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Response regulator protein TodT

 TODT_PSEPT              Reviewed;         227 AA.
I7CA98; O07832;
16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
16-OCT-2013, sequence version 2.
12-SEP-2018, entry version 34.
RecName: Full=Response regulator protein TodT;
Name=todT; Synonyms=tobT; OrderedLocusNames=T1E_4277;
Pseudomonas putida (strain DOT-T1E).
Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
Pseudomonadaceae; Pseudomonas.
NCBI_TaxID=1196325;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=DOT-T1E;
PubMed=10333523; DOI=10.1016/S0378-1119(99)00113-4;
Mosqueda G., Ramos-Gonzalez M.I., Ramos J.L.;
"Toluene metabolism by the solvent-tolerant Pseudomonas putida DOT-T1
strain, and its role in solvent impermeabilization.";
Gene 232:69-76(1999).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=DOT-T1E;
PubMed=23815283; DOI=10.1111/1751-7915.12061;
Udaondo Z., Molina L., Daniels C., Gomez M.J., Molina-Henares M.A.,
Matilla M.A., Roca A., Fernandez M., Duque E., Segura A., Ramos J.L.;
"Metabolic potential of the organic-solvent tolerant Pseudomonas
putida DOT-T1E deduced from its annotated genome.";
Microb. Biotechnol. 6:598-611(2013).
[3]
FUNCTION, DNA-BINDING, ACTIVITY REGULATION, AND PHOSPHORYLATION.
STRAIN=DOT-T1E;
PubMed=16702539; DOI=10.1073/pnas.0602902103;
Lacal J., Busch A., Guazzaroni M.E., Krell T., Ramos J.L.;
"The TodS-TodT two-component regulatory system recognizes a wide range
of effectors and works with DNA-bending proteins.";
Proc. Natl. Acad. Sci. U.S.A. 103:8191-8196(2006).
[4]
FUNCTION, DNA-BINDING, AND SUBUNIT.
STRAIN=DOT-T1E;
PubMed=18166197; DOI=10.1016/j.jmb.2007.12.004;
Lacal J., Guazzaroni M.E., Busch A., Krell T., Ramos J.L.;
"Hierarchical binding of the TodT response regulator to its multiple
recognition sites at the tod pathway operon promoter.";
J. Mol. Biol. 376:325-337(2008).
[5]
FUNCTION, AND DNA-BINDING.
STRAIN=DOT-T1E;
PubMed=18950641; DOI=10.1016/j.jmb.2008.10.011;
Lacal J., Guazzaroni M.E., Gutierrez-del-Arroyo P., Busch A.,
Velez M., Krell T., Ramos J.L.;
"Two levels of cooperativeness in the binding of TodT to the tod
operon promoter.";
J. Mol. Biol. 384:1037-1047(2008).
[6]
PHOSPHORYLATION BY TODS, AND MUTAGENESIS OF ASP-77.
STRAIN=DOT-T1E;
PubMed=19240030; DOI=10.1074/jbc.M900521200;
Busch A., Guazzaroni M.E., Lacal J., Ramos J.L., Krell T.;
"The sensor kinase TodS operates by a multiple step phosphorelay
mechanism involving two autokinase domains.";
J. Biol. Chem. 284:10353-10360(2009).
[7]
INDUCTION.
STRAIN=DOT-T1E;
PubMed=20543072; DOI=10.1128/JB.00379-10;
Busch A., Lacal J., Silva-Jimenez H., Krell T., Ramos J.L.;
"Catabolite repression of the TodS/TodT two-component system and
effector-dependent transphosphorylation of TodT as the basis for
toluene dioxygenase catabolic pathway control.";
J. Bacteriol. 192:4246-4250(2010).
[8]
FUNCTION IN TOLUENE DEGRADATION.
STRAIN=DOT-T1E;
PubMed=22212183; DOI=10.1111/j.1751-7915.2011.00322.x;
Silva-Jimenez H., Garcia-Fontana C., Cadirci B.H.,
Ramos-Gonzalez M.I., Ramos J.L., Krell T.;
"Study of the TmoS/TmoT two-component system: towards the functional
characterization of the family of TodS/TodT like systems.";
Microb. Biotechnol. 5:489-500(2012).
-!- FUNCTION: Member of the two-component regulatory system TodS/TodT
involved in the regulation of toluene degradation. Phosphorylated
TodT activates transcription of the tod operon (todXFC1C2BADEGIH).
