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
//