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Sensor histidine kinase TodS (EC 2.7.13.3)

 TODS_PSEPT              Reviewed;         978 AA.
E0X9C7; I7B4U5; I7CDZ1;
16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
02-NOV-2010, sequence version 1.
25-OCT-2017, entry version 47.
RecName: Full=Sensor histidine kinase TodS;
EC=2.7.13.3;
Name=todS; Synonyms=dhkD; OrderedLocusNames=T1E_4275/T1E_4276;
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, CATALYTIC ACTIVITY, DOMAIN, AND AUTOPHOSPHORYLATION.
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]
ENZYME REGULATION, AUTOPHOSPHORYLATION, AND MUTAGENESIS OF PHE-46;
ILE-74; PHE-79 AND ILE-114.
STRAIN=DOT-T1E;
PubMed=17693554; DOI=10.1073/pnas.0701547104;
Busch A., Lacal J., Martos A., Ramos J.L., Krell T.;
"Bacterial sensor kinase TodS interacts with agonistic and
antagonistic signals.";
Proc. Natl. Acad. Sci. U.S.A. 104:13774-13779(2007).
[5]
FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, AUTOPHOSPHORYLATION,
PHOSPHORELAY, DOMAIN, AND MUTAGENESIS OF HIS-190; ASP-500 AND HIS-760.
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).
[6]
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).
[7]
FUNCTION, ENZYME REGULATION, AND SUBCELLULAR LOCATION.
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. Phosphorylates
TodT via a four-step phosphorelay in response to toluene. Can also
be induced by benzene and ethylbenzene.
{ECO:0000269|PubMed:16702539, ECO:0000269|PubMed:19240030,
ECO:0000269|PubMed:22212183}.
-!- CATALYTIC ACTIVITY: ATP + protein L-histidine = ADP + protein N-
phospho-L-histidine. {ECO:0000269|PubMed:16702539,
ECO:0000269|PubMed:19240030}.
-!- ENZYME REGULATION: Activity is regulated by agonists and
antagonists. Binding of agonists such as toluene or benzene to
TodS stimulates autophosphorylation at His-190. Activity is
inhibited by antagonists such as o-xylene, o-chlorotoluene and
trimethylbenzene isomers, which bind to TodS but do not stimulate
autophosphorylation. Agonists and antagonists bind to the same PAS
domain. {ECO:0000269|PubMed:17693554, ECO:0000269|PubMed:19240030,
ECO:0000269|PubMed:22212183}.
-!- INTERACTION:
Self; NbExp=2; IntAct=EBI-15583094, EBI-15583094;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22212183}.
-!- INDUCTION: Constitutively expressed. Is under catabolite
repression. {ECO:0000269|PubMed:20543072}.
-!- DOMAIN: Toluene binds to the N-terminal PAS sensor domain but not
to the C-terminal PAS domain. The two PAS sensor domains may sense
two different signals. {ECO:0000269|PubMed:16702539,
ECO:0000269|PubMed:19240030}.
-!- PTM: Autophosphorylated. Activation requires a sequential transfer
of a phosphate group from a His in the primary transmitter domain,
to an Asp in the receiver domain and to a His in the secondary
transmitter domain.
-!- SEQUENCE CAUTION:
Sequence=AFO50104.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
Sequence=AFO50104.1; Type=Frameshift; Positions=394; Evidence={ECO:0000305};
Sequence=AFO50105.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=AFO50105.1; Type=Frameshift; Positions=394; Evidence={ECO:0000305};
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EMBL; GQ884177; ADI95406.1; -; Genomic_DNA.
EMBL; CP003734; AFO50104.1; ALT_SEQ; Genomic_DNA.
EMBL; CP003734; AFO50105.1; ALT_SEQ; Genomic_DNA.
ProteinModelPortal; E0X9C7; -.
SMR; E0X9C7; -.
DIP; DIP-61171N; -.
IntAct; E0X9C7; 1.
EnsemblBacteria; AFO50104; AFO50104; T1E_4275.
EnsemblBacteria; AFO50105; AFO50105; T1E_4276.
KEGG; ppx:T1E_4275; -.
KEGG; ppx:T1E_4276; -.
PATRIC; fig|1196325.3.peg.4232; -.
Proteomes; UP000006503; Chromosome.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
CDD; cd00075; HATPase_c; 2.
CDD; cd00082; HisKA; 2.
CDD; cd00130; PAS; 2.
CDD; cd00156; REC; 1.
Gene3D; 3.30.565.10; -; 2.
InterPro; IPR011006; CheY-like_superfamily.
InterPro; IPR003594; HATPase_C.
InterPro; IPR036890; HATPase_C_sf.
InterPro; IPR005467; His_kinase_dom.
InterPro; IPR003661; HisK_dim/P.
InterPro; IPR036097; HisK_dim/P_sf.
InterPro; IPR001610; PAC.
InterPro; IPR000014; PAS.
InterPro; IPR000700; PAS-assoc_C.
InterPro; IPR035965; PAS-like_dom_sf.
InterPro; IPR013656; PAS_4.
InterPro; IPR004358; Sig_transdc_His_kin-like_C.
InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
Pfam; PF02518; HATPase_c; 2.
Pfam; PF00512; HisKA; 2.
Pfam; PF08448; PAS_4; 1.
Pfam; PF13426; PAS_9; 1.
Pfam; PF00072; Response_reg; 1.
PRINTS; PR00344; BCTRLSENSOR.
SMART; SM00387; HATPase_c; 2.
SMART; SM00388; HisKA; 2.