Binds specifically to three boxes in the tod promoter region in a
cooperative manner. Boxes-1 and -2 are pseudopalindromes and Box-3
is a half-palindrome. {ECO:0000269|PubMed:16702539,
ECO:0000269|PubMed:18166197, ECO:0000269|PubMed:18950641,
ECO:0000269|PubMed:22212183}.
-!- ACTIVITY REGULATION: Phosphorylation by TodS probably induces
conformational changes, which allow or alter the interaction with
RNA polymerase in a process assisted by the integration host
factor (IHF). {ECO:0000269|PubMed:16702539}.
-!- SUBUNIT: Monomer. {ECO:0000269|PubMed:18166197}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
-!- INDUCTION: Constitutively expressed. Is under catabolite
repression. {ECO:0000269|PubMed:20543072}.
-!- PTM: Phosphorylated by TodS. {ECO:0000269|PubMed:16702539,
ECO:0000269|PubMed:19240030}.
-!- SEQUENCE CAUTION:
Sequence=AFO50106.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
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EMBL; GQ884177; ADI95407.1; -; Genomic_DNA.
EMBL; CP003734; AFO50106.1; ALT_INIT; Genomic_DNA.
ProteinModelPortal; I7CA98; -.
SMR; I7CA98; -.
DIP; DIP-61172N; -.
IntAct; I7CA98; 1.
EnsemblBacteria; AFO50106; AFO50106; T1E_4277.
KEGG; ppx:T1E_4277; -.
PATRIC; fig|1196325.3.peg.4234; -.
Proteomes; UP000006503; Chromosome.
CollecTF; EXPREG_000005e0; -.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0032993; C:protein-DNA complex; IDA:CollecTF.
GO; GO:0001216; F:bacterial-type RNA polymerase transcriptional activator activity, sequence-specific DNA binding; IDA:CollecTF.
GO; GO:0000976; F:transcription regulatory region sequence-specific DNA binding; IDA:CollecTF.
GO; GO:0000160; P:phosphorelay signal transduction system; IEA:UniProtKB-KW.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
CDD; cd06170; LuxR_C_like; 1.
CDD; cd00156; REC; 1.
Gene3D; 1.10.10.10; -; 1.
InterPro; IPR011006; CheY-like_superfamily.
InterPro; IPR016032; Sig_transdc_resp-reg_C-effctor.
InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
InterPro; IPR000792; Tscrpt_reg_LuxR_C.
InterPro; IPR036388; WH-like_DNA-bd_sf.
Pfam; PF00196; GerE; 1.
Pfam; PF00072; Response_reg; 1.
PRINTS; PR00038; HTHLUXR.
SMART; SM00421; HTH_LUXR; 1.
SMART; SM00448; REC; 1.
SUPFAM; SSF46894; SSF46894; 1.
SUPFAM; SSF52172; SSF52172; 1.
PROSITE; PS50043; HTH_LUXR_2; 1.
PROSITE; PS50110; RESPONSE_REGULATORY; 1.
1: Evidence at protein level;
Activator; Complete proteome; Cytoplasm; DNA-binding; Phosphoprotein;
Transcription; Transcription regulation;
Two-component regulatory system.
CHAIN 1 227 Response regulator protein TodT.
/FTId=PRO_0000423593.
DOMAIN 28 142 Response regulatory.
{ECO:0000255|PROSITE-ProRule:PRU00169}.
DOMAIN 158 223 HTH luxR-type. {ECO:0000255|PROSITE-
ProRule:PRU00411}.
DNA_BIND 182 201 H-T-H motif. {ECO:0000255|PROSITE-
ProRule:PRU00411}.
MOD_RES 77 77 4-aspartylphosphate. {ECO:0000305}.
MUTAGEN 77 77 D->A: Lack of phosphorylation.
{ECO:0000269|PubMed:19240030}.
SEQUENCE 227 AA; 25432 MW; 7A5D506B9213E26D CRC64;
MPARWGCLFP GKYPCQTGLR HMSDRASVIY ILDDDNAVLE ALSSLVRSIG LSVECFSSAS
VFLNDVNRSA CGCLILDVRM PEMSGLDVQR QLKELGEQIP IIFISGHGDI PMAVKAIKAG
AVDFFTKPFR EEELLGAIRA ALKLAPQQRS NAPRVSELKE NYESLSKREQ QVLKFVLRGY
LNKQTALELD ISEATVKVHR HNIMRKMKVS SIQDLVRVTE RLKDSLE


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