TODS_PSEPT
ID TODS_PSEPT Reviewed; 978 AA.
AC E0X9C7; I7B4U5; I7CDZ1;
DT 16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT 02-NOV-2010, sequence version 1.
DT 25-MAY-2022, entry version 59.
DE RecName: Full=Sensor histidine kinase TodS;
DE EC=2.7.13.3;
GN Name=todS; Synonyms=dhkD; OrderedLocusNames=T1E_4275/T1E_4276;
OS Pseudomonas putida (strain DOT-T1E).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1196325;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=DOT-T1E;
RX PubMed=10333523; DOI=10.1016/s0378-1119(99)00113-4;
RA Mosqueda G., Ramos-Gonzalez M.I., Ramos J.L.;
RT "Toluene metabolism by the solvent-tolerant Pseudomonas putida DOT-T1
RT strain, and its role in solvent impermeabilization.";
RL Gene 232:69-76(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DOT-T1E;
RX PubMed=23815283; DOI=10.1111/1751-7915.12061;
RA Udaondo Z., Molina L., Daniels C., Gomez M.J., Molina-Henares M.A.,
RA Matilla M.A., Roca A., Fernandez M., Duque E., Segura A., Ramos J.L.;
RT "Metabolic potential of the organic-solvent tolerant Pseudomonas putida
RT DOT-T1E deduced from its annotated genome.";
RL Microb. Biotechnol. 6:598-611(2013).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, DOMAIN, AND AUTOPHOSPHORYLATION.
RC STRAIN=DOT-T1E;
RX PubMed=16702539; DOI=10.1073/pnas.0602902103;
RA Lacal J., Busch A., Guazzaroni M.E., Krell T., Ramos J.L.;
RT "The TodS-TodT two-component regulatory system recognizes a wide range of
RT effectors and works with DNA-bending proteins.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:8191-8196(2006).
RN [4]
RP ACTIVITY REGULATION, AUTOPHOSPHORYLATION, AND MUTAGENESIS OF PHE-46;
RP ILE-74; PHE-79 AND ILE-114.
RC STRAIN=DOT-T1E;
RX PubMed=17693554; DOI=10.1073/pnas.0701547104;
RA Busch A., Lacal J., Martos A., Ramos J.L., Krell T.;
RT "Bacterial sensor kinase TodS interacts with agonistic and antagonistic
RT signals.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:13774-13779(2007).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, AUTOPHOSPHORYLATION,
RP PHOSPHORELAY, DOMAIN, AND MUTAGENESIS OF HIS-190; ASP-500 AND HIS-760.
RC STRAIN=DOT-T1E;
RX PubMed=19240030; DOI=10.1074/jbc.m900521200;
RA Busch A., Guazzaroni M.E., Lacal J., Ramos J.L., Krell T.;
RT "The sensor kinase TodS operates by a multiple step phosphorelay mechanism
RT involving two autokinase domains.";
RL J. Biol. Chem. 284:10353-10360(2009).
RN [6]
RP INDUCTION.
RC STRAIN=DOT-T1E;
RX PubMed=20543072; DOI=10.1128/jb.00379-10;
RA Busch A., Lacal J., Silva-Jimenez H., Krell T., Ramos J.L.;
RT "Catabolite repression of the TodS/TodT two-component system and effector-
RT dependent transphosphorylation of TodT as the basis for toluene dioxygenase
RT catabolic pathway control.";
RL J. Bacteriol. 192:4246-4250(2010).
RN [7]
RP FUNCTION, ACTIVITY REGULATION, AND SUBCELLULAR LOCATION.
RC STRAIN=DOT-T1E;
RX PubMed=22212183; DOI=10.1111/j.1751-7915.2011.00322.x;
RA Silva-Jimenez H., Garcia-Fontana C., Cadirci B.H., Ramos-Gonzalez M.I.,
RA Ramos J.L., Krell T.;
RT "Study of the TmoS/TmoT two-component system: towards the functional
RT characterization of the family of TodS/TodT like systems.";
RL Microb. Biotechnol. 5:489-500(2012).
CC -!- FUNCTION: Member of the two-component regulatory system TodS/TodT
CC involved in the regulation of toluene degradation. Phosphorylates TodT
CC via a four-step phosphorelay in response to toluene. Can also be
CC induced by benzene and ethylbenzene. {ECO:0000269|PubMed:16702539,
CC ECO:0000269|PubMed:19240030, ECO:0000269|PubMed:22212183}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC histidine.; EC=2.7.13.3; Evidence={ECO:0000269|PubMed:16702539,
CC ECO:0000269|PubMed:19240030};
CC -!- ACTIVITY REGULATION: Activity is regulated by agonists and antagonists.
CC Binding of agonists such as toluene or benzene to TodS stimulates
CC autophosphorylation at His-190. Activity is inhibited by antagonists
CC such as o-xylene, o-chlorotoluene and trimethylbenzene isomers, which
CC bind to TodS but do not stimulate autophosphorylation. Agonists and
CC antagonists bind to the same PAS domain. {ECO:0000269|PubMed:17693554,
CC ECO:0000269|PubMed:19240030, ECO:0000269|PubMed:22212183}.
