TORS_ECOLI
ID TORS_ECOLI Reviewed; 914 AA.
AC P39453; P75887;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 29-AUG-2001, sequence version 4.
DT 03-AUG-2022, entry version 191.
DE RecName: Full=Sensor protein TorS;
DE EC=2.7.13.3;
GN Name=torS; Synonyms=yccI; OrderedLocusNames=b0993, JW5135;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS TORS13; TORS726 AND
RP TORS729.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=8809780; DOI=10.1111/j.1365-2958.1996.tb02648.x;
RA Jourlin C., Bengrine A., Chippaux M., Mejean V.;
RT "An unorthodox sensor protein (TorS) mediates the induction of the tor
RT structural genes in response to trimethylamine N-oxide in Escherichia
RT coli.";
RL Mol. Microbiol. 20:1297-1306(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA Horiuchi T.;
RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 12.7-28.0 min region on the linkage map.";
RL DNA Res. 3:137-155(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-114.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=8083154; DOI=10.1128/jb.176.18.5601-5606.1994;
RA Simon G., Mejean V., Jourlin C., Chippaux M., Pascal M.-C.;
RT "The torR gene of Escherichia coli encodes a response regulator protein
RT involved in the expression of the trimethylamine N-oxide reductase genes.";
RL J. Bacteriol. 176:5601-5606(1994).
RN [6]
RP MUTAGENESIS OF HIS-453; ASP-733 AND HIS-860.
RX PubMed=9135110; DOI=10.1006/jmbi.1997.0919;
RA Jourlin C., Ansaldi M., Mejean V.;
RT "Transphosphorylation of the TorR response regulator requires the three
RT phosphorylation sites of the TorS unorthodox sensor in Escherichia coli.";
RL J. Mol. Biol. 267:770-777(1997).
RN [7]
RP CHARACTERIZATION.
RX PubMed=11274133; DOI=10.1128/jb.183.8.2691-2695.2001;
RA Ansaldi M., Jourlin-Castelli C., Lepelletier M., Theraulaz L., Mejean V.;
RT "Rapid dephosphorylation of the TorR response regulator by the TorS
RT unorthodox sensor in Escherichia coli.";
RL J. Bacteriol. 183:2691-2695(2001).
RN [8]
RP SUBCELLULAR LOCATION.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=15919996; DOI=10.1126/science.1109730;
RA Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.;
RT "Global topology analysis of the Escherichia coli inner membrane
RT proteome.";
RL Science 308:1321-1323(2005).
CC -!- FUNCTION: Member of the two-component regulatory system TorS/TorR
CC involved in the anaerobic utilization of trimethylamine-N-oxide (TMAO).
CC Detects the presence of TMAO in the medium and, in response, activates
CC TorR via a four-step phosphorelay. When TMAO is removed, TorS can
CC dephosphorylate TorR, probably by a reverse phosphorelay involving His-
CC 860 and Asp-733.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC histidine.; EC=2.7.13.3;
CC -!- ACTIVITY REGULATION: Inhibited by TorC apocytochrome.
CC -!- SUBUNIT: May form homomultimers. Seems to interact with TorT and TorC
CC apocytochrome.
CC -!- INTERACTION:
CC P39453; P39453: torS; NbExp=2; IntAct=EBI-9149134, EBI-9149134;
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000269|PubMed:15919996}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:15919996}.
CC -!- PTM: Activation requires a sequential transfer of a phosphate group
CC from a His in the primary transmitter domain, to an Asp in the receiver
CC domain and to a His in the secondary transmitter domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA63920.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; X94231; CAA63920.1; ALT_INIT; Genomic_DNA.
DR EMBL; U00096; AAC74078.2; -; Genomic_DNA.
DR EMBL; AP009048; BAA36135.2; -; Genomic_DNA.
DR PIR; G64840; G64840.
DR RefSeq; NP_415513.2; NC_000913.3.
DR RefSeq; WP_001300633.1; NZ_LN832404.1.
DR PDB; 3I9W; X-ray; 2.70 A; A=35-320.
