31617; -.
DR OMA; DTGTIQD; -.
DR PhylomeDB; O31617; -.
DR BioCyc; BSUB:BSU11680-MON; -.
DR BioCyc; MetaCyc:BSU11680-MON; -.
DR UniPathway; UPA00060; -.
DR EvolutionaryTrace; O31617; -.
DR Proteomes; UP000001570; 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 PANTHER; PTHR34472; PTHR34472; 1.
DR Pfam; PF02597; ThiS; 1.
DR SUPFAM; SSF54285; SSF54285; 1.
DR TIGRFAMs; TIGR01683; thiS; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Thiamine biosynthesis.
FT CHAIN 1..66
FT /note="Sulfur carrier protein ThiS"
FT /id="PRO_0000391751"
FT MOD_RES 66
FT /note="1-thioglycine; alternate"
FT /evidence="ECO:0000250"
FT MOD_RES 66
FT /note="Glycyl adenylate; alternate"
FT /evidence="ECO:0000250"
FT STRAND 2..4
FT /evidence="ECO:0007829|PDB:1TYG"
FT STRAND 7..9
FT /evidence="ECO:0007829|PDB:1TYG"
FT STRAND 12..14
FT /evidence="ECO:0007829|PDB:1TYG"
FT HELIX 18..24
FT /evidence="ECO:0007829|PDB:1TYG"
FT STRAND 33..36
FT /evidence="ECO:0007829|PDB:1TYG"
FT STRAND 39..41
FT /evidence="ECO:0007829|PDB:1TYG"
FT HELIX 43..45
FT /evidence="ECO:0007829|PDB:1TYG"
FT TURN 46..48
FT /evidence="ECO:0007829|PDB:1TYG"
FT STRAND 53..62
FT /evidence="ECO:0007829|PDB:1TYG"
SQ SEQUENCE 66 AA; 7626 MW; 476D61DCC98BAADE CRC64;
MLQLNGKDVK WKKDTGTIQD LLASYQLENK IVIVERNKEI IGKERYHEVE LCDRDVIEIV
HFVGGG
