ID B5YGI9_THEYD Unreviewed; 568 AA.
AC B5YGI9;
DT 25-NOV-2008, integrated into UniProtKB/TrEMBL.
DT 25-NOV-2008, sequence version 1.
DT 27-MAR-2024, entry version 86.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=THEYE_A1592 {ECO:0000313|EMBL:ACI22159.1},
GN THEYE_A1644 {ECO:0000313|EMBL:ACI20975.1};
OS Thermodesulfovibrio yellowstonii (strain ATCC 51303 / DSM 11347 / YP87).
OC Bacteria; Nitrospirota; Thermodesulfovibrionia; Thermodesulfovibrionales;
OC Thermodesulfovibrionaceae; Thermodesulfovibrio.
OX NCBI_TaxID=289376 {ECO:0000313|EMBL:ACI22159.1, 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:ACI22159.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=DSM 11347 {ECO:0000313|EMBL:ACI22159.1};
RA Dodson R.J., Durkin A.S., Wu M., Eisen J., Sutton G.;
RL Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:ACI22159.1, ECO:0000313|Proteomes:UP000000718}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51303 / DSM 11347 / YP87
RC {ECO:0000313|Proteomes:UP000000718}, and DSM 11347
RC {ECO:0000313|EMBL:ACI22159.1};
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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; CP001147; ACI20975.1; -; Genomic_DNA.
DR EMBL; CP001147; ACI22159.1; -; Genomic_DNA.
DR RefSeq; WP_012545703.1; NC_011296.1.
DR RefSeq; YP_002249387.1; NC_011296.1.
DR RefSeq; YP_002249437.1; NC_011296.1.
DR AlphaFoldDB; B5YGI9; -.
DR STRING; 289376.THEYE_A1592; -.
DR EnsemblBacteria; ACI20975; ACI20975; THEYE_A1644.
DR EnsemblBacteria; ACI22159; ACI22159; THEYE_A1592.
DR KEGG; tye:THEYE_A1592; -.
DR KEGG; tye:THEYE_A1644; -.
DR PATRIC; fig|289376.4.peg.1549; -.
DR eggNOG; COG3275; Bacteria.
DR HOGENOM; CLU_020473_3_3_0; -.
DR OrthoDB; 9776552at2; -.
DR Proteomes; UP000000718; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0071555; P:cell wall organization; IEA:InterPro.
DR Gene3D; 1.10.1760.20; -; 1.
DR Gene3D; 3.30.450.40; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR InterPro; IPR029016; GAF-like_dom_sf.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR005467; His_kinase_dom.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR010559; Sig_transdc_His_kin_internal.
DR InterPro; IPR011620; Sig_transdc_His_kinase_LytS_TM.
DR PANTHER; PTHR34220; SENSOR HISTIDINE KINASE YPDA; 1.
DR PANTHER; PTHR34220:SF7; SENSOR HISTIDINE KINASE YPDA; 1.
DR Pfam; PF07694; 5TM-5TMR_LYT; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF06580; His_kinase; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF55781; GAF domain-like; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 4: Predicted;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000000718};
KW Transferase {ECO:0000313|EMBL:ACI22159.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..24
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 44..62
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 74..94
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 101..125
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 137..157
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 169..189
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 338..557
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 568 AA; 62335 MW; 02A5848C69FFCAD6 CRC64;
MDILELTLIL SQRLGIIATV AFIVSRMPVF GRVLSRKPTI KDKFILTFVC GGLGILGTFG
AVEIHGALAN SRVVGVMVGG LLGGPVVGAG AGLIAGIHRY FIGGFTAFSC GLAAVVEGFL
GGVVYRYWKK GLIPWHVAWL AGFVGEIVQM LIILTFSKPF SEALELVKII ALPMITVNSI
GVGIFMLIIK SAVEHQERVA ANQARATLNI TNLILPHLRQ GLNEYSANKI ATIIMDSLGV
VAVAITDKKK ILAHVGIGSD HHHAGTPLLT KATLNAISLG EIQIANKKEE IGCRNSKCKL
SSAVIVPLKR RDEVIGTLKL YHDRENSITT VNLEVARGLA HIFSTQLEIV ELETLARLKT
EAELKSLQAQ IHPHFIFNAL NTIISLIRID SLKAKDLLLN LATFLRYSLK KEKEIPLREE
LSYVESYLAI EQARYRDKLT VNYYIEPTVD LNVTLPPFTI QPLVENAIKH GLKPKLEGGE
ILINILDDED STVISVEDNG IGINTHPNRM PDKKDSGLGL YLVNERLKKF YGEESMLHIE
SYPNLGTKVT FKIPKKSILK DVVFSHSS
//
