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Database: UniProt
Entry: A0A0R2FCP3_9LACO
LinkDB: A0A0R2FCP3_9LACO
Original site: A0A0R2FCP3_9LACO 
ID   A0A0R2FCP3_9LACO        Unreviewed;       217 AA.
AC   A0A0R2FCP3;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   RecName: Full=thiamine diphosphokinase {ECO:0000256|ARBA:ARBA00013245};
DE            EC=2.7.6.2 {ECO:0000256|ARBA:ARBA00013245};
GN   ORFNames=FD14_GL002279 {ECO:0000313|EMBL:KRN26306.1};
OS   Secundilactobacillus similis DSM 23365 = JCM 2765.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Secundilactobacillus.
OX   NCBI_TaxID=1423804 {ECO:0000313|EMBL:KRN26306.1, ECO:0000313|Proteomes:UP000051442};
RN   [1] {ECO:0000313|EMBL:KRN26306.1, ECO:0000313|Proteomes:UP000051442}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 23365 {ECO:0000313|EMBL:KRN26306.1,
RC   ECO:0000313|Proteomes:UP000051442};
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:KRN26306.1}.
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DR   EMBL; AYZM01000037; KRN26306.1; -; Genomic_DNA.
DR   RefSeq; WP_054737258.1; NZ_BBAD01000086.1.
DR   AlphaFoldDB; A0A0R2FCP3; -.
DR   STRING; 1423804.FD14_GL002279; -.
DR   PATRIC; fig|1423804.4.peg.2471; -.
DR   OrthoDB; 9804377at2; -.
DR   Proteomes; UP000051442; 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:KRN26306.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051442};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          145..209
FT                   /note="Thiamin pyrophosphokinase thiamin-binding"
FT                   /evidence="ECO:0000259|SMART:SM00983"
SQ   SEQUENCE   217 AA;  24417 MW;  3A20CD8154288A99 CRC64;
     MTHLNLLVGG PTSEWPDQLA AGKVSGDWIG VDRGTLRLLK MGITPLVAIG DFDSLSADEL
     SLVKRSVTDI RQAIPEKDET DTELAITVAL KEYQSDRLDI YGATGGRLDH FLANLWLVLK
     PRYREFAPKI RFIDRGNTIT FYLPGEYELQ KEADKKYLAF VPLEKVDHLK LLDEKYRLAD
     ENVPYPISYA SNEFVGETGH FSFTSGLLAV IQSRDTH
//
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