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Database: UniProt
Entry: A0A162MGN0_9FIRM
LinkDB: A0A162MGN0_9FIRM
Original site: A0A162MGN0_9FIRM 
ID   A0A162MGN0_9FIRM        Unreviewed;       374 AA.
AC   A0A162MGN0;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KYO65805.1};
GN   ORFNames=ATZ99_14430 {ECO:0000313|EMBL:KYO65805.1};
OS   Thermovenabulum gondwanense.
OC   Bacteria; Bacillota; Clostridia; Thermosediminibacterales;
OC   Thermosediminibacteraceae; Thermovenabulum.
OX   NCBI_TaxID=520767 {ECO:0000313|EMBL:KYO65805.1, ECO:0000313|Proteomes:UP000075737};
RN   [1] {ECO:0000313|EMBL:KYO65805.1, ECO:0000313|Proteomes:UP000075737}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=R270 {ECO:0000313|EMBL:KYO65805.1,
RC   ECO:0000313|Proteomes:UP000075737};
RA   Patel B.K.;
RT   "Draft genome of Thermovenabulum gondwanense isolated from a red
RT   thermophilic microbial mat colonisisng an outflow channel of a bore well.";
RL   Submitted (DEC-2015) 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:KYO65805.1}.
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DR   EMBL; LOHZ01000032; KYO65805.1; -; Genomic_DNA.
DR   RefSeq; WP_068748563.1; NZ_LOHZ01000032.1.
DR   AlphaFoldDB; A0A162MGN0; -.
DR   STRING; 520767.ATZ99_14430; -.
DR   PATRIC; fig|520767.4.peg.1547; -.
DR   OrthoDB; 9804377at2; -.
DR   Proteomes; UP000075737; 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   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}; Membrane {ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000075737};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        334..364
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          191..225
FT                   /note="Thiamin pyrophosphokinase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF04263"
FT   DOMAIN          319..370
FT                   /note="SteA-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF12555"
SQ   SEQUENCE   374 AA;  41725 MW;  9837A029F5D71ECB CRC64;
     MICGRACVGK KTKILVNKIR PGEIAVIFHK DIDELAASFL LEKKAKAVIN FETSCSGKYY
     NKGPETLIKA KIPLIDVISP YQGEIKEGDI VKIKDNGDIF VNDKFFSKGK FWDLDSLNKC
     KNLAKQNIDK HLLNFIENTI DYIEKNRDII YSNYSVPDVN VDIKGKHVLI VIRGHEYKED
     LSILRSYIEE MKPVLIGVDG GADAILEFGY TPDIIIGDMD SISDEGLLCG AEIIVHAYPD
     GKAPGLERIK NLGVKYSIFS VTGTSEDAAF LLAFEKGADL IVAVGTHTSM LDFLEKGRKG
     MASTLLVRLK MGHILIDAKG VNKLYKRKEE NISIILPLVL TGIIPIFILF LNSPILSHVF
     KLIYLKLKLV LMMF
//
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