ID L0IC66_HALRX Unreviewed; 650 AA.
AC L0IC66;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 24-JAN-2024, entry version 48.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=Halru_2589 {ECO:0000313|EMBL:AGB17170.1};
OS Halovivax ruber (strain DSM 18193 / JCM 13892 / XH-70).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC Natrialbaceae; Halovivax.
OX NCBI_TaxID=797302 {ECO:0000313|EMBL:AGB17170.1, ECO:0000313|Proteomes:UP000010846};
RN [1] {ECO:0000313|Proteomes:UP000010846}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18193 / JCM 13892 / XH-70
RC {ECO:0000313|Proteomes:UP000010846};
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Mikhailova N., Davenport K., Detter J.C., Han C., Tapia R.,
RA Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Sproer C.,
RA Anderson I., Woyke T.;
RT "Complete sequence of Halovivax ruber XH-70.";
RL Submitted (SEP-2011) 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};
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DR EMBL; CP003050; AGB17170.1; -; Genomic_DNA.
DR AlphaFoldDB; L0IC66; -.
DR STRING; 797302.Halru_2589; -.
DR KEGG; hru:Halru_2589; -.
DR eggNOG; arCOG02330; Archaea.
DR eggNOG; arCOG02331; Archaea.
DR eggNOG; arCOG02389; Archaea.
DR HOGENOM; CLU_000445_114_58_2; -.
DR OMA; TEITHEP; -.
DR OrthoDB; 8127at2157; -.
DR Proteomes; UP000010846; Chromosome.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 2.
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; 2.
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; IPR001610; PAC.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013656; PAS_4.
DR InterPro; IPR013767; PAS_fold.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR NCBIfam; TIGR00229; sensory_box; 2.
DR PANTHER; PTHR43711:SF1; HISTIDINE KINASE 1; 1.
DR PANTHER; PTHR43711; TWO-COMPONENT HISTIDINE KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00989; PAS; 1.
DR Pfam; PF08448; PAS_4; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00086; PAC; 2.
DR SMART; SM00091; PAS; 2.
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); 2.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 2.
DR PROSITE; PS50112; PAS; 2.
PE 4: Predicted;
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000010846}.
FT DOMAIN 143..187
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 217..268
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 265..340
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 346..398
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 409..638
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 650 AA; 70675 MW; BEF114DF9894F800 CRC64;
MRERIRVCWV GPTPEGQTQA IVEQAIHPIT VTNRSVEWLH DGETTGATVE HDADTPIADC
FVLDLDAEGR DAGIRAVPGQ TPVAVVLGHD EDTSHPLEAG AADVFRRDTV QQEPALVARR
LRSVVDASAS RPPLTRVSAD STRLGRYQTV VERAADPMYV LDSSGRCVLA NDALARFSGY
ERTDLVGTHA STFIGSAEFE RAGELLADLA SSDESAGRFE FTLETADGDE RVGEATIVPV
TTDDRVLGSV GVVRDISERT RRTRELARFR TIVETAPVGL FSLDETGTIS WANDEFVAPF
AEPADEIVGE PFQALVERGY FSPEEIDAYA ERVRTLLSDD TDVTEITHEP RLHTPDGETR
TYRATLTTLP LDDGEFTGTV NAFREITDER RYQRELERQN DRLEQFASLV SHDLRNPLNV
AQGHVDLLEE AVDHDSVSEV SWAIERMATL IDDLLTLTRQ GETVGDPERV DLAAVVDDAW
AVVEGPVTLR RDVAGTVAAD RSRLVELFTN LFRNVVDHGM ADENRAPIDH DAHANEAAVH
DPEATDNEQH PTNEPESARE ITVGWLDDEA SASAAPTGFF VDDDGPGLPD ADVFEAGVTT
DPDGTGIGLA IVAEIAEAHG WTATAGESPS GGARFAFRGV DSARAERSAR
//