THIF_BACSU
ID THIF_BACSU Reviewed; 336 AA.
AC O31619;
DT 02-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Sulfur carrier protein ThiS adenylyltransferase;
DE EC=2.7.7.73;
GN Name=thiF; Synonyms=yjbU; OrderedLocusNames=BSU11700;
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).
CC -!- FUNCTION: Catalyzes the adenylation by ATP of the carboxyl group of the
CC C-terminal glycine of sulfur carrier protein ThiS. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[sulfur-carrier protein ThiS]-C-terminal Gly-Gly + ATP + H(+)
CC = [sulfur-carrier protein ThiS]-C-terminal Gly-Gly-AMP + diphosphate;
CC Xref=Rhea:RHEA:43344, Rhea:RHEA-COMP:12909, Rhea:RHEA-COMP:12910,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:90618, ChEBI:CHEBI:90778; EC=2.7.7.73;
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis.
CC -!- SIMILARITY: Belongs to the HesA/MoeB/ThiF family. {ECO:0000305}.
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DR EMBL; AL009126; CAB13027.1; -; Genomic_DNA.
DR PIR; E69845; E69845.
DR RefSeq; NP_389052.1; NC_000964.3.
DR RefSeq; WP_003245868.1; NZ_JNCM01000035.1.
DR AlphaFoldDB; O31619; -.
DR SMR; O31619; -.
DR IntAct; O31619; 1.
DR MINT; O31619; -.
DR STRING; 224308.BSU11700; -.
DR PaxDb; O31619; -.
DR PRIDE; O31619; -.
DR EnsemblBacteria; CAB13027; CAB13027; BSU_11700.
DR GeneID; 939816; -.
DR KEGG; bsu:BSU11700; -.
DR PATRIC; fig|224308.179.peg.1259; -.
DR eggNOG; COG0476; Bacteria.
DR InParanoid; O31619; -.
DR OMA; SAKWKLE; -.
DR PhylomeDB; O31619; -.
DR BioCyc; BSUB:BSU11700-MON; -.
DR BioCyc; MetaCyc:BSU11700-MON; -.
DR BRENDA; 2.7.7.73; 658.
DR UniPathway; UPA00060; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016779; F:nucleotidyltransferase activity; IBA:GO_Central.
DR GO; GO:0008641; F:ubiquitin-like modifier activating enzyme activity; IEA:InterPro.
DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway.
DR InterPro; IPR045886; ThiF/MoeB/HesA.
DR InterPro; IPR000594; ThiF_NAD_FAD-bd.
DR InterPro; IPR035985; Ubiquitin-activating_enz.
DR PANTHER; PTHR10953; PTHR10953; 1.
DR Pfam; PF00899; ThiF; 1.
DR SUPFAM; SSF69572; SSF69572; 1.
PE 3: Inferred from homology;
KW ATP-binding; Metal-binding; Nucleotide-binding; Nucleotidyltransferase;
KW Reference proteome; Thiamine biosynthesis; Transferase; Zinc.
FT CHAIN 1..336
FT /note="Sulfur carrier protein ThiS adenylyltransferase"
FT /id="PRO_0000391752"
FT ACT_SITE 181
FT /note="Glycyl persulfide ester intermediate"
FT /evidence="ECO:0000250"
FT BINDING 7
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 34
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 55
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 66
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 81
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 105
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 125..129
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 166
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 169
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 238
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 241
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
SQ SEQUENCE 336 AA; 36400 MW; 5FA4F7AE438625C5 CRC64;
MTGRYSRQEL FAPIGPSGQK KLKEARAVII GAGALGTASA EMLVRAGVGS VKIADRDYVE
WSNLQRQQLY TEDDVKKEMP KAAAAERRLR SINSDVDVTG LVMDVTAENI FELIRDASII
VDAADNFETR LIVNDAAVKE GIPFLYGACV GSYGLTFTVV PGSTPCLHCL LDALPIGGAT
CDTAGIISPA VLQVAVFQVT DALKLLTGEE CEPVLRSFDL WKNERSEVRA ASLKHDACPS
CGTKDFPFLS YENQTKAAVL CGRNTVQIRS SITKEADLEA LAGQLRQAGL EVAANPYLIS
CRSDDMKMVL FRDGRALIHG TNDIARAKSI YHKWIG
