ID B5YJ23_THEYD Unreviewed; 742 AA.
AC B5YJ23;
DT 25-NOV-2008, integrated into UniProtKB/TrEMBL.
DT 25-NOV-2008, sequence version 1.
DT 27-MAR-2024, entry version 94.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=THEYE_A0391 {ECO:0000313|EMBL:ACI20983.1};
OS Thermodesulfovibrio yellowstonii (strain ATCC 51303 / DSM 11347 / YP87).
OC Bacteria; Nitrospirota; Thermodesulfovibrionia; Thermodesulfovibrionales;
OC Thermodesulfovibrionaceae; Thermodesulfovibrio.
OX NCBI_TaxID=289376 {ECO:0000313|EMBL:ACI20983.1, 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:ACI20983.1, 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};
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DR EMBL; CP001147; ACI20983.1; -; Genomic_DNA.
DR RefSeq; WP_012545711.1; NC_011296.1.
DR RefSeq; YP_002248238.1; NC_011296.1.
DR AlphaFoldDB; B5YJ23; -.
DR STRING; 289376.THEYE_A0391; -.
DR EnsemblBacteria; ACI20983; ACI20983; THEYE_A0391.
DR KEGG; tye:THEYE_A0391; -.
DR PATRIC; fig|289376.4.peg.386; -.
DR eggNOG; COG0643; Bacteria.
DR eggNOG; COG0745; Bacteria.
DR eggNOG; COG2198; Bacteria.
DR HOGENOM; CLU_000650_3_7_0; -.
DR InParanoid; B5YJ23; -.
DR OrthoDB; 9803176at2; -.
DR Proteomes; UP000000718; Chromosome.
DR GO; GO:0004673; F:protein histidine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0006935; P:chemotaxis; IEA:InterPro.
DR GO; GO:0000160; P:phosphorelay signal transduction system; IEA:InterPro.
DR CDD; cd00088; HPT; 1.
DR Gene3D; 3.40.50.2300; -; 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; IPR036061; CheW-like_dom_sf.
DR InterPro; IPR002545; CheW-lke_dom.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR005467; His_kinase_dom.
DR InterPro; IPR036641; HPT_dom_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR008207; Sig_transdc_His_kin_Hpt_dom.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR PANTHER; PTHR43395:SF1; CHEMOTAXIS PROTEIN CHEA; 1.
DR PANTHER; PTHR43395; SENSOR HISTIDINE KINASE CHEA; 1.
DR Pfam; PF01584; CheW; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF01627; Hpt; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00260; CheW; 1.
DR SMART; SM00387; HATPase_c; 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; SSF50341; CheW-like; 1.
DR SUPFAM; SSF52172; CheY-like; 1.
DR SUPFAM; SSF47226; Histidine-containing phosphotransfer domain, HPT domain; 1.
DR PROSITE; PS50851; CHEW; 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}; Kinase {ECO:0000313|EMBL:ACI20983.1};
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169};
KW Reference proteome {ECO:0000313|Proteomes:UP000000718};
KW Transferase {ECO:0000313|EMBL:ACI20983.1}.
FT DOMAIN 1..111
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 273..473
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 475..606
FT /note="CheW-like"
FT /evidence="ECO:0000259|PROSITE:PS50851"
FT DOMAIN 623..739
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT COILED 97..124
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 47
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
FT MOD_RES 672
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 742 AA; 84748 MW; 0800DD391FB2810C CRC64;
MINKSELIKY FLLEADDCLN VLVEGTEELE TKGYNKSTIE SLFRATHTLK GSASIVKFNK
ITTLSHKLED LFEALLNGEI NYDNSLIYHI RNVINLIVAL VNEVHEAGEE KSEIEKEVIE
LIDNILNKKE IPAVQQKSVI FDALPVTDNV RVELKVIENI FASLSEVLVQ KNTITDKEKE
LFHIVEEISN SGKKLLKEIT DFSDMYWLST YERGQKVIDS FFVDFSDLEF DRYDEYHIFL
RKIQEITNDI TEGINSLFIF SENLSSHFKS LGREINYLKD SLIEIRMIPI GKLLHRLSEA
IKENAKDIGK TVEIDIKGAE IKIDKPVFDS LYEPIIHILR NAIQHGIESF EERIKKGKEQ
TGHIKIDVKK EGKYIVIAIK DDGRGIDIDK VKEIAVQKGL ISSEYTSFIS EEEILSYIFV
PGFSTSDEID FQSGRGMGLN IVKTAISKLK GTIEVFSELD KETTFIIKIP QSLTISNLLI
FSSHNLDFAI PINYIEEILT LEDFPHALEE RSINHKNRII PVKIFSEIFF SLNGKTLQKG
YIIVFNFSGI RKGLIVDEIL GHEEATVHNF GKFLEGLIQY LGYFISGKGS PRYVIDPLKL
FEEEFIFTGL SDKITESFIY SGSVLVVDDS ISVRKTLQSV LEAKKLRVYT AKDGVEALNL
LERNKVDMVV TDLEMPVMHG YELISRLRKD ARFKNLPIIV LTSRGTKKHE EKAFELGADG
YIVKPFDEKT IEEEILDRLK LL
//
