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Database: UniProt
Entry: E0DEQ1_9CORY
LinkDB: E0DEQ1_9CORY
Original site: E0DEQ1_9CORY 
ID   E0DEQ1_9CORY            Unreviewed;       407 AA.
AC   E0DEQ1;
DT   02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2010, sequence version 1.
DT   24-JAN-2024, entry version 33.
DE   RecName: Full=SteA-like C-terminal domain-containing protein {ECO:0000259|Pfam:PF12555};
GN   ORFNames=HMPREF0299_6336 {ECO:0000313|EMBL:EFM48852.1};
OS   Corynebacterium matruchotii ATCC 14266.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC   Corynebacteriaceae; Corynebacterium.
OX   NCBI_TaxID=553207 {ECO:0000313|EMBL:EFM48852.1, ECO:0000313|Proteomes:UP000004218};
RN   [1] {ECO:0000313|EMBL:EFM48852.1, ECO:0000313|Proteomes:UP000004218}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 14266 {ECO:0000313|EMBL:EFM48852.1,
RC   ECO:0000313|Proteomes:UP000004218};
RA   Harkins D.M., Madupu R., Durkin A.S., Torralba M., Methe B., Sutton G.G.,
RA   Nelson K.E.;
RL   Submitted (AUG-2010) 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:EFM48852.1}.
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DR   EMBL; ACSH02000005; EFM48852.1; -; Genomic_DNA.
DR   AlphaFoldDB; E0DEQ1; -.
DR   STRING; 553207.HMPREF0299_6336; -.
DR   eggNOG; COG4825; Bacteria.
DR   OrthoDB; 5169996at2; -.
DR   Proteomes; UP000004218; 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   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:UP000004218};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        363..385
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          349..401
FT                   /note="SteA-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF12555"
SQ   SEQUENCE   407 AA;  42732 MW;  070BC01C95A84481 CRC64;
     MAFPGLWGVV GENGGMSLFS RTVDLPGVQA VMRDLSVRGK KGYKKLGAGD IAVIDAPDVS
     RAVAQWLIDS QVVAVVNTGE FSTGAIPNFG PQMMLDAGIM LVEDVGDGVL VGLKDGKKGR
     LTESGELFCG DKLLGSGVVV TPADAEERFL VAQQRLVDYM EAFFGNTIQF IHSESPLLID
     GLGIPEVGDA LRDRKVLVVS PGRYFRSELK ELRNFIREFS PVIIAVDEAA DALVELGYGV
     DFIVGDPGGI GAAALRSGAR VVVPAGPDGH VVGLERIQDL GVGALTFPSA VENATDLALF
     LADFHQAELV VNVGASVTLD SLFAQSGYAS PSALLSRMKL GPRLVDASAI ATLYNIRSGK
     NIAFLWGVMG VLVALATVIM VAGLAGEGSF MVNVVDTWNN IIGRVAS
//
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