SMART; SM00086; PAC; 2.
SMART; SM00091; PAS; 2.
SMART; SM00448; REC; 1.
SUPFAM; SSF47384; SSF47384; 2.
SUPFAM; SSF52172; SSF52172; 1.
SUPFAM; SSF55785; SSF55785; 2.
SUPFAM; SSF55874; SSF55874; 2.
TIGRFAMs; TIGR00229; sensory_box; 2.
PROSITE; PS50109; HIS_KIN; 2.
PROSITE; PS50113; PAC; 2.
PROSITE; PS50112; PAS; 2.
PROSITE; PS50110; RESPONSE_REGULATORY; 1.
1: Evidence at protein level;
ATP-binding; Complete proteome; Cytoplasm; Kinase; Nucleotide-binding;
Phosphoprotein; Repeat; Transferase; Two-component regulatory system.
CHAIN 1 978 Sensor histidine kinase TodS.
/FTId=PRO_0000423590.
DOMAIN 32 103 PAS 1. {ECO:0000255|PROSITE-
ProRule:PRU00140}.
DOMAIN 108 162 PAC 1. {ECO:0000255|PROSITE-
ProRule:PRU00141}.
DOMAIN 187 405 Histidine kinase 1. {ECO:0000255|PROSITE-
ProRule:PRU00107}.
DOMAIN 452 567 Response regulatory.
{ECO:0000255|PROSITE-ProRule:PRU00169}.
DOMAIN 611 681 PAS 2. {ECO:0000255|PROSITE-
ProRule:PRU00140}.
DOMAIN 685 737 PAC 2. {ECO:0000255|PROSITE-
ProRule:PRU00141}.
DOMAIN 757 974 Histidine kinase 2. {ECO:0000255|PROSITE-
ProRule:PRU00107}.
MOD_RES 190 190 Phosphohistidine; by autocatalysis.
{ECO:0000305}.
MOD_RES 500 500 4-aspartylphosphate. {ECO:0000305}.
MOD_RES 760 760 Phosphohistidine. {ECO:0000305}.
MUTAGEN 46 46 F->A: Decreases affinity for agonists and
antagonists.
{ECO:0000269|PubMed:17693554}.
MUTAGEN 74 74 I->A: Decreases affinity for agonists and
antagonists.
{ECO:0000269|PubMed:17693554}.
MUTAGEN 79 79 F->A: Does not bind agonists and
antagonists. Does not stimulate
autophosphorylation and transcription of
target genes.
{ECO:0000269|PubMed:17693554}.
MUTAGEN 114 114 I->A: Decreases affinity for agonists and
antagonists.
{ECO:0000269|PubMed:17693554}.
MUTAGEN 190 190 H->A: Strong decrease in TodT
phosphorylation.
{ECO:0000269|PubMed:19240030}.
MUTAGEN 500 500 D->A: Strong decrease in TodT
phosphorylation.
{ECO:0000269|PubMed:19240030}.
MUTAGEN 760 760 H->A: Lack of TodT phosphorylation.
{ECO:0000269|PubMed:19240030}.
SEQUENCE 978 AA; 108018 MW; F059F981E8D03E32 CRC64;
MSSLDRKKPQ NRSKNNYYNI CLKEKGSEEL TCEEHARIIF DGLYEFVGLL DAHGNVLEVN
QVALEGAGIT LEEIRGKPFW KARWWQISKK TEATQKRLVE TASSGEFVRC DVEILGKSGG
REVIAVDFSL LPICNEEGSI VYLLAEGRNI TDKKKAEAML ALKNQELEQS VERIRKLDNA
KSDFFAKVSH ELRTPLSLIL GPLEAVMAAE AGRESPYWKQ FEVIQRNAMT LLKQVNTLLD
LAKMDARQMG LSYRRANLSQ LTRTISSNFE GIAQQKSITF DTKLPVQMVA EVDCEKYERI
ILNLLSNAFK FTPDGGLIRC CLSLSRPNYA LVTVSDSGPG IPPALRKEIF ERFHQLSQEG
QQATRGTGLG LSIVKEFVEL HRGTISVSDA PGGGALFQVK LPLNAPEGAY VASNTAPRRD
NPQVVDTDEY LLLAPNAENE AEVLPFQSDQ PRVLIVEDNP DMRGFIKDCL SSDYQVYVAP
DGAKALELMS NMPPDLLITD LMMPVMSGDM LVHQVRKKNE LSHIPIMVLS AKSDAELRVK
LLSESVQDFL LKPFSAHELR ARVSNLVSMK VAGDALRKEL SDQGDDIAIL THRLIKSRHR
LQQSNIALSA SEARWKAVYE NSAAGIVLTD PENRILNANP AFQRITGYGE KDLEGLSMEQ
LTPSDESPQI KQRLANLLQG GGAEYSVERS YLCKNGSTIW ANASVSLMPQ RVGESPVILQ
IIDDITEKKQ AQENLNQLQQ QLVYVSRSAT MGEFAAYIAH EINQPLSAIM TNANAGTRWL
GNEPSNIPEA KEALARIIRD SDRAAEIIRM VRSFLKRQET VLKPIDLKAL VTDTSLILKA
PSQNNSVNLD VVADDELPEI WGDGVQIQQL IINLAMNAIE AISQADCETR QLTLSFSGND
TGDALVISVK DTGPGISERQ MAQLFNAFYT TKKEGLGMGL AICLTITEVH NGKIWVECPP
AGGACFLVSI PARQGSGT


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