ID TMOS_PSEME Reviewed; 973 AA.
AC Q8KIY1;
DT 16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 27-MAR-2024, entry version 93.
DE RecName: Full=Sensor histidine kinase TmoS;
DE EC=2.7.13.3;
GN Name=tmoS;
OS Pseudomonas mendocina.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=300;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND GENE NAME.
RC STRAIN=KR1;
RX PubMed=12446657; DOI=10.1128/jb.184.24.7062-7067.2002;
RA Ramos-Gonzalez M.I., Olson M., Gatenby A.A., Mosqueda G., Manzanera M.,
RA Campos M.J., Vichez S., Ramos J.L.;
RT "Cross-regulation between a novel two-component signal transduction system
RT for catabolism of toluene in Pseudomonas mendocina and the TodST system
RT from Pseudomonas putida.";
RL J. Bacteriol. 184:7062-7067(2002).
RN [2]
RP FUNCTION, ACTIVITY REGULATION, SUBCELLULAR LOCATION, AND
RP AUTOPHOSPHORYLATION.
RC STRAIN=KR1;
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 TmoS/TmoT
CC involved in the regulation of toluene degradation. Probably
CC phosphorylates TmoT via a four-step phosphorelay in response to
CC toluene. Can also be induced by benzene and ethylbenzene.
CC {ECO:0000269|PubMed:12446657, 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;
CC -!- ACTIVITY REGULATION: Activity is regulated by agonists and antagonists.
CC Binding of agonists such as toluene or benzene to TmoS stimulates
CC autophosphorylation. Toluene causes the most pronounced increase,
CC followed by benzene, chlorobenzene and ethylbenzene. Activity is
CC inhibited by antagonists such as o-xylene, o-chlorotoluene and
CC trimethylbenzene isomers, which bind to TmoS but do not stimulate
CC autophosphorylation. {ECO:0000269|PubMed:22212183}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22212183}.
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 (Probable). {ECO:0000305}.
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DR EMBL; AY052500; AAL13332.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8KIY1; -.
DR SMR; Q8KIY1; -.
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; cd16920; HATPase_TmoS-FixL-DctS-like; 1.
DR CDD; cd00082; HisKA; 2.
DR CDD; cd00130; PAS; 2.
DR CDD; cd00156; REC; 1.
DR Gene3D; 1.10.287.130; -; 2.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 2.
DR Gene3D; 3.30.450.20; PAS domain; 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 NCBIfam; TIGR00229; sensory_box; 2.
DR PANTHER; PTHR43547:SF2; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE C; 1.
DR PANTHER; PTHR43547; TWO-COMPONENT HISTIDINE KINASE; 1.
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; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 2.
DR SUPFAM; SSF52172; CheY-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 2.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 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..973
FT /note="Sensor histidine kinase TmoS"
FT /id="PRO_0000423589"
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..973
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"
SQ SEQUENCE 973 AA; 107289 MW; 15545FD9BD89D094 CRC64;
MSSLDKRKTQ NRSKKNSYSI CLKEKASAEL KREELARIIF DGLYEFVGLL DAQGNVLEVN
QAALNGAGVT LEEIRGKPFW KARWWQISKE SVANQKRLVE AASSGEFVRC DIEILGKSGG
REVIAVDFSL LPIRDEQENI VFLLAEGRNI TDKKKAEAML ALKNHELEQL VERIRKLDNA
KSDFFAKVSH ELRTPLSLIL GPLETIMEAE SGRGSPYWKK FEVIQRNAMT LLKQVNTLLD
LAKMDAQQMG LSYRRADLSQ LTRVISSNFD GIAQQKSITL DAELPPHLIA EVDCEKYERI
ILNLLSNAFK FTPDGGLIRC HLSLSQPAHA LITVSDSGPG IPQNLRKEIF ERFHQLNQEG
QQANQGTGLG LSIVKEFVEL HHGTISVSDA PGGGALFQVK LPLNAPEGAY VANNAMSRSD
NPQTVNPDEY LLPIPTAGSG AELPQFQSDQ PRVLIVEDNP DMRCFIRDCL STDYQVYVAP
DGAKALELMC SAPPDLLITD LMMPVMSGDT LVHKVREKNE FAHIPIMVLS AKPDEKLRVK
LLSESVQDYL LKPFSAHELR ARVSNLISMK IAGDALRKEL SDQSNDIALL THRLIKSRHR
LQQSNIALTA SEARWKAVYE NSAAGIVLTD TENRILNANP AFQRITGYTE KDLAQLSMEQ
LTPPNERTQM KQRLARLLQS GGAEYSVECS YLCKNGSTIW ANASVSLMSP RVDEPQVILQ
IIDDITEKKQ AQETLNQLQQ ELVQVSRSAT MGEFAAYIAH EINQPLSAIM TNANAGTRWI
GNEPPNIMEA KEALARIIRD SDRAADIIRM VRSFLKRQGP VLKPIDLKAL VADTTLILKA
PSQSNGVSLN VIAGDTLPAI MGDAVQIQQL VINLAMNSIE AMSQVGCETR QLALSFSSNA
SNDALIICVK DTGPGIPEDQ IGQLFNAFYT TKKEGLGMGL AICLTIAEVH NGKIWAESPP
AGGACFFVSI PVS
//
