ID A0A0C2JRM9_9ACTN Unreviewed; 394 AA.
AC A0A0C2JRM9;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE SubName: Full=Thiamin pyrophosphokinase {ECO:0000313|EMBL:KIH99477.1};
GN ORFNames=LP52_07150 {ECO:0000313|EMBL:KIH99477.1};
OS Streptomonospora alba.
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Nocardiopsaceae; Streptomonospora.
OX NCBI_TaxID=183763 {ECO:0000313|EMBL:KIH99477.1, ECO:0000313|Proteomes:UP000031675};
RN [1] {ECO:0000313|Proteomes:UP000031675}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YIM 90003 {ECO:0000313|Proteomes:UP000031675};
RX PubMed=25601074; DOI=10.1016/j.chembiol.2014.11.017;
RA Metelev M., Tietz J.I., Melby J.O., Blair P.M., Zhu L., Livnat I.,
RA Severinov K., Mitchell D.A.;
RT "Structure, bioactivity, and resistance mechanism of streptomonomicin, an
RT unusual lasso Peptide from an understudied halophilic actinomycete.";
RL Chem. Biol. 22:241-250(2015).
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:KIH99477.1}.
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DR EMBL; JROO01000011; KIH99477.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0C2JRM9; -.
DR STRING; 183763.LP52_07150; -.
DR Proteomes; UP000031675; 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; 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, ECO:0000313|EMBL:KIH99477.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000031675};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 342..363
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 332..383
FT /note="SteA-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF12555"
SQ SEQUENCE 394 AA; 41643 MW; CEE21191D317AD2F CRC64;
MSRFGRGRGG GSTGVTAPVR CDRRTKNLAK RLRPGDIAVI DHVDLDRASA EALLEREVAA
VLNTAVSISG RFPNLGPRLI VEAGVPLVDD VDPEVFARVH EGERLTLDGG ALLKGESVLA
TGTPQTSESV AAAMDAARAG ISVQLEAFAA NTAEYLRHEH DLLFDGVGIP DVSTPMEGRH
VLVAVRGYHH REDLAALHPY IRDFRPVLIG VDGGADALVE AGFRPALVVG DFDCVSDQAL
NSGAELVVHA DRDGRAPGLK RVRELGREAA AFRGAGSGED AAILLADHAG ASVIVLAGAQ
SALEEFLDRG RVGMAGSFLT RLRVGGRLVD AKGAARLYRR RISPWSLIAL AGAALLVVVL
AALSSPARSG YVAFLTTRWD LLAEYAYRLT GLFT
//
