ID L9W4M4_9EURY Unreviewed; 688 AA.
AC L9W4M4;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=C495_10944 {ECO:0000313|EMBL:ELY44414.1};
OS Natronorubrum sulfidifaciens JCM 14089.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC Natrialbaceae; Natronorubrum.
OX NCBI_TaxID=1230460 {ECO:0000313|EMBL:ELY44414.1, ECO:0000313|Proteomes:UP000011661};
RN [1] {ECO:0000313|EMBL:ELY44414.1, ECO:0000313|Proteomes:UP000011661}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 14089 {ECO:0000313|EMBL:ELY44414.1,
RC ECO:0000313|Proteomes:UP000011661};
RX PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT strategies for static and dynamic osmo-response.";
RL PLoS Genet. 10:E1004784-E1004784(2014).
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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ELY44414.1}.
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DR EMBL; AOHX01000039; ELY44414.1; -; Genomic_DNA.
DR AlphaFoldDB; L9W4M4; -.
DR STRING; 1230460.C495_10944; -.
DR PATRIC; fig|1230460.4.peg.2222; -.
DR eggNOG; arCOG02358; Archaea.
DR eggNOG; arCOG06712; Archaea.
DR Proteomes; UP000011661; Unassembled WGS sequence.
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; 3.
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; 3.
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; IPR013767; PAS_fold.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR NCBIfam; TIGR00229; sensory_box; 3.
DR PANTHER; PTHR43304:SF1; PAC DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR43304; PHYTOCHROME-LIKE PROTEIN CPH1; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00989; PAS; 2.
DR Pfam; PF08448; PAS_4; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00091; PAS; 3.
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); 3.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50112; PAS; 3.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:ELY44414.1};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000011661};
KW Transferase {ECO:0000313|EMBL:ELY44414.1}.
FT DOMAIN 62..111
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 193..263
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 306..350
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 465..678
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 401..430
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 688 AA; 76503 MW; 4B9F9B34EBAFD642 CRC64;
MWTHSPEAVA NGGDQRSHDR IDVGLMPPSG VVRTMSDRTE SSGAECWSAG DERTARRCCQ
ALVETVDGGV FRLDVDDRFV AVDDTFLELT GYSCSELLGE RLATVLPSLE PAQFEEAVRG
HRPDGTANVV PLERTLRTAA GDTVRCDLRL TRLRADGRTA EFVGIVRPVE QSEPSAVPDQ
PKSTAVESTA MALETTVSEI LGRVSDAFYA LDESWRFTHV NERAEELLGH SSDDLVGERI
WEVFPGGKRS ELADRYQEAM ATQESISWER YSQSLELWME IQVYPSETGL SVYFRDITAR
KRRERQLERY ERIIETIDDG IYVLDEDDRF VAVNDAYTEL TGYDRDELLG APASLISSEP
ALEQTKQLAT DDNEPSTLET TLETKDGTPV PIEATVTTIS TAEHTAPDAA VGTSSDTPRD
GERTRADAAD GSNKWAGIVR DVTEREAYQR ELEASNERLE QFAYAASHDL QEPLRMVSSY
LRLLERRYDD ALDDDGLEFL EYAVDGAERM SAMIDGLLEY SRVETRAGEL EPVDLEAVFE
DAREDLALRI DEQEADVTVS SLPCVRGDGN QLRQVFQNLL SNAFEYSGDE PPRVHVSAEQ
SGSEWIVSVR DEGIGIDPDE TTRIFEVFQR LHTHDEHPGT GIGLALCRRI VERHGGDIWV
ETEPGAGATF SMTLPAVDDP ESCEPCSH
//
