ID F9UMY4_LACPL Unreviewed; 287 AA.
AC F9UMY4;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE RecName: Full=Glucose-1-phosphate thymidylyltransferase {ECO:0000256|ARBA:ARBA00012461, ECO:0000256|RuleBase:RU003706};
DE EC=2.7.7.24 {ECO:0000256|ARBA:ARBA00012461, ECO:0000256|RuleBase:RU003706};
GN Name=rfbA {ECO:0000313|EMBL:CCC78573.1};
GN OrderedLocusNames=lp_1186 {ECO:0000313|EMBL:CCC78573.1};
OS Lactiplantibacillus plantarum (strain ATCC BAA-793 / NCIMB 8826 / WCFS1)
OS (Lactobacillus plantarum).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lactiplantibacillus.
OX NCBI_TaxID=220668 {ECO:0000313|EMBL:CCC78573.1, ECO:0000313|Proteomes:UP000000432};
RN [1] {ECO:0000313|EMBL:CCC78573.1, ECO:0000313|Proteomes:UP000000432}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-793 / NCIMB 8826 / WCFS1
RC {ECO:0000313|Proteomes:UP000000432};
RX PubMed=12566566; DOI=10.1073/pnas.0337704100;
RA Kleerebezem M., Boekhorst J., van Kranenburg R., Molenaar D., Kuipers O.P.,
RA Leer R., Tarchini R., Peters S.A., Sandbrink H.M., Fiers M.W., Stiekema W.,
RA Lankhorst R.M., Bron P.A., Hoffer S.M., Groot M.N., Kerkhoven R.,
RA de Vries M., Ursing B., de Vos W.M., Siezen R.J.;
RT "Complete genome sequence of Lactobacillus plantarum WCFS1.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:1990-1995(2003).
RN [2] {ECO:0000313|EMBL:CCC78573.1, ECO:0000313|Proteomes:UP000000432}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-793 / NCIMB 8826 / WCFS1
RC {ECO:0000313|Proteomes:UP000000432};
RX PubMed=22156394; DOI=10.1128/JB.06275-11;
RA Siezen R.J., Francke C., Renckens B., Boekhorst J., Wels M.,
RA Kleerebezem M., van Hijum S.A.F.T.;
RT "Complete resequencing and reannotation of the Lactobacillus plantarum
RT WCFS1 genome.";
RL J. Bacteriol. 194:195-196(2012).
CC -!- FUNCTION: Catalyzes the formation of dTDP-glucose, from dTTP and
CC glucose 1-phosphate, as well as its pyrophosphorolysis.
CC {ECO:0000256|RuleBase:RU003706}.
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:0000256|ARBA:ARBA00001095,
CC ECO:0000256|RuleBase:RU003706};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SIMILARITY: Belongs to the glucose-1-phosphate thymidylyltransferase
CC family. {ECO:0000256|ARBA:ARBA00010480, ECO:0000256|RuleBase:RU003706}.
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DR EMBL; AL935263; CCC78573.1; -; Genomic_DNA.
DR RefSeq; WP_011101289.1; NC_004567.2.
DR RefSeq; YP_004889087.1; NC_004567.2.
DR AlphaFoldDB; F9UMY4; -.
DR STRING; 220668.lp_1186; -.
DR EnsemblBacteria; CCC78573; CCC78573; lp_1186.
DR KEGG; lpl:lp_1186; -.
DR PATRIC; fig|220668.9.peg.1004; -.
DR eggNOG; COG1209; Bacteria.
DR HOGENOM; CLU_029499_9_0_9; -.
DR OrthoDB; 9803871at2; -.
DR PhylomeDB; F9UMY4; -.
DR Proteomes; UP000000432; 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 InterPro; IPR005907; G1P_thy_trans_s.
DR InterPro; IPR005835; NTP_transferase_dom.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR NCBIfam; TIGR01207; rmlA; 1.
DR PANTHER; PTHR43532; GLUCOSE-1-PHOSPHATE THYMIDYLYLTRANSFERASE; 1.
DR PANTHER; PTHR43532:SF1; GLUCOSE-1-PHOSPHATE THYMIDYLYLTRANSFERASE 1; 1.
DR Pfam; PF00483; NTP_transferase; 1.
DR SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
PE 3: Inferred from homology;
KW Magnesium {ECO:0000256|RuleBase:RU003706};
KW Metal-binding {ECO:0000256|RuleBase:RU003706};
KW Nucleotidyltransferase {ECO:0000256|RuleBase:RU003706,
KW ECO:0000313|EMBL:CCC78573.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000432};
KW Transferase {ECO:0000256|RuleBase:RU003706, ECO:0000313|EMBL:CCC78573.1}.
FT DOMAIN 2..238
FT /note="Nucleotidyl transferase"
FT /evidence="ECO:0000259|Pfam:PF00483"
SQ SEQUENCE 287 AA; 31859 MW; C92EA4CA2F0D6BBB CRC64;
MKGIILAGGS GTRLYPVTKV TSKQLLPIYD KPMIYYPLST LMLSGIKDIL IISTSRDSNS
FKALLGDGSE LGIHIEYAIQ QEPNGLAEAF IIGKQFIGDD SVCLILGDNI FYGNGLSETL
QKAVRLKDGA IVYGYRVKDP ERFGVVSFDN KKNVISIEEK PTDPKSDFAV TGIYFFDNDV
VSIAESIKPS ARGELEITDI NNVYLKRKKL KVELLSRGFA WLDTGTHESL QDASSFIQTV
ERRQNILIAS IEEVAFRMGY IDSKQLQSLA APLHKTRYGQ YLASLVE
//
