ID B8CW30_HALOH Unreviewed; 652 AA.
AC B8CW30;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 90.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=Hore_07420 {ECO:0000313|EMBL:ACL69499.1};
OS Halothermothrix orenii (strain H 168 / OCM 544 / DSM 9562).
OC Bacteria; Bacillota; Clostridia; Halanaerobiales; Halothermotrichaceae;
OC Halothermothrix.
OX NCBI_TaxID=373903 {ECO:0000313|EMBL:ACL69499.1, ECO:0000313|Proteomes:UP000000719};
RN [1] {ECO:0000313|EMBL:ACL69499.1, ECO:0000313|Proteomes:UP000000719}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H 168 / OCM 544 / DSM 9562 {ECO:0000313|Proteomes:UP000000719};
RX PubMed=19145256; DOI=10.1371/journal.pone.0004192;
RA Mavromatis K., Ivanova N., Anderson I., Lykidis A., Hooper S.D., Sun H.,
RA Kunin V., Lapidus A., Hugenholtz P., Patel B., Kyrpides N.C.;
RT "Genome analysis of the anaerobic thermohalophilic bacterium
RT Halothermothrix orenii.";
RL PLoS ONE 4:E4192-E4192(2009).
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; CP001098; ACL69499.1; -; Genomic_DNA.
DR RefSeq; WP_012635687.1; NC_011899.1.
DR AlphaFoldDB; B8CW30; -.
DR STRING; 373903.Hore_07420; -.
DR KEGG; hor:Hore_07420; -.
DR eggNOG; COG5002; Bacteria.
DR HOGENOM; CLU_000445_89_20_9; -.
DR OrthoDB; 9813394at2; -.
DR Proteomes; UP000000719; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 1.
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; IPR033425; MASE3.
DR InterPro; IPR001610; PAC.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR NCBIfam; TIGR00229; sensory_box; 1.
DR PANTHER; PTHR43547:SF2; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE C; 1.
DR PANTHER; PTHR43547; TWO-COMPONENT HISTIDINE KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF17159; MASE3; 1.
DR Pfam; PF13426; PAS_9; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00086; PAC; 1.
DR SMART; SM00091; PAS; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 1.
DR PROSITE; PS50112; PAS; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:ACL69499.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000000719};
KW Transferase {ECO:0000313|EMBL:ACL69499.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {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 37..54
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 61..78
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 98..119
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 131..151
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 163..182
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 194..212
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 263..334
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 339..391
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 401..622
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 652 AA; 75461 MW; 62739DE5AD6E5679 CRC64;
MIKSKFYVGD LPFILLFIIL FLASFYNYIF FHSVVELLTI ITASNVFIIA FATTEIGENN
YFKFLGLAYG FVAFFDLLHM TSCQGLGIFP EYDINLCIQF WIVARLIESI SLLVSFAFVN
SNTNNFKKYR FFIRYIFISV LFLVLLFYEL FPLCYHNNSL TNFKVITEYA ISFILLLSII
VLKKSSSWFS SSVYRLLFLS LVFTFMSELL LASYLNPYGF RNILGHLFKL VSFYLIYKSV
SVTSLKKPFE TLFYKLNQAN KKLKNEKNKI LDITEAIFIF IDKEGKITLI NKKGCEVLGY
QEEEIIGKEW VTNFVYKDDR ERVRKTLENI VTCGCNNGNN FEHQVVTRDN TRRTILWKNT
VLKDERGQIR GVLSSGLDIT DKKLLEEELE YNKLRTEFFA NLSHEFKTPL NVIFSALHLI
EWSLDKNPLK KDKIKSYLKT ITHNSYRLLR LITNLLDITK IDANSYQLNI CNCDIVKIVK
SAVNSVKGHI NNKTRKIVFN TNVNEKIIAC DPFDIERILY NLLSNAIKFT GEGDKITVEI
KDRGQSLNII VKDTGIGIPE EMQDYIFKRF RQVDKSFRRN NEGSGLGLSL TKSLVELHGG
SISIESKPGK GSTFIIKLPV FQVSNNLCEN TRKKSKELID RINLEFSDIY EL
//
