ID A0A1A2BBU3_9MYCO Unreviewed; 393 AA.
AC A0A1A2BBU3;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE SubName: Full=Thiamine pyrophosphokinase {ECO:0000313|EMBL:OBF65907.1};
GN ORFNames=A5753_01035 {ECO:0000313|EMBL:OBF65907.1};
OS Mycobacterium sp. 852002-51971_SCH5477799-a.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=1834106 {ECO:0000313|EMBL:OBF65907.1, ECO:0000313|Proteomes:UP000091887};
RN [1] {ECO:0000313|EMBL:OBF65907.1, ECO:0000313|Proteomes:UP000091887}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=852002-51971_SCH5477799-a {ECO:0000313|EMBL:OBF65907.1,
RC ECO:0000313|Proteomes:UP000091887};
RA Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
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:OBF65907.1}.
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DR EMBL; LZIF01000075; OBF65907.1; -; Genomic_DNA.
DR RefSeq; WP_067125820.1; NZ_LZIF01000075.1.
DR AlphaFoldDB; A0A1A2BBU3; -.
DR STRING; 1834106.A5753_01035; -.
DR OrthoDB; 5169996at2; -.
DR Proteomes; UP000091887; 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:OBF65907.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 344..366
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 334..384
FT /note="SteA-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF12555"
SQ SEQUENCE 393 AA; 42287 MW; 5E1714401DC01565 CRC64;
MKMSGLLSRN PARPGLVGTA RVDRNIDRLL RRVCPGDIVV LDVLDLDRIT ADALVEADIA
AVVNASPSVS GRYPNMGPEV LVNNGVTLID EAGPDIFRKV KDGSKIRLHE GGVYVGDRRL
VRGTERTDHD IADLMREAKS GLSAHLEAFA GNTIEFIKSE SPLLIDGIGI PDVDVDLRRR
HVVIVADEPS AEEDLKSLKP FIKEYQPALI GVGTGADVLR KAGYRPQVIV GDPDQISTDA
LKCGAQVVLP ADADGHAPGL ERIQDLGVGA MTFPAAGSAI DLALLLADHH GAALLVTAGH
TANIETFFDR TRAHSNPSTF LTRLRVGEKV VDAKAVATLY RNHISAGAIA LLALTMLIAV
IVALWVSRTD GVVLHWVTDY WNHFCLTVQK WVT
//