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Database: UniProt
Entry: A0A0M4H5J3_9ACTO
LinkDB: A0A0M4H5J3_9ACTO
Original site: A0A0M4H5J3_9ACTO 
ID   A0A0M4H5J3_9ACTO        Unreviewed;       408 AA.
AC   A0A0M4H5J3;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   SubName: Full=Thiamin pyrophosphokinase {ECO:0000313|EMBL:ALC99415.1};
GN   ORFNames=AM609_07795 {ECO:0000313|EMBL:ALC99415.1};
OS   Actinomyces sp. oral taxon 414.
OC   Bacteria; Actinomycetota; Actinomycetes; Actinomycetales; Actinomycetaceae;
OC   Actinomyces.
OX   NCBI_TaxID=712122 {ECO:0000313|EMBL:ALC99415.1, ECO:0000313|Proteomes:UP000061022};
RN   [1] {ECO:0000313|Proteomes:UP000061022}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F0588 {ECO:0000313|Proteomes:UP000061022};
RA   Holder M.E., Ajami N.J., Petrosino J.F.;
RL   Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; CP012590; ALC99415.1; -; Genomic_DNA.
DR   RefSeq; WP_053586822.1; NZ_CP012590.1.
DR   AlphaFoldDB; A0A0M4H5J3; -.
DR   STRING; 712122.AM609_07795; -.
DR   KEGG; acq:AM609_07795; -.
DR   PATRIC; fig|712122.3.peg.1756; -.
DR   OrthoDB; 5169996at2; -.
DR   Proteomes; UP000061022; Chromosome.
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   Gene3D; 3.40.50.10240; Thiamin pyrophosphokinase, catalytic domain; 1.
DR   InterPro; IPR047795; Put_SteA-like.
DR   InterPro; IPR022215; SteA-like_C.
DR   InterPro; IPR007371; TPK_catalytic.
DR   InterPro; IPR036759; TPK_catalytic_sf.
DR   NCBIfam; NF040608; division_SteA; 1.
DR   Pfam; PF12555; SteA-like_C; 1.
DR   Pfam; PF04263; TPK_catalytic; 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:ALC99415.1};
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        354..373
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          214..247
FT                   /note="Thiamin pyrophosphokinase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF04263"
FT   DOMAIN          341..391
FT                   /note="SteA-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF12555"
SQ   SEQUENCE   408 AA;  43349 MW;  EBECFD981B0EB0F4 CRC64;
     MRNPFRKPSA PEPGRPVGVV RVDARTKKLA KRLRAGEFAV IDHADLDRVA AESLVECRPA
     AVLNAAPSIS GRYPNLGPGI LIEAGVPLID DLGPDIMRLK EGQRVVLDLA EDSPDRGSVR
     PVGSDEILAQ GTVQTAASVA TAMEEAKAGL AVQLEAFAAN TMEYMRGERD LLLNGVGMPD
     VRTDMNGRHV LVVVRGYSYK EDLRALKPYI REYKPVIIGV DGGADAVLEA GFKPDMIVGD
     MDSVSDRALG CGAEVVVHAY RDGRAPGLKR VEDLGVEHLV FAATGTSEDV AMLLADAAGA
     ELIVALGTHA TLLEFLDKGR AGMSSTFLTR LKVGGRLIDA KGVSRLYRTR ISGWHLMVLA
     LAGLIALFVA LAATPAGQTL LGLSGAMWDD IINFFRSILG LAPKTPSV
//
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