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Database: UniProt
Entry: A0A1A0M5P8_9MYCO
LinkDB: A0A1A0M5P8_9MYCO
Original site: A0A1A0M5P8_9MYCO 
ID   A0A1A0M5P8_9MYCO        Unreviewed;       393 AA.
AC   A0A1A0M5P8;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   SubName: Full=Thiamine pyrophosphokinase {ECO:0000313|EMBL:OBA80715.1};
GN   ORFNames=A9W99_15665 {ECO:0000313|EMBL:OBA80715.1};
OS   Mycobacterium sp. 1164966.3.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=1856861 {ECO:0000313|EMBL:OBA80715.1, ECO:0000313|Proteomes:UP000092060};
RN   [1] {ECO:0000313|Proteomes:UP000092060}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1164966.3 {ECO:0000313|Proteomes:UP000092060};
RA   Sutton G., Brinkac L., Sanka R., Adams M., Lau E., Garcia-Basteiro A.,
RA   Lopez-Varela E., Palencia S.;
RL   Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
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:OBA80715.1}.
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DR   EMBL; LZSG01000040; OBA80715.1; -; Genomic_DNA.
DR   RefSeq; WP_067378549.1; NZ_LZSG01000040.1.
DR   AlphaFoldDB; A0A1A0M5P8; -.
DR   STRING; 1856861.A9W99_15665; -.
DR   OrthoDB; 5169996at2; -.
DR   Proteomes; UP000092060; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
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   InterPro; IPR047795; Put_SteA-like.
DR   InterPro; IPR022215; SteA-like_C.
DR   InterPro; IPR036759; TPK_catalytic_sf.
DR   NCBIfam; NF040608; division_SteA; 1.
DR   Pfam; PF12555; SteA-like_C; 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:OBA80715.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000092060};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        348..366
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          334..382
FT                   /note="SteA-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF12555"
SQ   SEQUENCE   393 AA;  42306 MW;  9247B8EB6115ED7F CRC64;
     MRMSTLLTRN TTRPGIVGTA RVDRNIDRLL RRVCPGDIVV LDILDLDRIT ADALVEADIA
     AVVNASPSVS GRYPNLGPEV LVNNGVTLID ETGPEVFKKV KDGAKIRLHE GGVYAGDRRL
     VRGTQRTDHD IADLMREAKG GLAAHLEAFA GNTIEFIKSE SPLLIDGIGI PDIDVDLRRR
     HVVIVADEPT AADDLRALKP FIKEYQPVLV GVGTGADVLR KAGYRPQIIV GDPDQISTDA
     LKSGAQVVLP ADADGHAPGL ERIQDLGVGA MTFPAAGSAV DLALLLADHH GAALLVTAGH
     TANIETFFDR TRTQSNPSTF LTRLRVGEKL VDARAVATLY RNHMSGGAIA LLALTMLIAV
     IVALWVSRTD ATVLHFVVDY WNRSSFWVQH LVS
//
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