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Database: UniProt
Entry: A0A1A2BBU3_9MYCO
LinkDB: A0A1A2BBU3_9MYCO
Original site: A0A1A2BBU3_9MYCO 
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
//
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