DR PDBsum; 3I9W; -.
DR AlphaFoldDB; P39453; -.
DR SMR; P39453; -.
DR BioGRID; 4262839; 4.
DR BioGRID; 849969; 1.
DR DIP; DIP-11017N; -.
DR IntAct; P39453; 1.
DR STRING; 511145.b0993; -.
DR iPTMnet; P39453; -.
DR jPOST; P39453; -.
DR PaxDb; P39453; -.
DR PRIDE; P39453; -.
DR EnsemblBacteria; AAC74078; AAC74078; b0993.
DR EnsemblBacteria; BAA36135; BAA36135; BAA36135.
DR GeneID; 945595; -.
DR KEGG; ecj:JW5135; -.
DR KEGG; eco:b0993; -.
DR PATRIC; fig|511145.12.peg.1029; -.
DR EchoBASE; EB2501; -.
DR eggNOG; COG0784; Bacteria.
DR eggNOG; COG2198; Bacteria.
DR eggNOG; COG2205; Bacteria.
DR HOGENOM; CLU_000445_40_1_6; -.
DR InParanoid; P39453; -.
DR OMA; VMLDIQL; -.
DR PhylomeDB; P39453; -.
DR BioCyc; EcoCyc:TORS-MON; -.
DR BioCyc; MetaCyc:TORS-MON; -.
DR BRENDA; 2.7.13.3; 2026.
DR EvolutionaryTrace; P39453; -.
DR PRO; PR:P39453; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0004721; F:phosphoprotein phosphatase activity; IDA:EcoCyc.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IMP:EcoCyc.
DR GO; GO:0009061; P:anaerobic respiration; IMP:EcoCyc.
DR GO; GO:0071310; P:cellular response to organic substance; IMP:EcoCyc.
DR GO; GO:0000160; P:phosphorelay signal transduction system; IMP:EcoCyc.
DR GO; GO:0046777; P:protein autophosphorylation; IMP:EcoCyc.
DR GO; GO:0006470; P:protein dephosphorylation; IDA:EcoCyc.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00088; HPT; 1.
DR CDD; cd16172; TorS_sensor_domain; 1.
DR Gene3D; 1.20.120.160; -; 1.
DR Gene3D; 1.20.58.920; -; 1.
DR Gene3D; 3.30.565.10; -; 1.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR003660; HAMP_dom.
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; IPR036641; HPT_dom_sf.
DR InterPro; IPR037952; Sensor_TorS.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR008207; Sig_transdc_His_kin_Hpt_dom.
DR InterPro; IPR014302; Sig_transdc_His_kinase_TorS.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR InterPro; IPR038188; TorS_sensor_sf.
DR Pfam; PF00672; HAMP; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF01627; Hpt; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PIRSF; PIRSF036437; HK_TorS; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00304; HAMP; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00073; HPT; 1.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF47226; SSF47226; 1.
DR SUPFAM; SSF47384; SSF47384; 1.
DR SUPFAM; SSF52172; SSF52172; 1.
DR SUPFAM; SSF55874; SSF55874; 1.
DR TIGRFAMs; TIGR02956; TMAO_torS; 1.
DR PROSITE; PS50885; HAMP; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50894; HPT; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cell inner membrane; Cell membrane; Kinase;
KW Membrane; Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Transferase; Transmembrane; Transmembrane helix;
KW Two-component regulatory system.
FT CHAIN 1..914
FT /note="Sensor protein TorS"
FT /id="PRO_0000074888"
FT TOPO_DOM 1..8
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 9..29
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 30..332
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 333..353
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 354..914
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 354..407
FT /note="HAMP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00102"
FT DOMAIN 450..664
FT /note="Histidine kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT DOMAIN 683..798
FT /note="Response regulatory"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT DOMAIN 821..914
FT /note="HPt"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00110"
FT MOD_RES 453
FT /note="Phosphohistidine; by autocatalysis"
FT /evidence="ECO:0000305"
FT MOD_RES 733
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000305"
FT MOD_RES 860
FT /note="Phosphohistidine"
FT /evidence="ECO:0000305"
FT VARIANT 295..297
FT /note="Missing (in torS726; constitutively active)"
FT VARIANT 408
FT /note="H -> L (in torS729; partial activation)"
FT VARIANT 414
FT /note="A -> P (in torS13; partial activation)"
FT MUTAGEN 453
FT /note="H->Q: Loss of activity."
