ID B5YFV1_THEYD Unreviewed; 890 AA.
AC B5YFV1;
DT 25-NOV-2008, integrated into UniProtKB/TrEMBL.
DT 25-NOV-2008, sequence version 1.
DT 27-MAR-2024, entry version 93.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=THEYE_A1339 {ECO:0000313|EMBL:ACI21526.1};
OS Thermodesulfovibrio yellowstonii (strain ATCC 51303 / DSM 11347 / YP87).
OC Bacteria; Nitrospirota; Thermodesulfovibrionia; Thermodesulfovibrionales;
OC Thermodesulfovibrionaceae; Thermodesulfovibrio.
OX NCBI_TaxID=289376 {ECO:0000313|EMBL:ACI21526.1, ECO:0000313|Proteomes:UP000000718};
RN [1] {ECO:0000313|Proteomes:UP000000718}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51303 / DSM 11347 / YP87
RC {ECO:0000313|Proteomes:UP000000718};
RA Dodson R.J., Durkin A.S., Wu M., Eisen J., Sutton G.;
RT "The complete genome sequence of Thermodesulfovibrio yellowstonii strain
RT ATCC 51303 / DSM 11347 / YP87.";
RL Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ACI21526.1, ECO:0000313|Proteomes:UP000000718}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51303 / DSM 11347 / YP87
RC {ECO:0000313|Proteomes:UP000000718};
RX PubMed=25635016;
RA Bhatnagar S., Badger J.H., Madupu R., Khouri H.M., O'Connor E.M.,
RA Robb F.T., Ward N.L., Eisen J.A.;
RT "Genome Sequence of the Sulfate-Reducing Thermophilic Bacterium
RT Thermodesulfovibrio yellowstonii Strain DSM 11347T (Phylum Nitrospirae).";
RL Genome Announc. 3:0-0(2015).
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 -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00169}.
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DR EMBL; CP001147; ACI21526.1; -; Genomic_DNA.
DR RefSeq; WP_012546240.1; NC_011296.1.
DR RefSeq; YP_002249149.1; NC_011296.1.
DR AlphaFoldDB; B5YFV1; -.
DR STRING; 289376.THEYE_A1339; -.
DR EnsemblBacteria; ACI21526; ACI21526; THEYE_A1339.
DR KEGG; tye:THEYE_A1339; -.
DR PATRIC; fig|289376.4.peg.1306; -.
DR eggNOG; COG0745; Bacteria.
DR eggNOG; COG5002; Bacteria.
DR HOGENOM; CLU_000445_104_15_0; -.
DR InParanoid; B5YFV1; -.
DR OrthoDB; 9762493at2; -.
DR Proteomes; UP000000718; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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 Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.450.290; -; 1.
DR Gene3D; 3.40.50.2300; -; 2.
DR Gene3D; 1.10.8.500; HAMP domain in histidine kinase; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal 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; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR PANTHER; PTHR43547:SF2; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE C; 1.
DR PANTHER; PTHR43547; TWO-COMPONENT HISTIDINE KINASE; 1.
DR Pfam; PF00672; HAMP; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00072; Response_reg; 2.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00304; HAMP; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00448; REC; 2.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF52172; CheY-like; 2.
DR SUPFAM; SSF158472; HAMP domain-like; 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; PS50110; RESPONSE_REGULATORY; 2.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:ACI21526.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000000718};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 13..35
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 193..211
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 213..264
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 307..534
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 649..761
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 768..884
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT COILED 260..303
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 697
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 890 AA; 100549 MW; C157A3E13A7542B4 CRC64;
MFKFITNKIG NKLMLTFIGI ILVVMIIEMT FRIYFGVQDR LRIAEMGNKE VMDTIYATMK
HPLTVGDSDT IHRDLDEIGQ KYKNISVYLC DFNRDISFST DKKVINTKID QIINNKDFID
NLNESFKGNG DEYKSLVFNI KERRNLISVL PIKNAPECFH CHGSSRKILG ALIMKTDVED
VYKTVIAQRN RSLALTAFAS LLAIFITNLV VSKFIRKPLS NLVDATHRFA KGEMSTIIKY
PPDEIGTLTE TFNYMVNEVA KSKMELEKEL TRRAKLLEER DELVALLQKA NKQLKELDTL
KSAFIANMSH ELRTPMNAII GYTDLLLDEV DGPLNDDQKT SLKKVAANAR HLLQLINDVL
DISKIESGKI ELHPREIDLK ELIDGIMVTF EPLIAKKGLS FTLNIESGAE KLYVDEDKTK
QILINLISNA VKFTHQGGIT IKAKVSERGK AKDGSPQFIE ISVSDTGIGI KREDLDKIFD
KFAQADVSTT RQYEGTGLGL SIVRGLVALH KGMVWAESEV GKGSTFYVLL PFKKEVFEQT
GPVIEEEMAE ALGEYFEVPK EVFLQDPSYE GKLVRCWDYT QCGHVNCPEY GSPEKRCWLV
VGTHCKGMKI GSYPEKADAC KLCEVVRDLV LHKEPLSPDI SKISEKEKVV LAIDDNPDAI
DLIKKYLEKD YKVIGILSSE EAVKKAKEIK PVAITLDIMM PKKDGWQVLK ELKEDEETKN
IPVIIVSIIE NKTLAFSLGA ADYFVKPLDG YSLLRRIKNI GIHRPIKKVF LLERDERTNY
DISKILKESG YEVYATNSSK QAMELVKSEK PDLLIVNITD PDSSAFDFID FIKTSAELRD
IPIIALTNKE LSEQEKEALN GRIKDIINKA LFSEEELITE LKNSLKKIGG
//
