TSAR_COMTE
ID TSAR_COMTE Reviewed; 298 AA.
AC P94678;
DT 01-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=HTH-type transcriptional regulator TsaR;
GN Name=tsaR;
OS Comamonas testosteroni (Pseudomonas testosteroni).
OG Plasmid pTSA.
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Comamonas.
OX NCBI_TaxID=285;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=DSM 6577 / T-2;
RX PubMed=9006050; DOI=10.1128/jb.179.3.919-927.1997;
RA Junker F., Kiewitz R., Cook A.M.;
RT "Characterization of the p-toluenesulfonate operon tsaMBCD and tsaR in
RT Comamonas testosteroni T-2.";
RL J. Bacteriol. 179:919-927(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=DSM 6577 / T-2;
RX PubMed=11282598; DOI=10.1128/aem.67.4.1508-1516.2001;
RA Tralau T., Cook A.M., Ruff J.;
RT "Map of the IncP1beta plasmid pTSA encoding the widespread genes (tsa) for
RT p-toluenesulfonate degradation in Comamonas testosteroni T-2.";
RL Appl. Environ. Microbiol. 67:1508-1516(2001).
RN [3]
RP FUNCTION, DNA-BINDING, AND ACTIVITY REGULATION.
RC STRAIN=DSM 6577 / T-2;
RX PubMed=12676713; DOI=10.1128/aem.69.4.2298-2305.2003;
RA Tralau T., Mampel J., Cook A.M., Ruff J.;
RT "Characterization of TsaR, an oxygen-sensitive LysR-type regulator for the
RT degradation of p-toluenesulfonate in Comamonas testosteroni T-2.";
RL Appl. Environ. Microbiol. 69:2298-2305(2003).
RN [4]
RP FUNCTION.
RC STRAIN=DSM 6577 / T-2;
RX PubMed=13680097; DOI=10.1007/s00203-003-0594-8;
RA Tralau T., Cook A.M., Ruff J.;
RT "An additional regulator, TsaQ, is involved with TsaR in regulation of
RT transport during the degradation of p-toluenesulfonate in Comamonas
RT testosteroni T-2.";
RL Arch. Microbiol. 180:319-326(2003).
RN [5]
RP CRYSTALLIZATION.
RC STRAIN=DSM 6577 / T-2;
RX PubMed=18678953; DOI=10.1107/s1744309108019738;
RA Monferrer D., Tralau T., Kertesz M.A., Panjikar S., Uson I.;
RT "High crystallizability under air-exclusion conditions of the full-length
RT LysR-type transcriptional regulator TsaR from Comamonas testosteroni T-2
RT and data-set analysis for a MIRAS structure-solution approach.";
RL Acta Crystallogr. F 64:764-769(2008).
RN [6] {ECO:0007744|PDB:3FXQ, ECO:0007744|PDB:3FXR, ECO:0007744|PDB:3FXU, ECO:0007744|PDB:3FZJ}
RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF FREE PROTEIN AND COMPLEX WITH
RP TOLUENE-4-SULFONATE, H-T-H MOTIF, DNA-BINDING, AND SUBUNIT.
RC STRAIN=DSM 6577 / T-2;
RX PubMed=20059681; DOI=10.1111/j.1365-2958.2010.07043.x;
RA Monferrer D., Tralau T., Kertesz M.A., Dix I., Sola M., Uson I.;
RT "Structural studies on the full-length LysR-type regulator TsaR from
RT Comamonas testosteroni T-2 reveal a novel open conformation of the
RT tetrameric LTTR fold.";
RL Mol. Microbiol. 75:1199-1214(2010).
CC -!- FUNCTION: Regulates expression of the tsaMBCD1 operon and of tsaT in
CC response to p-toluenesulfonate (TSA). Acts by binding directly to the
CC promoter region. Binding to the tsa promoter depends on TSA
CC concentration. {ECO:0000269|PubMed:12676713,
CC ECO:0000269|PubMed:13680097}.
CC -!- ACTIVITY REGULATION: Sensitive to oxygen.
CC {ECO:0000269|PubMed:12676713}.
CC -!- SUBUNIT: Homotetramer. Dimer of dimers related by a twofold axis.
CC {ECO:0000269|PubMed:20059681}.
CC -!- SIMILARITY: Belongs to the LysR transcriptional regulatory family.
CC {ECO:0000305}.
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DR EMBL; AF311437; AAC44806.1; -; Genomic_DNA.
DR PDB; 3FXQ; X-ray; 1.85 A; A/B=1-298.
DR PDB; 3FXR; X-ray; 2.50 A; A/B=1-298.
DR PDB; 3FXU; X-ray; 1.95 A; A/B=1-298.
DR PDB; 3FZJ; X-ray; 7.10 A; A/B/C/D/E/F/G/H/I/J=1-298.
DR PDB; 3N6T; X-ray; 1.85 A; A=91-295.
DR PDB; 3N6U; X-ray; 1.87 A; A=91-295.
DR PDBsum; 3FXQ; -.
DR PDBsum; 3FXR; -.
DR PDBsum; 3FXU; -.
