ID   RMLA_BACSU              Reviewed;         246 AA.
AC   P39629;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   03-AUG-2022, entry version 112.
DE   RecName: Full=Glucose-1-phosphate thymidylyltransferase;
DE            EC=2.7.7.24;
DE   AltName: Full=Spore coat polysaccharide biosynthesis protein SpsI;
DE   AltName: Full=dTDP-glucose pyrophosphorylase;
DE   AltName: Full=dTDP-glucose synthase;
GN   Name=rmlA; Synonyms=spsI; OrderedLocusNames=BSU37840; ORFNames=ipa-71d;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=7934828; DOI=10.1111/j.1365-2958.1993.tb01963.x;
RA   Glaser P., Kunst F., Arnaud M., Coudart M.P., Gonzales W., Hullo M.-F.,
RA   Ionescu M., Lubochinsky B., Marcelino L., Moszer I., Presecan E.,
RA   Santana M., Schneider E., Schweizer J., Vertes A., Rapoport G., Danchin A.;
RT   "Bacillus subtilis genome project: cloning and sequencing of the 97 kb
RT   region from 325 degrees to 333 degrees.";
RL   Mol. Microbiol. 10:371-384(1993).
RN   [2]
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   [3]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=22960854; DOI=10.1038/nchembio.1063;
RA   Plata G., Fuhrer T., Sauer U., Vitkup D.;
RT   "Global probabilistic annotation of metabolic networks enables enzyme
RT   discovery.";
RL   Nat. Chem. Biol. 8:848-854(2012).
CC   -!- FUNCTION: Catalyzes the formation of dTDP-glucose, from dTTP and
CC       glucose 1-phosphate, as well as its pyrophosphorolysis.
CC       {ECO:0000269|PubMed:22960854}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=alpha-D-glucose 1-phosphate + dTTP + H(+) = diphosphate +
CC         dTDP-alpha-D-glucose; Xref=Rhea:RHEA:15225, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:37568, ChEBI:CHEBI:57477,
CC         ChEBI:CHEBI:58601; EC=2.7.7.24;
CC         Evidence={ECO:0000269|PubMed:22960854};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250};
CC   -!- PATHWAY: Spore coat biogenesis; spore coat polysaccharide biosynthesis.
CC   -!- SIMILARITY: Belongs to the glucose-1-phosphate thymidylyltransferase
CC       family. {ECO:0000305}.
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DR   EMBL; X73124; CAA51627.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB15810.1; -; Genomic_DNA.
DR   PIR; S39726; S39726.
DR   RefSeq; NP_391663.1; NC_000964.3.
DR   RefSeq; WP_003243368.1; NZ_JNCM01000034.1.
DR   AlphaFoldDB; P39629; -.
DR   SMR; P39629; -.
DR   STRING; 224308.BSU37840; -.
DR   PaxDb; P39629; -.
DR   PRIDE; P39629; -.
DR   EnsemblBacteria; CAB15810; CAB15810; BSU_37840.
DR   GeneID; 937229; -.
DR   KEGG; bsu:BSU37840; -.
DR   PATRIC; fig|224308.179.peg.4097; -.
DR   eggNOG; COG1209; Bacteria.
DR   InParanoid; P39629; -.
DR   OMA; PFIMYLG; -.
DR   PhylomeDB; P39629; -.
DR   BioCyc; BSUB:BSU37840-MON; -.
DR   UniPathway; UPA00953; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0008879; F:glucose-1-phosphate thymidylyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0045226; P:extracellular polysaccharide biosynthetic process; IEA:InterPro.
DR   CDD; cd02538; G1P_TT_short; 1.
DR   Gene3D; 3.90.550.10; -; 1.
DR   InterPro; IPR005907; G1P_thy_trans_s.
DR   InterPro; IPR005835; NTP_transferase_dom.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   PANTHER; PTHR43532; PTHR43532; 1.
DR   Pfam; PF00483; NTP_transferase; 1.
DR   SUPFAM; SSF53448; SSF53448; 1.
PE   1: Evidence at protein level;
KW   Magnesium; Metal-binding; Nucleotidyltransferase; Reference proteome;
KW   Transferase.
FT   CHAIN           1..246
FT                   /note="Glucose-1-phosphate thymidylyltransferase"
FT                   /id="PRO_0000208007"
FT   BINDING         108
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         221
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   246 AA;  27773 MW;  4348B12FF9347D6D CRC64;
     MKGVILAGGN GSRLMPLTKA VNKHLLPVGP YPMIYWSIMK LQEAGIKDIL LISQKEHMPQ
     FYKLLGNGEE LGVTITYQVQ PAASGISDGL SYAKRFTKKE SFILLLGDNI FEDSLKPYTE
     RFEQQGKGAK VLLKEVDDPE RFGIAEIDEK NKRIRSIIEK PEQPPTNLCV TGIYMYDAEV
     FSYIEQISPS KRGELEITDV NNLYIENSQL TYDVLSGWWV DAGTHESLYL ASQLVHQALR
     KGQDEK