ID   TDIS_THAAR              Reviewed;         548 AA.
AC   O87939;
DT   05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   25-MAY-2022, entry version 98.
DE   RecName: Full=Sensor protein TdiS;
DE            EC=2.7.13.3;
GN   Name=tdiS;
OS   Thauera aromatica.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Rhodocyclales; Zoogloeaceae;
OC   Thauera.
OX   NCBI_TaxID=59405;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=DSM 6984 / CIP 107765 / K172;
RX   PubMed=9632263; DOI=10.1046/j.1365-2958.1998.00826.x;
RA   Leuthner B., Leutwein C., Schulz H., Horth P., Haehnel W., Schiltz E.,
RA   Schagger H., Heider J.;
RT   "Biochemical and genetic characterization of benzylsuccinate synthase from
RT   Thauera aromatica: a new glycyl radical enzyme catalysing the first step in
RT   anaerobic toluene metabolism.";
RL   Mol. Microbiol. 28:615-628(1998).
RN   [2]
RP   FUNCTION.
RC   STRAIN=DSM 6984 / CIP 107765 / K172;
RX   PubMed=9741082; DOI=10.1111/j.1574-6968.1998.tb13180.x;
RA   Leuthner B., Heider J.;
RT   "A two-component system involved in regulation of anaerobic toluene
RT   metabolism in Thauera aromatica.";
RL   FEMS Microbiol. Lett. 166:35-41(1998).
CC   -!- FUNCTION: Member of the two-component regulatory system TdiR/TdiS,
CC       which probably regulates transcription of toluene catabolic genes (bss
CC       operon). May activate TdiR by phosphorylation.
CC       {ECO:0000269|PubMed:9741082}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC         histidine.; EC=2.7.13.3;
CC   -!- PTM: Autophosphorylated. {ECO:0000250}.
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DR   EMBL; AJ001848; CAA05048.1; -; Genomic_DNA.
DR   AlphaFoldDB; O87939; -.
DR   SMR; O87939; -.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004673; F:protein histidine kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0000160; P:phosphorelay signal transduction system; IEA:UniProtKB-KW.
DR   CDD; cd00130; PAS; 1.
DR   Gene3D; 3.30.565.10; -; 1.
DR   InterPro; IPR003594; HATPase_C.
DR   InterPro; IPR036890; HATPase_C_sf.
DR   InterPro; IPR005467; His_kinase_dom.
DR   InterPro; IPR001610; PAC.
DR   InterPro; IPR000014; PAS.
DR   InterPro; IPR000700; PAS-assoc_C.
DR   InterPro; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF13188; PAS_8; 1.
DR   Pfam; PF13426; PAS_9; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00086; PAC; 2.
DR   SMART; SM00091; PAS; 2.
DR   SUPFAM; SSF55785; SSF55785; 2.
DR   SUPFAM; SSF55874; SSF55874; 1.
DR   TIGRFAMs; TIGR00229; sensory_box; 2.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50113; PAC; 1.
DR   PROSITE; PS50112; PAS; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Kinase; Nucleotide-binding; Phosphoprotein; Repeat;
KW   Transferase; Two-component regulatory system.
FT   CHAIN           1..548
FT                   /note="Sensor protein TdiS"
FT                   /id="PRO_0000418870"
FT   DOMAIN          20..89
FT                   /note="PAS 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00140"
FT   DOMAIN          94..145
FT                   /note="PAC 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00141"
FT   DOMAIN          185..256
FT                   /note="PAS 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00140"
FT   DOMAIN          263..314
FT                   /note="PAC 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00141"
FT   DOMAIN          334..548
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT   MOD_RES         337
FT                   /note="Phosphohistidine; by autocatalysis"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
SQ   SEQUENCE   548 AA;  62441 MW;  ACEB9ADF05EFCA4A CRC64;
     MSGNAIASTE TEMEADHGND PATGYEVIFR NTPLAICHLR NRAFVRCNTR FEELFGYARG
     ELDNKSVRLL YPTDESFRTI GENYGHFFER HDTFKDERPI IRKDGSVIWC IVTGSLLDSS
     NPRLGSIWVV QDISEHKRTE DDLKASVEKL EILVHQRTLE LHKHVNKLEQ EVATRKLAEE
     VANEHREKYE KLFHMLPIGI SITDNEGRIL EANRQFTELV GTPEKPPITW QQLPQRFFLS
     DGTKVARKRL PWRIHDVQKD SIKNIEIGMR EEESRKQRWL SVSSSLLELK GQKMVVAAFT
     DITYRKRIEE LERLRHAELT RLGRINAMAG MAAALAHQMG QPLVSALNYL QGCRLRLEHI
     RGAAEISQSL GLAITHLDQA GEILRRVKDF VCKHTPERTP ENINEVIQDT LSFLSFDVHR
     HNVTVNLQLI PSPPAVPLCK IEIQQVLFNL VKNGIEAMSE MEPESRILTI GNEISTDGRS
     MKIFVQDHGV GVEKRAEKRA FEPYFTTKPD GLGIGLTICR SIIESHGGEL SFSKTGERGS
     KFQFTLPI