DR PDBsum; 3FZJ; -.
DR PDBsum; 3N6T; -.
DR PDBsum; 3N6U; -.
DR AlphaFoldDB; P94678; -.
DR SMR; P94678; -.
DR EvolutionaryTrace; P94678; -.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR005119; LysR_subst-bd.
DR InterPro; IPR000847; Tscrpt_reg_HTH_LysR.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR Pfam; PF00126; HTH_1; 1.
DR Pfam; PF03466; LysR_substrate; 1.
DR PRINTS; PR00039; HTHLYSR.
DR SUPFAM; SSF46785; SSF46785; 1.
DR PROSITE; PS50931; HTH_LYSR; 1.
PE 1: Evidence at protein level;
KW 3D-structure; DNA-binding; Plasmid; Transcription;
KW Transcription regulation.
FT CHAIN 1..298
FT /note="HTH-type transcriptional regulator TsaR"
FT /id="PRO_0000430301"
FT DOMAIN 1..58
FT /note="HTH lysR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00253"
FT DNA_BIND 18..37
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00253"
FT BINDING 98
FT /ligand="toluene-4-sulfonate"
FT /ligand_id="ChEBI:CHEBI:27023"
FT /evidence="ECO:0000269|PubMed:20059681,
FT ECO:0007744|PDB:3FXU"
FT BINDING 100
FT /ligand="toluene-4-sulfonate"
FT /ligand_id="ChEBI:CHEBI:27023"
FT /evidence="ECO:0000269|PubMed:20059681,
FT ECO:0007744|PDB:3FXU"
FT HELIX 2..15
FT /evidence="ECO:0007829|PDB:3FXQ"
FT HELIX 18..24
FT /evidence="ECO:0007829|PDB:3FXQ"
FT HELIX 29..43
FT /evidence="ECO:0007829|PDB:3FXQ"
FT STRAND 47..50
FT /evidence="ECO:0007829|PDB:3FXQ"
FT STRAND 52..57
FT /evidence="ECO:0007829|PDB:3FXQ"
FT HELIX 59..90
FT /evidence="ECO:0007829|PDB:3FXQ"
FT STRAND 92..97
FT /evidence="ECO:0007829|PDB:3FXQ"
FT HELIX 99..103
FT /evidence="ECO:0007829|PDB:3FXQ"
FT HELIX 105..116
FT /evidence="ECO:0007829|PDB:3FXQ"
FT STRAND 121..126
FT /evidence="ECO:0007829|PDB:3FXQ"
FT TURN 129..132
FT /evidence="ECO:0007829|PDB:3FXQ"
FT HELIX 133..138
FT /evidence="ECO:0007829|PDB:3FXQ"
FT STRAND 139..147
FT /evidence="ECO:0007829|PDB:3FXQ"
FT HELIX 150..152
FT /evidence="ECO:0007829|PDB:3FXQ"
FT STRAND 157..164
FT /evidence="ECO:0007829|PDB:3FXQ"
FT STRAND 167..172
FT /evidence="ECO:0007829|PDB:3FXQ"
FT TURN 176..179
FT /evidence="ECO:0007829|PDB:3FXQ"
FT HELIX 183..186
FT /evidence="ECO:0007829|PDB:3FXQ"
FT STRAND 189..194
FT /evidence="ECO:0007829|PDB:3FXQ"
FT HELIX 202..210
FT /evidence="ECO:0007829|PDB:3FXQ"
FT STRAND 217..222
FT /evidence="ECO:0007829|PDB:3FXQ"
FT TURN 225..227
FT /evidence="ECO:0007829|PDB:3FXQ"
FT HELIX 228..233
FT /evidence="ECO:0007829|PDB:3FXQ"
FT STRAND 238..242
FT /evidence="ECO:0007829|PDB:3FXQ"
FT HELIX 243..247
FT /evidence="ECO:0007829|PDB:3FXQ"
FT HELIX 252..254
FT /evidence="ECO:0007829|PDB:3FXQ"
FT STRAND 255..257
FT /evidence="ECO:0007829|PDB:3FXQ"
FT STRAND 268..274
FT /evidence="ECO:0007829|PDB:3FXQ"
FT HELIX 281..293
FT /evidence="ECO:0007829|PDB:3FXQ"
SQ SEQUENCE 298 AA; 32663 MW; 4740B8B80DED0C22 CRC64;
MKLQTLQALI CIEEVGSLRA AAQLLHLSQP ALSAAIQQLE DELKAPLLVR TKRGVSLTSF
GQAFMKHARL IVTESRRAQE EIGQLRGRWE GHITFAASPA IALAALPLAL ASFAREFPDV
TVNVRDGMYP AVSPQLRDGT LDFALTAAHK HDIDTDLEAQ PLYVSDVVIV GQRQHPMANA
TRLAELQECR WAFSSAPRGP GAIIRNAFAR YGLPEPKLGL VCESFLALPG VVAHSDLLTT
MPRTLYERNA FKDQLCSIPL QDALPNPTIY VLRRHDLPVT PAAAGLIRWI QHHALQTG
