ID Q1RDM4_ECOUT Unreviewed; 910 AA.
AC Q1RDM4;
DT 16-MAY-2006, integrated into UniProtKB/TrEMBL.
DT 16-MAY-2006, sequence version 1.
DT 27-MAR-2024, entry version 128.
DE RecName: Full=Chemotaxis protein CheY {ECO:0000256|ARBA:ARBA00040987};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN Name=torS {ECO:0000313|EMBL:ABE06540.1};
GN OrderedLocusNames=UTI89_C1056 {ECO:0000313|EMBL:ABE06540.1};
OS Escherichia coli (strain UTI89 / UPEC).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=364106 {ECO:0000313|EMBL:ABE06540.1, ECO:0000313|Proteomes:UP000001952};
RN [1] {ECO:0000313|EMBL:ABE06540.1, ECO:0000313|Proteomes:UP000001952}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UTI89 / UPEC {ECO:0000313|Proteomes:UP000001952};
RX PubMed=16585510; DOI=10.1073/pnas.0600938103;
RA Chen S.L., Hung C.S., Xu J., Reigstad C.S., Magrini V., Sabo A.,
RA Blasiar D., Bieri T., Meyer R.R., Ozersky P., Armstrong J.R., Fulton R.S.,
RA Latreille J.P., Spieth J., Hooton T.M., Mardis E.R., Hultgren S.J.,
RA Gordon J.I.;
RT "Identification of genes subject to positive selection in uropathogenic
RT strains of Escherichia coli: a comparative genomics approach.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:5977-5982(2006).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC histidine.; EC=2.7.13.3; Evidence={ECO:0000256|ARBA:ARBA00000085};
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000256|ARBA:ARBA00004429}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004429}.
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DR EMBL; CP000243; ABE06540.1; -; Genomic_DNA.
DR AlphaFoldDB; Q1RDM4; -.
DR KEGG; eci:UTI89_C1056; -.
DR HOGENOM; CLU_000445_40_1_6; -.
DR Proteomes; UP000001952; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd06225; HAMP; 1.
DR CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00088; HPT; 1.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR CDD; cd16172; TorS_sensor_domain; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 1.20.58.920; -; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 6.10.340.10; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 1.20.120.160; HPT domain; 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 NCBIfam; TIGR02956; TMAO_torS; 1.
DR PANTHER; PTHR43047:SF72; OSMOSENSING HISTIDINE PROTEIN KINASE SLN1; 1.
DR PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 1.
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 Pfam; PF21689; TorS_sensor_domain; 1.
DR PIRSF; PIRSF036437; HK_TorS; 2.
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; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF52172; CheY-like; 1.
DR SUPFAM; SSF47226; Histidine-containing phosphotransfer domain, HPT domain; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50885; HAMP; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50894; HPT; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777}; Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ABE06540.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT TRANSMEM 12..31
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 331..352
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 354..410
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 450..664
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 683..798
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 821..905
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT COILED 409..443
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 733
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 860
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 910 AA; 100673 MW; F8C40AA9070C84CD CRC64;
MNLTLTRRLW MGFALMALLT LTSTLVGWYN LRFISQVEKD NTQALIPTMN MARQLSEASA
WELFAAQNLT SADNEKMWQA QGRMLTAQSL KINALLQALR EQGFDTTAIE QQEQEISRSL
RQQGELVGQR LQLRQQQQQL SQQIVAAADE IARLAQGQAN NAATSAGATQ AGIYDLIEQH
QRQAAESALD RLIDIDLEYV NQMNELRLSA LRVQQMVMNL GLEQIQKNAP TLEKQLNNAV
KILQRRQIRI EDPGVRTQVA TTLTTVSQYS DLLALYQQDS EISNHLQTLA QNNIAQFAQF
SSEVSQLVDT IELRNQHGLA HLEKASARGQ YSLLLLGLVS LCALILILWR VVYRSVTRPL
AEQTQALQRL LDGDIDSPFP ETAGVRELDT IGRLMDAFRS SVHALNRHRE QLAAQVKART
AELQELVIEH RQARAEAEKA SQAKSAFLAA MSHEIRTPLY GILGTAQLLA DNPALNAQRD
DLRAITDSGE SLLTILNDIL DYSAIEAGGK NVSVSDEPFE PRPLLESTLQ LMSGRVKGRP
IRLATEIADD VPTALMGDPR RIRQVITNLL SNALRFTDEG HIILRSRTDG EQWLVEVEDS
GCGIDPAKLA EIFQPFVQVS SKRGGTGLGL TISSRLAQAM GGELSATSTP EVGSCFCLRL
PLRIATAPVP KTVNQAVRLD DLRLLLIEDN PLTQRITVEM LNTSGAQVVA VGNAAQAIEA
LQNSEPFAAA LVDFDLPDID GITLARQLAQ QYPSLVLIGF SAHVIDETLR QRTSSLFRGI
IPKPVPREVL GQLLAHYLQL QVNNDQPLDV SQLNEDAHLM GAEKIHEWLI LFKQHALPLL
DEIDIARASQ DNEKIKRAAH QLKSSCSSLG MRSASQQCAQ LEQQPLSAPL PHEEITRSVA
ALEAWLIRKT
//
