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Database: UniProt
Entry: O31617
LinkDB: O31617
Original site: O31617 
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   02-JUN-2021, entry version 109.
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}.
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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   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; DVIEIVH; -.
DR   PhylomeDB; O31617; -.
DR   BioCyc; BSUB:BSU11680-MONOMER; -.
DR   BioCyc; MetaCyc:BSU11680-MONOMER; -.
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
//
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