FT /evidence="ECO:0000269|PubMed:9135110"
FT MUTAGEN 733
FT /note="D->A,E: Loss of activity."
FT /evidence="ECO:0000269|PubMed:9135110"
FT MUTAGEN 860
FT /note="H->Q: Decrease in activity."
FT /evidence="ECO:0000269|PubMed:9135110"
FT CONFLICT 771..772
FT /note="QR -> HG (in Ref. 1; CAA63920)"
FT /evidence="ECO:0000305"
FT HELIX 49..71
FT /evidence="ECO:0007829|PDB:3I9W"
FT HELIX 75..100
FT /evidence="ECO:0007829|PDB:3I9W"
FT TURN 101..103
FT /evidence="ECO:0007829|PDB:3I9W"
FT HELIX 107..173
FT /evidence="ECO:0007829|PDB:3I9W"
FT TURN 177..179
FT /evidence="ECO:0007829|PDB:3I9W"
FT HELIX 182..218
FT /evidence="ECO:0007829|PDB:3I9W"
FT HELIX 223..227
FT /evidence="ECO:0007829|PDB:3I9W"
FT HELIX 229..247
FT /evidence="ECO:0007829|PDB:3I9W"
FT HELIX 253..266
FT /evidence="ECO:0007829|PDB:3I9W"
FT HELIX 269..313
FT /evidence="ECO:0007829|PDB:3I9W"
SQ SEQUENCE 914 AA; 101024 MW; 45D66BD027B69FCD CRC64;
MNLTLTRRLW MGFALMALLT LTSTLVGWYN LRFISQVEKD NTQALIPTMN MARQLSEASA
WELFAAQNLT SADNEKMWQA QGRMLTAQSL KINALLQALR EQGFDTTAIE QQEQEISRSL
RQQGELVGQR LQLRQQQQQL SQQIVAAADE IARLAQGQAN NATTSAGATQ AGIYDLIEQD
QRQAAESALD RLIDIDLEYV NQMNELRLSA LRVQQMVMNL GLEQIQKNAP TLEKQLNNAV
KILQRRQIRI EDPGVRAQVA TTLTTVSQYS DLLALYQQDS EISNHLQTLA QNNIAQFAQF
SSEVSQLVDT IELRNQHGLA HLEKASARGQ YSLLLLGMVS LCALILILWR VVYRSVTRPL
AEQTQALQRL LDGDIDSPFP ETAGVRELDT IGRLMDAFRS NVHALNRHRE QLAAQVKART
AELQELVIEH RQARAEAEKA SQAKSAFLAA MSHEIRTPLY GILGTAQLLA DNPALNAQRD
DLRAITDSGE SLLTILNDIL DYSAIEAGGK NVSVSDEPFE PRPLLESTLQ LMSGRVKGRP
IRLATAIADD MPCALMGDPR RIRQVITNLL SNALRFTDEG YIILRSRTDG EQWLVEVEDS
GCGIDPAKLA EIFQPFVQVS GKRGGTGLGL TISSRLAQAM GGELSATSTP EVGSCFCLRL
PLRVATAPVP KTVNQAVRLD GLRLLLIEDN PLTQRITIEM LKTSGAQIVA VGNAAQALET
LQNSEPFAAA LVDFDLPDID GITLARQLAQ QYPSLVLIGF SAHVIDETLR QRTSSLFRGI
IPKPVPREVL GQLLAHYLQL QVNNDQSLDV SQLNEDAQLM GTEKIHEWLV LFTQHALPLL
DEIDIARASQ DSEKIKRAAH QLKSSCSSLG MHIASQLCAQ LEQQPLSAPL PHEEITRSVA
ALEAWLHKKD LNAI
