ID L0I9Q9_HALRX Unreviewed; 718 AA.
AC L0I9Q9;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=Halru_0043 {ECO:0000313|EMBL:AGB14697.1};
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:AGB14697.1, 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; AGB14697.1; -; Genomic_DNA.
DR AlphaFoldDB; L0I9Q9; -.
DR STRING; 797302.Halru_0043; -.
DR KEGG; hru:Halru_0043; -.
DR eggNOG; arCOG02333; Archaea.
DR eggNOG; arCOG02334; Archaea.
DR eggNOG; arCOG06918; Archaea.
DR HOGENOM; CLU_020780_0_0_2; -.
DR OrthoDB; 8127at2157; -.
DR Proteomes; UP000010846; Chromosome.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.450.40; -; 2.
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; IPR003018; GAF.
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; IPR003661; HisK_dim/P.
DR InterPro; IPR036097; HisK_dim/P_sf.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013656; PAS_4.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR NCBIfam; TIGR00229; sensory_box; 1.
DR PANTHER; PTHR43711:SF1; HISTIDINE KINASE 1; 1.
DR PANTHER; PTHR43711; TWO-COMPONENT HISTIDINE KINASE; 1.
DR Pfam; PF13185; GAF_2; 2.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF08448; PAS_4; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00065; GAF; 2.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF55781; GAF domain-like; 2.
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; PS50112; PAS; 1.
PE 4: Predicted;
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000010846}.
FT DOMAIN 405..457
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 521..718
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT REGION 1..68
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 718 AA; 78148 MW; A57124E6CEB17E2D CRC64;
MTGNIGPGDD ITRPEPDEGT DGATTDGGEP VTPPEHEATD GSPSDTDAEA TADESEGSTA
LPTEDDRSKI ARLHEMATEI VACREEAELF DLAVDTAKGV LDFDTTAFLI HEEREDGEWL
VHRAGTSTFP LDYETEFRPT GLAGETFRTG ETFHVDDAES HPVAQPASER FKSAISVPIG
GSYGVFQAIS TEYAGFDDRD VELAEILASH VAETLRRIRV EERLRERREL VTRLHEGTLG
IAAADSEAEL FEHAVDTAER ILDIDVCYLG IVEDGEFVPK GRPSWPIREE IGALPLEYGL
MGETYRTGES YRIGDAATDD RTHDEVGDFR ACISVPIDEF GVLQAVSTTP DTYDESDLEL
VELLAAHVAE SLARLRAEQD VVEEHDRLSA LFANVPDPAI RFEFVDDEPV VRDVNDAFEG
VFGYDRATVM GESVDDYIVP PGFEDEGNAL NEALLAGETV QHVTKRETAE GLRDVRIDVV
PLQLGEHSPE GFAIYTDITV QKRRERELRE QNERLDRFAS VLSHDLRNPL SVAAGYIEQA
RETDDLSLLE EAERGIDRSF DIVEDVLTLA REGGEVTETA PVDLPAVASD AWANVDTGAA
TLDLSTTATV EADRSRLRQL LENLVRNCVE HGTPDGDGQD LTITVADTPD GFAVVDDGCG
FGDEVDLDRL FDSGYTTSHD GTGLGLSIVS EIAAGHGWSV SAEESEAGGA RFDFQLGA
//
