ID   TDIR_THAAR              Reviewed;         227 AA.
AC   O87940;
DT   05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   25-MAY-2022, entry version 99.
DE   RecName: Full=Transcriptional regulatory protein TdiR;
GN   Name=tdiR;
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, AND DNA-BINDING.
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). Binds to DNA. {ECO:0000269|PubMed:9741082}.
CC   -!- PTM: Phosphorylated by TdiS. {ECO:0000250}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AJ001848; CAA05049.1; -; Genomic_DNA.
DR   AlphaFoldDB; O87940; -.
DR   SMR; O87940; -.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0000160; P:phosphorelay signal transduction system; IEA:UniProtKB-KW.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR   CDD; cd06170; LuxR_C_like; 1.
DR   Gene3D; 1.10.10.10; -; 1.
DR   InterPro; IPR011006; CheY-like_superfamily.
DR   InterPro; IPR016032; Sig_transdc_resp-reg_C-effctor.
DR   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR   InterPro; IPR000792; Tscrpt_reg_LuxR_C.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   Pfam; PF00196; GerE; 1.
DR   Pfam; PF00072; Response_reg; 1.
DR   PRINTS; PR00038; HTHLUXR.
DR   SMART; SM00421; HTH_LUXR; 1.
DR   SMART; SM00448; REC; 1.
DR   SUPFAM; SSF46894; SSF46894; 1.
DR   SUPFAM; SSF52172; SSF52172; 1.
DR   PROSITE; PS00622; HTH_LUXR_1; 1.
DR   PROSITE; PS50043; HTH_LUXR_2; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   1: Evidence at protein level;
KW   DNA-binding; Phosphoprotein; Transcription; Transcription regulation;
KW   Two-component regulatory system.
FT   CHAIN           1..227
FT                   /note="Transcriptional regulatory protein TdiR"
FT                   /id="PRO_0000418871"
FT   DOMAIN          11..125
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT   DOMAIN          141..206
FT                   /note="HTH luxR-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00411"
FT   DNA_BIND        165..184
FT                   /note="H-T-H motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00411"
FT   MOD_RES         60
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   227 AA;  24759 MW;  E741F397A850D807 CRC64;
     MQATKTGNAS TVFVVDDEAS VRDSLTWLLN SISLDVRTFE SAKDFLDADI SCTHGCVVLD
     VRMQNVSGLQ LQQALSERGF KLPIIFLSAY GDAQMGAQAV KKGAFDFLQK PYRNQDLLDA
     VNAALALNRE MADKQNEKQK HLDLLATLSQ REMEILDKVV AGSSSKEIAK LLGISYKTVE
     AHRGRIISKL GLKSTGDLMH FVMRGSSHCS DCGRQPLPGS SPCRPAA