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Database: UniProt
Entry: I0RZF0_MYCXE
LinkDB: I0RZF0_MYCXE
Original site: I0RZF0_MYCXE 
ID   I0RZF0_MYCXE            Unreviewed;       393 AA.
AC   I0RZF0;
DT   13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2012, sequence version 1.
DT   24-JAN-2024, entry version 29.
DE   RecName: Full=SteA-like C-terminal domain-containing protein {ECO:0000259|Pfam:PF12555};
GN   ORFNames=MXEN_03954 {ECO:0000313|EMBL:EID16503.1};
OS   Mycobacterium xenopi RIVM700367.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=1150591 {ECO:0000313|EMBL:EID16503.1, ECO:0000313|Proteomes:UP000003584};
RN   [1] {ECO:0000313|EMBL:EID16503.1, ECO:0000313|Proteomes:UP000003584}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RIVM700367 {ECO:0000313|EMBL:EID16503.1,
RC   ECO:0000313|Proteomes:UP000003584};
RX   PubMed=22628510; DOI=10.1128/JB.00482-12;
RA   Abdallah A.M., Rashid M., Adroub S.A., Elabdalaoui H., Ali S.,
RA   van Soolingen D., Bitter W., Pain A.;
RT   "Complete Genome Sequence of Mycobacterium xenopi Type Strain RIVM700367.";
RL   J. Bacteriol. 194:3282-3283(2012).
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:EID16503.1}.
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DR   EMBL; AJFI01000023; EID16503.1; -; Genomic_DNA.
DR   RefSeq; WP_003919520.1; NZ_AJFI01000023.1.
DR   AlphaFoldDB; I0RZF0; -.
DR   PATRIC; fig|1150591.3.peg.796; -.
DR   OrthoDB; 5169996at2; -.
DR   Proteomes; UP000003584; 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:UP000003584};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        348..367
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          334..384
FT                   /note="SteA-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF12555"
SQ   SEQUENCE   393 AA;  42115 MW;  FAC67CC468564117 CRC64;
     MRMSALLSRN ADRPGVVGTA RVDRDIDRLL RRVGPGDIVV LDVLDLDRVT ADALVEADIA
     GVVNASPSVS GRYPNLGPEV LVANGVTLID ETGPEVFKKV KDGAKVRLYN GGVYSGDRRL
     IRGTERTDHD IADLMHEAKS GLVAHLEAFA GNTIEFIRSE SPLLIDGIGI PDIDVDLRRR
     HVVVVSDEPG AADDLKALKP FIKEYQPVLV GVGAGADVLR KAGYRPQIIV GDPEQMSAEV
     LKCGAQVVLP ADADGHAPGL ERIQDLGVGA MTFPAAGSAT DLALLLADHH GAALLVTAGH
     TANIETFFDR TRVNSNPSTF LTRLRVGEKL VDAKAVATLY RSHMSGGAVA LLVLTMLIAV
     IAVLWVSRAD AAVMHWVVEY WNRFSVWVQG RIT
//
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