CC -!- INTERACTION:
CC E0X9C7; E0X9C7: todS; NbExp=2; IntAct=EBI-15583094, EBI-15583094;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22212183}.
CC -!- INDUCTION: Constitutively expressed. Is under catabolite repression.
CC {ECO:0000269|PubMed:20543072}.
CC -!- DOMAIN: Toluene binds to the N-terminal PAS sensor domain but not to
CC the C-terminal PAS domain. The two PAS sensor domains may sense two
CC different signals. {ECO:0000269|PubMed:16702539,
CC ECO:0000269|PubMed:19240030}.
CC -!- PTM: Autophosphorylated. Activation requires a sequential transfer of a
CC phosphate group from a His in the primary transmitter domain, to an Asp
CC in the receiver domain and to a His in the secondary transmitter
CC domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=AFO50104.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AFO50104.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AFO50105.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AFO50105.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; GQ884177; ADI95406.1; -; Genomic_DNA.
DR EMBL; CP003734; AFO50104.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP003734; AFO50105.1; ALT_SEQ; Genomic_DNA.
DR AlphaFoldDB; E0X9C7; -.
DR SMR; E0X9C7; -.
DR DIP; DIP-61171N; -.
DR IntAct; E0X9C7; 1.
DR EnsemblBacteria; AFO50104; AFO50104; T1E_4275.
DR EnsemblBacteria; AFO50105; AFO50105; T1E_4276.
DR KEGG; ppx:T1E_4275; -.
DR KEGG; ppx:T1E_4276; -.
DR PATRIC; fig|1196325.3.peg.4232; -.
DR HOGENOM; CLU_000445_89_2_6; -.
DR Proteomes; UP000006503; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd00082; HisKA; 2.
DR CDD; cd00130; PAS; 2.
DR Gene3D; 3.30.565.10; -; 2.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR005467; His_kinase_dom.
DR InterPro; IPR003661; HisK_dim/P.
DR InterPro; IPR036097; HisK_dim/P_sf.
DR InterPro; IPR001610; PAC.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013656; PAS_4.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR Pfam; PF02518; HATPase_c; 2.
DR Pfam; PF00512; HisKA; 2.
DR Pfam; PF08448; PAS_4; 1.
DR Pfam; PF13426; PAS_9; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 2.
DR SMART; SM00388; HisKA; 2.
DR SMART; SM00086; PAC; 2.
DR SMART; SM00091; PAS; 2.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF47384; SSF47384; 2.
DR SUPFAM; SSF52172; SSF52172; 1.
DR SUPFAM; SSF55785; SSF55785; 2.
DR SUPFAM; SSF55874; SSF55874; 2.
DR TIGRFAMs; TIGR00229; sensory_box; 2.
DR PROSITE; PS50109; HIS_KIN; 2.
DR PROSITE; PS50113; PAC; 2.
DR PROSITE; PS50112; PAS; 2.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cytoplasm; Kinase; Nucleotide-binding; Phosphoprotein; Repeat;
KW Transferase; Two-component regulatory system.
FT CHAIN 1..978
FT /note="Sensor histidine kinase TodS"
FT /id="PRO_0000423590"
FT DOMAIN 32..103
FT /note="PAS 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00140"
FT DOMAIN 108..162
FT /note="PAC 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00141"
FT DOMAIN 187..405
FT /note="Histidine kinase 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT DOMAIN 452..567
FT /note="Response regulatory"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT DOMAIN 611..681
FT /note="PAS 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00140"
FT DOMAIN 685..737
FT /note="PAC 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00141"
FT DOMAIN 757..974
FT /note="Histidine kinase 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT MOD_RES 190
FT /note="Phosphohistidine; by autocatalysis"
FT /evidence="ECO:0000305"
FT MOD_RES 500
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000305"
FT MOD_RES 760
FT /note="Phosphohistidine"
FT /evidence="ECO:0000305"
FT MUTAGEN 46
FT /note="F->A: Decreases affinity for agonists and
FT antagonists."
FT /evidence="ECO:0000269|PubMed:17693554"
FT MUTAGEN 74
FT /note="I->A: Decreases affinity for agonists and
FT antagonists."
FT /evidence="ECO:0000269|PubMed:17693554"
FT MUTAGEN 79
FT /note="F->A: Does not bind agonists and antagonists. Does
FT not stimulate autophosphorylation and transcription of
FT target genes."
FT /evidence="ECO:0000269|PubMed:17693554"
FT MUTAGEN 114
FT /note="I->A: Decreases affinity for agonists and
FT antagonists."
FT /evidence="ECO:0000269|PubMed:17693554"
FT MUTAGEN 190
FT /note="H->A: Strong decrease in TodT phosphorylation."
FT /evidence="ECO:0000269|PubMed:19240030"
FT MUTAGEN 500
FT /note="D->A: Strong decrease in TodT phosphorylation."
FT /evidence="ECO:0000269|PubMed:19240030"
FT MUTAGEN 760
FT /note="H->A: Lack of TodT phosphorylation."
FT /evidence="ECO:0000269|PubMed:19240030"
SQ 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
