TORS_ECO57
ID TORS_ECO57 Reviewed; 914 AA.
AC P58356;
DT 16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT 16-NOV-2001, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Sensor protein TorS;
DE EC=2.7.13.3;
GN Name=torS; OrderedLocusNames=Z1410, ECs1148;
OS Escherichia coli O157:H7.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83334;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=11206551; DOI=10.1038/35054089;
RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA Blattner F.R.;
RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL Nature 409:529-533(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA Shiba T., Hattori M., Shinagawa H.;
RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT genomic comparison with a laboratory strain K-12.";
RL DNA Res. 8:11-22(2001).
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 (By similarity). {ECO:0000250}.
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. {ECO:0000250}.
CC -!- SUBUNIT: May form homomultimers. Seems to interact with TorT and TorC
CC apocytochrome (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Multi-pass
CC membrane protein {ECO:0000250}.
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. {ECO:0000250}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG55540.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAB34571.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE005174; AAG55540.1; ALT_INIT; Genomic_DNA.
DR EMBL; BA000007; BAB34571.1; ALT_INIT; Genomic_DNA.
DR PIR; D90772; D90772.
DR PIR; H85634; H85634.
DR RefSeq; NP_309175.2; NC_002695.1.
DR RefSeq; WP_001054754.1; NZ_SWKA01000005.1.
DR AlphaFoldDB; P58356; -.
DR SMR; P58356; -.
DR STRING; 155864.EDL933_1331; -.
DR PRIDE; P58356; -.
DR EnsemblBacteria; AAG55540; AAG55540; Z1410.
DR EnsemblBacteria; BAB34571; BAB34571; ECs_1148.
DR GeneID; 913641; -.
DR KEGG; ece:Z1410; -.
DR KEGG; ecs:ECs_1148; -.
DR PATRIC; fig|386585.9.peg.1264; -.
DR eggNOG; COG0784; Bacteria.
DR eggNOG; COG2198; Bacteria.
DR eggNOG; COG2205; Bacteria.
DR HOGENOM; CLU_000445_40_1_6; -.
DR OMA; VMLDIQL; -.
DR BRENDA; 2.7.13.3; 2026.
DR Proteomes; UP000000558; Chromosome.
DR Proteomes; UP000002519; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; 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; 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 3: Inferred from homology;
KW ATP-binding; Cell inner membrane; Cell membrane; Kinase; Membrane;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; Transferase;
KW Transmembrane; Transmembrane helix; Two-component regulatory system.
FT CHAIN 1..914
FT /note="Sensor protein TorS"
FT /id="PRO_0000074889"
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..410
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:0000255|PROSITE-ProRule:PRU00107"
FT MOD_RES 733
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT MOD_RES 860
FT /note="Phosphohistidine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 914 AA; 100846 MW; 70EA83E00DD97386 CRC64;
MNLTLTRRLW MGFALMALLT LTSTLVGWYN LRFISQVEKD NTQALIPTMN MARQLSEASA
WELFAAQNLT SADNEKMWQA QGRMLTAQSL KINALLQALR EQGFDTTAIE QQEQEISRSL
RQQGELVGRR LQLRQQQQRL SQQIVAAADE IARLAQGQAN NAATSAGATQ AGIYDLIEQD
QRQAAESALD RLIDIDLEYV NQMNELRLSA LRVQQMVMNL GLEQIQKNAP TLEKQLNNAV
KILQRRQIRI EDPGVRAQVA TTLTTVSQYS DLLALFQQDS EISNHLQTLA QNNIAQFAQF
SSEVSQLVDT IELRNQHGLA HLEKASARGQ YSLLLLGMVS LCALILILWR VVYRSVTRPL
AEQTQALQRL LDGDIDSPFP ETAGVRELDT IGRLMDAFRS SVHALNRHRE QLAAQVKART
AELQELVIEH RQARAEAEKA SQAKSAFLAA MSHEIRTPLY GILGTAQLLA DNPALNAQRD
DLRAITDSGE SLLTILNDIL DYSAIEAGGK NVSVSDEPFE PRPLLESTLQ LMSGRVKGRP
IRLATAIADD VPTALMGDPR RIRQVITNLL SNALRFTDEG QIVLRSRTDG EQWLVEVEDS
GCGIDPAKLA EIFQPFIQVS GKRGGTGLGL TISSRLAQAM GGELSATSTP EVGSCFCLRL
PLRVATAPVP KTVNQAVRLD GLRLLLIEDN PLTQRITVEM LNTSGAQVVA IGNAAQALET
LQNSEPFAAA LVDFDLPDVN GITLARQLAR QYPSLVLIGF SAHVIDETLR QRTSSLFRGI
IPKPVPREVL GQLLAHYLQL QANNDLPLDV SQLNEDAQLM GTEKIHEWLA LFTQHALPLL
DEIDIARATQ DSEKIKRAAH QLKSSCSSLG MRSASQLCAQ LEQQPLSAPL PHEEITRSVA
ALEAWLNKKD LNAI
