ID L9Y523_9EURY Unreviewed; 798 AA.
AC L9Y523;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 24-JAN-2024, entry version 53.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=C489_08180 {ECO:0000313|EMBL:ELY67968.1};
OS Natrinema versiforme JCM 10478.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC Natrialbaceae; Natrinema.
OX NCBI_TaxID=1227496 {ECO:0000313|EMBL:ELY67968.1, ECO:0000313|Proteomes:UP000011632};
RN [1] {ECO:0000313|EMBL:ELY67968.1, ECO:0000313|Proteomes:UP000011632}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 10478 {ECO:0000313|EMBL:ELY67968.1,
RC ECO:0000313|Proteomes:UP000011632};
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: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00169}.
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:ELY67968.1}.
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DR EMBL; AOID01000026; ELY67968.1; -; Genomic_DNA.
DR RefSeq; WP_006430707.1; NZ_AOID01000026.1.
DR AlphaFoldDB; L9Y523; -.
DR STRING; 1227496.C489_08180; -.
DR PATRIC; fig|1227496.3.peg.1654; -.
DR OrthoDB; 8127at2157; -.
DR Proteomes; UP000011632; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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; 3.30.450.40; -; 1.
DR Gene3D; 3.40.50.2300; -; 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; IPR011006; CheY-like_superfamily.
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; IPR001610; PAC.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013767; PAS_fold.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR NCBIfam; TIGR00229; sensory_box; 2.
DR PANTHER; PTHR43711:SF1; HISTIDINE KINASE 1; 1.
DR PANTHER; PTHR43711; TWO-COMPONENT HISTIDINE KINASE; 1.
DR Pfam; PF13185; GAF_2; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00989; PAS; 1.
DR Pfam; PF13188; PAS_8; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00065; GAF; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00086; PAC; 1.
DR SMART; SM00091; PAS; 2.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF52172; CheY-like; 1.
DR SUPFAM; SSF55781; GAF domain-like; 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; 1.
DR PROSITE; PS50112; PAS; 2.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 14..132
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 162..223
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 281..351
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 356..408
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 604..798
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT COILED 561..601
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 798 AA; 86727 MW; 4A35C24D987C578D CRC64;
MATFGPTRFE RPTTVVYADP APDDRRRVAD GLESIADGLT VVPVATLAEL RDAVADASGR
TCVVTEYQFA ETDALSLYDR IRADGIGDVP IVLYTADGDE RLASDAVTAG FSGYVPKGLE
DSLERLVAQL RAIVNQPVAP NGGQTAGSRL RPDTERGSLR AERDQFAALF EHSPDAVIVT
RRDDPNRIID VNPAFEAIFG HDRGDIAGGA LDDILVPNDA EPVSMADTVG LGTIVTEPVE
RLTVDGRRDF FLRGFAAEVA GEVYEYAIYT DISDQKRRER ELERYRTLVD AVGDSMYVLD
ETGRIEMVND AMADALGTTR ADLVGQPPSR YMPAEDVERA TELLLDILAD DDRTWGTFEM
EFQPVDGEPF VVENNVAPIV AEDGSLAGSV GAIRDISDRI ERERQIRKLH EGTRRLMAAE
RTAEVARVAS EIARDALSLE INSVHLYEER TASRTVSADG PPVAADPSLE SRRERGILVP
AAATDRTEAL FGSVPAIGPG DGISWDAFEA GETIVHGDVR RAENVRNPET AIRSEAHIPL
GTMGIFIVSS TTPNDFDPET ITLARILAAN VEAALEQARR EAELAERTAE LERQNDRLEA
FASTVSHDLR NPLTLAAGHL ENLEAHVDEE GERYRKEIDW ALERMDDLIE NVLTLARSGQ
RLTATEPVAL DEVVDQARRT VDPDLDLVRE EPLPTVEADA DRLLVCFENV FRNARDHVGD
DVTITIETTD DGFAIADDGP GVPPGERGDI LESGYSTSPD GTGFGLAIVS EVVEAHGWSV
TVGESDAGGL RLAVSLEE
//
