GenomeNet

Database: UniProt
Entry: Q47T93_THEFY
LinkDB: Q47T93_THEFY
Original site: Q47T93_THEFY 
ID   Q47T93_THEFY            Unreviewed;      1406 AA.
AC   Q47T93;
DT   13-SEP-2005, integrated into UniProtKB/TrEMBL.
DT   13-SEP-2005, sequence version 1.
DT   27-MAR-2024, entry version 140.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   OrderedLocusNames=Tfu_0286 {ECO:0000313|EMBL:AAZ54324.1};
OS   Thermobifida fusca (strain YX).
OC   Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC   Nocardiopsaceae; Thermobifida.
OX   NCBI_TaxID=269800 {ECO:0000313|EMBL:AAZ54324.1};
RN   [1] {ECO:0000313|EMBL:AAZ54324.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=YX {ECO:0000313|EMBL:AAZ54324.1};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Di Bartolo G., Chain P., Schmutz J.,
RA   Larimer F., Land M., Lykidis A., Richardson P.;
RT   "Complete sequence of Thermobifida fusca YX.";
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000088; AAZ54324.1; -; Genomic_DNA.
DR   STRING; 269800.Tfu_0286; -.
DR   KEGG; tfu:Tfu_0286; -.
DR   eggNOG; COG0745; Bacteria.
DR   eggNOG; COG1511; Bacteria.
DR   eggNOG; COG2203; Bacteria.
DR   eggNOG; COG2205; Bacteria.
DR   HOGENOM; CLU_000445_3_0_11; -.
DR   GO; GO:0016020; C:membrane; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   CDD; cd06225; HAMP; 6.
DR   CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR   CDD; cd00082; HisKA; 1.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 1.20.120.1530; -; 4.
DR   Gene3D; 3.30.450.40; -; 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; 1.10.287.950; Methyl-accepting chemotaxis protein; 1.
DR   InterPro; IPR011006; CheY-like_superfamily.
DR   InterPro; IPR003018; GAF.
DR   InterPro; IPR029016; GAF-like_dom_sf.
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; IPR004358; Sig_transdc_His_kin-like_C.
DR   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR   PANTHER; PTHR45339; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR   PANTHER; PTHR45339:SF1; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR   Pfam; PF13185; GAF_2; 1.
DR   Pfam; PF00672; HAMP; 4.
DR   Pfam; PF18947; HAMP_2; 3.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF00072; Response_reg; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00065; GAF; 1.
DR   SMART; SM00304; HAMP; 8.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 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; SSF55781; GAF domain-like; 1.
DR   SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR   SUPFAM; SSF58104; Methyl-accepting chemotaxis protein (MCP) signaling domain; 3.
DR   PROSITE; PS50885; HAMP; 7.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:AAZ54324.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW   ProRule:PRU00169};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:AAZ54324.1}.
FT   DOMAIN          104..161
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          201..253
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          293..345
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          385..437
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          477..529
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          569..621
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          661..713
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          964..1197
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          1276..1393
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   REGION          1224..1247
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          885..954
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   MOD_RES         1326
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   1406 AA;  153442 MW;  F869629E2A9CAD45 CRC64;
     MPRLMPRMKN RTLTESELDA LLDALYRMRD GDFTVRLSPR GATRFSEVAR VLNEVFDQCE
     QLSNEVQWVS ETVSTDGRLS ERVSISPARG SWGQSVRALN QMLDEVSEPV TAVARILDSV
     ANGDLSQRVD LASRHGELHG DLLRLATSVN RMADQMSEFA GEVTRVAREV GTEGKLGGRA
     NVKGVSGIWK DLTDNVNSMA DNLTNQVRDI SQVTTAVARG DLTKKVTVDV QGEMLQLKDT
     VNTMVDQLST FADEVTRVAR EVGTEGKLGG RANVKGVSGI WKDLTDNVNS MADNLTNQVR
     DISQVTTAVA RGDLTKKVTV DVQGEMLQLK DTVNTMVDQL STFADEVTRV AREVGTEGKL
     GGRANVKGVS GIWKDLTDNV NSMADSLTHQ VRNISQVTSA VAAGDLTKKI TVDAQGEILE
     LKDTVNTMVD QLSAFADEVT RVAREVGTEG KLGGQAHVSG VSGVWKDLTD NVNSMANNLT
     HQVRQISVVT TAVARGDLTK KVTVNAKGEI LELKDTINTM VDQLSTFADE VTRVTREVGT
     EGKLGGRANV KGVSGIWKDL TDNVNSMSHN LTTQVRNISQ VTTAVARGDL TKRITVDAQG
     EMLELKDTIN TMVDQLSTFA LEVTRVGHEV GIEGKLGVQA KVAGVSGVWK DLTDSVNELA
     KNLTTQVRAI ASVASAVARG DLTQSIQVSA RGELATLKDN VNLMVSNLRE TTAAQRDEDW
     LKSNLARLSG LLQGRRDLNE LARLIMTEVT PLVDAQHGAC YLPEDENDTE TFRLYAGYGY
     QPSEERRRIT AGQGLAGEAI AQRKELIVHN VPGDYVRIES GLGEAPPLSL AIFPIVSEDR
     VLGVIELGSY GTFREIHLNF LRQLVSLLSA TITTILANSK TEYLLAQSQQ LTTALQERSN
     ELQRQQEELR RKNAELHSKA GQLASQNRAI ELQNRQIERA RRSLEDRAHQ LQVSSKYKSE
     FLANMSHELR TPLNSLLILA RLLADNSEKN LTPKQVEFAQ TIYKAGSDLL QLINEILDLS
     KVEAGRMELN PSHVSISQLV DYVEASFRPL ASEKGLAFAV EVSPDVPDQL WTDEQRLQQV
     LRNLLSNAVK FTSSGEVRLV IEPAWAVEDI DVDTFTDPDE VIAFSVIDTG IGIPEDKLQL
     IFEAFHQGDG GTSRRFGGTG LGLSISRNMA ELLGGEIRVS STVGEGSTFT LLLPVRLPEG
     TSERMYRSLS DADVVTSFDR PTDTVVLPTE TPGPKAADTD PLASSEDEPY VPVLTAESVP
     QAAGGPQQDD VLAGKRVLIV DDDIRNVFAL ASALEAHGLE VLYADNGREG IAKLEANEDI
     DLVLMDIMMP ELDGDATTRM IREMPQFADL PIISLTAKAM RGDRENSLAA GASDYVSKPV
     DLDHLLNVMR RWLDRGKSDN STSREQ
//
DBGET integrated database retrieval system