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-OCT-2012, entry version 70.
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; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   MEDLINE=98044033; PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G.,
RA   Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S.,
RA   Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S.,
RA   Brouillet S., Bruschi C.V., Caldwell B., Capuano V., Carter N.M.,
RA   Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A.,
RA   Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T.,
RA   Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D.,
RA   Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N.,
RA   Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G.,
RA   Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A.,
RA   Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M.,
RA   Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M.,
RA   Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S.,
RA   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.,
RA   Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B.,
RA   Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R.,
RA   Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P.,
RA   Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H.,
RA   Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P.,
RA   Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F.,
RA   Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H.,
RA   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
RT   sulfur 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
RP   SUBUNIT.
RX   PubMed=15362849; DOI=10.1021/bi0488911;
RA   Settembre E.C., Dorrestein P.C., Zhai H., Chatterjee A.,
RA   McLafferty F.W., 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.
CC   -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis.
CC   -!- SUBUNIT: Forms heterodimers with thiG.
CC   -!- PTM: C-terminal thiocarboxylation occurs in 2 steps, it is first
CC       acyl-adenylated (-COAMP) by thiF, then thiocarboxylated (-COSH) by
CC       thiI (By similarity).
CC   -!- SIMILARITY: Belongs to the sulfur carrier protein ThiS family.
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DR   EMBL; AL009126; CAB13025.1; -; Genomic_DNA.
DR   PIR; C69845; C69845.
DR   RefSeq; NP_389050.1; NC_000964.3.
DR   PDB; 1TYG; X-ray; 3.15 A; B/G=1-66.
DR   PDBsum; 1TYG; -.
DR   ProteinModelPortal; O31617; -.
DR   SMR; O31617; 1-65.
DR   IntAct; O31617; 1.
DR   EnsemblBacteria; EBBACT00000001881; EBBACP00000001881; EBBACG00000001878.
DR   GeneID; 939811; -.
DR   GenomeReviews; AL009126_GR; BSU11680.
DR   KEGG; bsu:BSU11680; -.
DR   PATRIC; 18974053; VBIBacSub10457_1220.
DR   GenoList; BSU11680; -.
DR   eggNOG; COG2104; -.
DR   HOGENOM; HOG000248060; -.
DR   KO; K03154; -.
DR   OMA; RIIQKHE; -.
DR   ProtClustDB; CLSK887075; -.
DR   BioCyc; BSUB:BSU11680-MONOMER; -.
DR   UniPathway; UPA00060; -.
DR   EvolutionaryTrace; O31617; -.
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; G3DSA:3.10.20.30; Ferredoxin_fold; 1.
DR   InterPro; IPR012675; Beta-grasp_dom.
DR   InterPro; IPR016155; Mopterin_synth/thiamin_S_b.
DR   InterPro; IPR010035; Thi_S.
DR   InterPro; IPR003749; ThiS/MoaD.
DR   Pfam; PF02597; ThiS; 1.
DR   SUPFAM; SSF54285; Mo_synth/thiamin_syn_S_b-grasp; 1.
DR   TIGRFAMs; TIGR01683; thiS; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Complete proteome; Nucleotide-binding;
KW   Reference proteome; Thiamine biosynthesis.
FT   CHAIN         1     66       Sulfur carrier protein ThiS.
FT                                /FTId=PRO_0000391751.
FT   MOD_RES      66     66       1-thioglycine; alternate (By similarity).
FT   MOD_RES      66     66       Glycyl adenylate; alternate (By
FT                                similarity).
FT   STRAND        2      4
FT   STRAND        7      9
FT   STRAND       12     14
FT   HELIX        18     24
FT   STRAND       33     36
FT   STRAND       39     41
FT   HELIX        43     45
FT   TURN         46     48
FT   STRAND       53     62
SQ   SEQUENCE   66 AA;  7626 MW;  476D61DCC98BAADE CRC64;
     MLQLNGKDVK WKKDTGTIQD LLASYQLENK IVIVERNKEI IGKERYHEVE LCDRDVIEIV
     HFVGGG
//