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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
 
 
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