TODS_PSEP1
ID TODS_PSEP1 Reviewed; 978 AA.
AC A5W4E3; O07831;
DT 16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 1.
DT 25-MAY-2022, entry version 91.
DE RecName: Full=Sensor histidine kinase TodS;
DE EC=2.7.13.3;
GN Name=todS; OrderedLocusNames=Pput_2872;
OS Pseudomonas putida (strain ATCC 700007 / DSM 6899 / BCRC 17059 / F1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=351746;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBUNIT, SUBCELLULAR LOCATION,
RP DOMAIN, DISRUPTION PHENOTYPE, AND GENE NAME.
RC STRAIN=ATCC 700007 / DSM 6899 / BCRC 17059 / F1;
RX PubMed=9037074; DOI=10.1073/pnas.94.4.1453;
RA Lau P.C., Wang Y., Patel A., Labbe D., Bergeron H., Brousseau R.,
RA Konishi Y., Rawlings M.;
RT "A bacterial basic region leucine zipper histidine kinase regulating
RT toluene degradation.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:1453-1458(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700007 / DSM 6899 / BCRC 17059 / F1;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Lykidis A., Parales R., Richardson P.;
RT "Complete sequence of Pseudomonas putida F1.";
RL Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases.
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 (Probable).
CC {ECO:0000305|PubMed:9037074}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC histidine.; EC=2.7.13.3;
CC -!- SUBUNIT: Homodimer. Binds as a dimer to a pseudopalindromic sequence.
CC {ECO:0000269|PubMed:9037074}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9037074}.
CC -!- DOMAIN: Contains a basic region leucine zipper dimerization motif at
CC the N-terminus. {ECO:0000269|PubMed:9037074}.
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 domain
CC (By similarity). {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Mutants are unable to use toluene as the sole
CC carbon source, are incapable of converting indole to indigo and do not
CC have catechol dioxygenase activity. {ECO:0000269|PubMed:9037074}.
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DR EMBL; U72354; AAC45438.1; -; Genomic_DNA.
DR EMBL; CP000712; ABQ79003.1; -; Genomic_DNA.
DR RefSeq; WP_012052592.1; NC_009512.1.
DR PDB; 5HWT; X-ray; 1.70 A; A/B=43-168.
DR PDB; 5HWV; X-ray; 1.65 A; A/B=43-168.
DR PDB; 5HWW; X-ray; 2.00 A; A/B=43-168.
DR PDBsum; 5HWT; -.
DR PDBsum; 5HWV; -.
DR PDBsum; 5HWW; -.
DR AlphaFoldDB; A5W4E3; -.
DR SMR; A5W4E3; -.
DR STRING; 351746.Pput_2872; -.
DR EnsemblBacteria; ABQ79003; ABQ79003; Pput_2872.
DR KEGG; ppf:Pput_2872; -.
DR eggNOG; COG0745; Bacteria.
DR eggNOG; COG2205; Bacteria.
DR eggNOG; COG4191; Bacteria.
DR HOGENOM; CLU_000445_82_2_6; -.
DR OMA; FFAKVSH; -.
DR OrthoDB; 1755994at2; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cytoplasm; Kinase; Nucleotide-binding;
KW Phosphoprotein; Repeat; Transferase; Two-component regulatory system.
FT CHAIN 1..978
FT /note="Sensor histidine kinase TodS"
FT /id="PRO_0000423591"
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:0000255|PROSITE-ProRule:PRU00107"
FT MOD_RES 500
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT MOD_RES 760
FT /note="Phosphohistidine"
FT /evidence="ECO:0000250"
FT CONFLICT 202..208
FT /note="PLEAVMA -> HWKPLWR (in Ref. 1; AAC45438)"
FT /evidence="ECO:0000305"
FT STRAND 45..51
FT /evidence="ECO:0007829|PDB:5HWV"
FT STRAND 54..59
FT /evidence="ECO:0007829|PDB:5HWV"
FT HELIX 61..67
FT /evidence="ECO:0007829|PDB:5HWV"
FT HELIX 71..74
FT /evidence="ECO:0007829|PDB:5HWV"
FT HELIX 79..81
FT /evidence="ECO:0007829|PDB:5HWV"
FT HELIX 83..85
FT /evidence="ECO:0007829|PDB:5HWV"
FT HELIX 89..103
FT /evidence="ECO:0007829|PDB:5HWV"
FT STRAND 108..117
FT /evidence="ECO:0007829|PDB:5HWV"
FT HELIX 118..120
FT /evidence="ECO:0007829|PDB:5HWV"
FT STRAND 122..134
FT /evidence="ECO:0007829|PDB:5HWV"
FT STRAND 140..149
FT /evidence="ECO:0007829|PDB:5HWV"
FT HELIX 151..164
FT /evidence="ECO:0007829|PDB:5HWV"
SQ SEQUENCE 978 AA; 107933 MW; AB011A49F6B62AF9 CRC64;
MSSLDRKKPQ NRSKNNYYNI CLKEKGSEEL TCEEHARIIF DGLYEFVGLL DAHGNVLEVN
QVALEGGGIT LEEIRGKPFW KARWWQISKK TEATQKRLVE TASSGEFVRC DVEILGKSGG
REVIAVDFSL LPICNEEGSI VYLLAEGRNI TDKKKAEAML ALKNQELEQS VECIRKLDNA
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 LIMPVMSGDM 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
