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Database: UniProt
Entry: A0A0R2D1F9_9LACO
LinkDB: A0A0R2D1F9_9LACO
Original site: A0A0R2D1F9_9LACO 
ID   A0A0R2D1F9_9LACO        Unreviewed;       218 AA.
AC   A0A0R2D1F9;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   RecName: Full=thiamine diphosphokinase {ECO:0000256|ARBA:ARBA00013245};
DE            EC=2.7.6.2 {ECO:0000256|ARBA:ARBA00013245};
GN   ORFNames=FC56_GL000604 {ECO:0000313|EMBL:KRM93884.1};
OS   Lentilactobacillus senioris DSM 24302 = JCM 17472.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lentilactobacillus.
OX   NCBI_TaxID=1423802 {ECO:0000313|EMBL:KRM93884.1, ECO:0000313|Proteomes:UP000051256};
RN   [1] {ECO:0000313|EMBL:KRM93884.1, ECO:0000313|Proteomes:UP000051256}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 24302 {ECO:0000313|EMBL:KRM93884.1,
RC   ECO:0000313|Proteomes:UP000051256};
RX   PubMed=26415554; DOI=10.1038/ncomms9322;
RA   Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA   Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA   Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA   Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA   de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA   Zhang H., O'Toole P.W.;
RT   "Expanding the biotechnology potential of lactobacilli through comparative
RT   genomics of 213 strains and associated genera.";
RL   Nat. Commun. 6:8322-8322(2015).
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KRM93884.1}.
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DR   EMBL; AYZR01000008; KRM93884.1; -; Genomic_DNA.
DR   RefSeq; WP_054669777.1; NZ_BBCR01000002.1.
DR   AlphaFoldDB; A0A0R2D1F9; -.
DR   STRING; 1423802.FC56_GL000604; -.
DR   PATRIC; fig|1423802.4.peg.613; -.
DR   Proteomes; UP000051256; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0030975; F:thiamine binding; IEA:InterPro.
DR   GO; GO:0004788; F:thiamine diphosphokinase activity; IEA:InterPro.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:InterPro.
DR   GO; GO:0006772; P:thiamine metabolic process; IEA:InterPro.
DR   CDD; cd07995; TPK; 1.
DR   Gene3D; 3.40.50.10240; Thiamin pyrophosphokinase, catalytic domain; 1.
DR   InterPro; IPR006282; Thi_PPkinase.
DR   InterPro; IPR007373; Thiamin_PyroPKinase_B1-bd.
DR   InterPro; IPR007371; TPK_catalytic.
DR   InterPro; IPR036759; TPK_catalytic_sf.
DR   NCBIfam; TIGR01378; thi_PPkinase; 1.
DR   PANTHER; PTHR41299; THIAMINE PYROPHOSPHOKINASE; 1.
DR   PANTHER; PTHR41299:SF1; THIAMINE PYROPHOSPHOKINASE; 1.
DR   Pfam; PF04265; TPK_B1_binding; 1.
DR   Pfam; PF04263; TPK_catalytic; 1.
DR   SMART; SM00983; TPK_B1_binding; 1.
DR   SUPFAM; SSF63999; Thiamin pyrophosphokinase, catalytic domain; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:KRM93884.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051256};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          146..209
FT                   /note="Thiamin pyrophosphokinase thiamin-binding"
FT                   /evidence="ECO:0000259|SMART:SM00983"
SQ   SEQUENCE   218 AA;  24717 MW;  058D66385C49DA4F CRC64;
     MTIKLNLLVG GPQELWPQSL LDNRIQGDWI GIDRGNLRLI KLGIDPLVAI GDFDSMSDDE
     LAIVKEHVTD IRQSIPEKDD TDTQLGLLVA LNEFHADQID IYGATGGRID HFLANLWLVL
     EPRFRKNAPK IRMIDRQNTI SFYLPGNYQI TKEVDKKYLA FVPLTPVTNL TLNDEKYRLT
     NFTANRPISF ASNEFVGEVG HFSFDSGVVC VIQSKDWQ
//
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