ID   RMLA_NEIMB              Reviewed;         288 AA.
AC   P55255;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2000, sequence version 2.
DT   03-AUG-2022, entry version 114.
DE   RecName: Full=Glucose-1-phosphate thymidylyltransferase;
DE            EC=2.7.7.24;
DE   AltName: Full=dTDP-glucose pyrophosphorylase;
DE   AltName: Full=dTDP-glucose synthase;
GN   Name=rmlA1; Synonyms=rfbA1; OrderedLocusNames=NMB0062;
GN   and
GN   Name=rmlA2; Synonyms=rfbA2; OrderedLocusNames=NMB0080;
OS   Neisseria meningitidis serogroup B (strain MC58).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=122586;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=B1940 / Serogroup B;
RX   PubMed=8022265; DOI=10.1111/j.1365-2958.1994.tb00367.x;
RA   Hammerschmidt S., Birkholz C., Zaehringer U., Robertson B.D.,
RA   van Putten J.P.M., Ebeling O., Frosch M.;
RT   "Contribution of genes from the capsule gene complex (cps) to
RT   lipooligosaccharide biosynthesis and serum resistance in Neisseria
RT   meningitidis.";
RL   Mol. Microbiol. 11:885-896(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MC58;
RX   PubMed=10710307; DOI=10.1126/science.287.5459.1809;
RA   Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., Nelson K.E.,
RA   Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., Nelson W.C.,
RA   Gwinn M.L., DeBoy R.T., Peterson J.D., Hickey E.K., Haft D.H.,
RA   Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., Mason T.M.,
RA   Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., Cotton M.D.,
RA   Utterback T.R., Khouri H.M., Qin H., Vamathevan J.J., Gill J., Scarlato V.,
RA   Masignani V., Pizza M., Grandi G., Sun L., Smith H.O., Fraser C.M.,
RA   Moxon E.R., Rappuoli R., Venter J.C.;
RT   "Complete genome sequence of Neisseria meningitidis serogroup B strain
RT   MC58.";
RL   Science 287:1809-1815(2000).
CC   -!- FUNCTION: Catalyzes the formation of dTDP-glucose, from dTTP and
CC       glucose 1-phosphate, as well as its pyrophosphorolysis. {ECO:0000250}.
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   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the glucose-1-phosphate thymidylyltransferase
CC       family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAC37050.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; L09189; AAC37050.1; ALT_INIT; Genomic_DNA.
DR   EMBL; AE002098; AAF40530.1; -; Genomic_DNA.
DR   EMBL; AE002098; AAF40544.1; -; Genomic_DNA.
DR   PIR; B81240; B81240.
DR   RefSeq; NP_273126.1; NC_003112.2.
DR   RefSeq; NP_273143.1; NC_003112.2.
DR   RefSeq; WP_002224747.1; NC_003112.2.
DR   AlphaFoldDB; P55255; -.
DR   SMR; P55255; -.
DR   STRING; 122586.NMB0062; -.
DR   PaxDb; P55255; -.
DR   EnsemblBacteria; AAF40530; AAF40530; NMB0062.
DR   EnsemblBacteria; AAF40544; AAF40544; NMB0080.
DR   KEGG; nme:NMB0062; -.
DR   KEGG; nme:NMB0080; -.
DR   PATRIC; fig|122586.8.peg.115; -.
DR   HOGENOM; CLU_029499_9_0_4; -.
DR   OMA; FTWLDTG; -.
DR   Proteomes; UP000000425; 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.
DR   TIGRFAMs; TIGR01207; rmlA; 1.
PE   3: Inferred from homology;
KW   Magnesium; Metal-binding; Nucleotidyltransferase; Reference proteome;
KW   Transferase.
FT   CHAIN           1..288
FT                   /note="Glucose-1-phosphate thymidylyltransferase"
FT                   /id="PRO_0000207998"
FT   BINDING         108
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         223
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        125
FT                   /note="A -> R (in Ref. 1; AAC37050)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        198
FT                   /note="T -> S (in Ref. 1; AAC37050)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   288 AA;  32162 MW;  8A65B50B531F2907 CRC64;
     MKGIILAGGS GTRLYPITRG VSKQLLPVYD KPMIYYPLSV LMLAGIRDIL VITAPEDNAS
     FKRLLGDGSD FGISISYAVQ PSPDGLAQAF IIGEEFIGND NVCLVLGDNI FYGQSFTQTL
     KQAAAQTHGA TVFAYQVKNP ERFGVVEFNE NFRAVSIEEK PQRPKSDWAV TGLYFYDNRA
     VEFAKQLKPS ARGELEITDL NRMYLEDGSL SVQILGRGFA WLDTGTHESL HEAASFVQTV
     QNIQNLHIAC LEEIAWRNGW LSDEKLEELA RPMAKNQYGQ YLLRLLKK