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Database: UniProt
Entry: A0A0F6R1N8_9CORY
LinkDB: A0A0F6R1N8_9CORY
Original site: A0A0F6R1N8_9CORY 
ID   A0A0F6R1N8_9CORY        Unreviewed;       394 AA.
AC   A0A0F6R1N8;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   SubName: Full=Putative membrane-anchored protein {ECO:0000313|EMBL:AKE41153.1};
GN   ORFNames=UL82_04870 {ECO:0000313|EMBL:AKE41153.1};
OS   Corynebacterium kutscheri.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC   Corynebacteriaceae; Corynebacterium.
OX   NCBI_TaxID=35755 {ECO:0000313|EMBL:AKE41153.1, ECO:0000313|Proteomes:UP000033457};
RN   [1] {ECO:0000313|EMBL:AKE41153.1, ECO:0000313|Proteomes:UP000033457}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 20755 {ECO:0000313|EMBL:AKE41153.1,
RC   ECO:0000313|Proteomes:UP000033457};
RX   PubMed=26021937;
RA   Ruckert C., Albersmeier A., Winkler A., Tauch A.;
RT   "Complete Genome Sequence of Corynebacterium kutscheri DSM 20755, a
RT   Corynebacterial Type Strain with Remarkably Low G+C Content of Chromosomal
RT   DNA.";
RL   Genome Announc. 3:e00571-15(2015).
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DR   EMBL; CP011312; AKE41153.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0F6R1N8; -.
DR   STRING; 35755.UL82_04870; -.
DR   KEGG; cku:UL82_04870; -.
DR   HOGENOM; CLU_046690_0_0_11; -.
DR   Proteomes; UP000033457; 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   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}; Membrane {ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000033457};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        347..367
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          336..386
FT                   /note="SteA-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF12555"
SQ   SEQUENCE   394 AA;  41594 MW;  96EE0A13FB81438E CRC64;
     MSLFSRASEL PGLSAPLRDC RDNAKGFKRL SEGDIAVIDQ ADVSRGLAQK LIDAHPAAVI
     NAGQFSTGII PNFGPQMLLD EGIILVEGVG EEVWNGFKDG KKARLTDEGQ LYYGDKMVVA
     GVVVTTESAE QNFAEAQRSL VDHMEAYFGN SIQFIHSEAP LLIDGLGIPD IGSTIEGRKV
     LVVSPGMGHR SQMKQLRNFI REFEPAIIGV DGAADTLVEL GYKPDLIVGN PAGIGSDALR
     SGARVVLPAD PDGHATGLER IQDLGIAAMT FPAAVDSATD LALLLADYHG AQLIVNAGAP
     LNLAGIFSGG EQANPSSLIS RAKVGTKLVD AQVIGDLYTI RTVGNLAWLW AVLGIFVACA
     VIVLIAGTTG SGSFSENLID TWNNIALWFQ GLFS
//
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