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Database: UniProt
Entry: A0A2T4Z9J7_9BACL
LinkDB: A0A2T4Z9J7_9BACL
Original site: A0A2T4Z9J7_9BACL 
ID   A0A2T4Z9J7_9BACL        Unreviewed;       386 AA.
AC   A0A2T4Z9J7;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   24-JAN-2024, entry version 15.
DE   SubName: Full=Putative membrane-anchored protein {ECO:0000313|EMBL:PTM58545.1};
GN   ORFNames=C8J48_1130 {ECO:0000313|EMBL:PTM58545.1};
OS   Desmospora activa DSM 45169.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Thermoactinomycetaceae;
OC   Desmospora.
OX   NCBI_TaxID=1121389 {ECO:0000313|EMBL:PTM58545.1, ECO:0000313|Proteomes:UP000241639};
RN   [1] {ECO:0000313|EMBL:PTM58545.1, ECO:0000313|Proteomes:UP000241639}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 45169 {ECO:0000313|EMBL:PTM58545.1,
RC   ECO:0000313|Proteomes:UP000241639};
RA   Goeker M.;
RT   "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT   (KMG-II): from individual species to whole genera.";
RL   Submitted (APR-2018) 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:PTM58545.1}.
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DR   EMBL; PZZP01000001; PTM58545.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2T4Z9J7; -.
DR   Proteomes; UP000241639; 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:UP000241639};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        348..366
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          207..247
FT                   /note="Thiamin pyrophosphokinase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF04263"
FT   DOMAIN          334..370
FT                   /note="SteA-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF12555"
SQ   SEQUENCE   386 AA;  42828 MW;  D74C0428BCE2BE36 CRC64;
     MGDWWKRWRK KGDLSIQGRV MVDRRTKRLL ARISPGEIAV IDHRDLDEVA AMGLVGAGVA
     AVVNVSASIS GRYPAQGCRL LLEAGIPVLD EVGEQAIQRL ADGDEVRIEG KLLRSVQEDW
     VATGSRLTWQ HWREKMAEAH QGFEQTLQPF IENTLNYAYR EREWVTQPLS LPPLRQSWRG
     RDVVVVVRGP GFAEDLYALR TFIREADPFL MAVDGGADAL LKYGWTPHLI LGDMDSISDQ
     ALLQAEELVV HAYSDGRAPG LERVERLGLT AHLLPSPGTS EDVALLAAFE GGAESIVAVG
     THSHMVDFLE KGREGMASTL LARIKMGARL VDAKGVSRLY RPRHPAKGVA VLTLASVMPV
     AAWLWVHPQL FETGRLFWTV LQIWLT
//
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