ID L9W192_9EURY Unreviewed; 1155 AA.
AC L9W192;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=C496_06917 {ECO:0000313|EMBL:ELY43046.1};
OS Natronorubrum tibetense GA33.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC Natrialbaceae; Natronorubrum.
OX NCBI_TaxID=1114856 {ECO:0000313|EMBL:ELY43046.1, ECO:0000313|Proteomes:UP000011599};
RN [1] {ECO:0000313|EMBL:ELY43046.1, ECO:0000313|Proteomes:UP000011599}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GA33 {ECO:0000313|EMBL:ELY43046.1,
RC ECO:0000313|Proteomes:UP000011599};
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:ELY43046.1}.
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DR EMBL; AOHW01000022; ELY43046.1; -; Genomic_DNA.
DR RefSeq; WP_006089203.1; NZ_KB913017.1.
DR AlphaFoldDB; L9W192; -.
DR STRING; 1114856.GCA_000383975_00904; -.
DR PATRIC; fig|1114856.3.peg.1448; -.
DR eggNOG; arCOG02329; Archaea.
DR eggNOG; arCOG02334; Archaea.
DR eggNOG; arCOG02352; Archaea.
DR eggNOG; arCOG02358; Archaea.
DR eggNOG; arCOG06712; Archaea.
DR OrthoDB; 342253at2157; -.
DR Proteomes; UP000011599; 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; 4.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.450.40; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 6.
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; IPR013656; PAS_4.
DR InterPro; IPR013767; PAS_fold.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR NCBIfam; TIGR00229; sensory_box; 5.
DR PANTHER; PTHR43304:SF1; PAC DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR43304; PHYTOCHROME-LIKE PROTEIN CPH1; 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; PF08448; PAS_4; 4.
DR Pfam; PF13426; PAS_9; 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; 4.
DR SMART; SM00091; PAS; 6.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 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); 6.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 2.
DR PROSITE; PS50112; PAS; 4.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:ELY43046.1};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Transferase {ECO:0000313|EMBL:ELY43046.1}.
FT DOMAIN 28..75
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 153..198
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 520..572
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 577..647
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 690..734
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 760..811
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 942..1155
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT COILED 553..587
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1155 AA; 129513 MW; D89B9214E216E1A1 CRC64;
MSDRTESSGT RFWTAGDDRA TMACCQTLVD TVEDGVFRLD ADDRFLAIDD ALLETTGYAR
DAVLGEHVSL LFPRSDAETL EGAVRNDSDG VTSLELLIRT SDGTTIPCDC RVNGVRVDDR
FRGSIVTVRE LEASATETDS VSERTSSPSP SATFEAATTV LEEADVGVFV LDDEFDVAWI
NEATERYFGL DREAVVGRDK HRLIDESIAG RLADPDAFTE AVTATYADNS SVERFECHVT
AGDEREERWL EHRSKPIDTG RYAGGRIELY YDVTAQHDRV SQLRRLNEAV REWLAEDSRE
RIAELASRHV REILDLEING VFCYDDETRT LHPAGWSDPA EALLGDIPSF APGEGIAWRV
FETGEPVIYD DVTTDSDVYN PDTPIRSEIC LPIGDHGILI IGSEQPTEFD DGDLSLAKIV
ASSLEVIFDR IRHERHLERE RTQTEKLLQT APIGISVEDA DGETVLANQR VQKRVDSMAE
AALGETEMVR EWAVRDASGE PIEPGSNPSA RVRETGEPVF DEELVVEGPT GERRWLSVNA
VPVFDADGGL ERVISSAEDI TALKERKRRL ERRKSELETE LSEIFGRISD GFYALDEEFR
FTHVNETAER LLDRSRRELL GTVLWDIYPE VAGSELKERY GEALTTQEPV SFEQYVEPMG
IWAQVQVYPS ETGLSIYFRD VTEEKTRERE LITYETIFET VEDGIYVIDG EGRFTAANEA
YAAMTGYDRD ELIGTHASIV VDESVMDLAR EIAAEESDVP TVEAELETKA GGCVPIEATV
TALSVTGSDR ERVGVVRDVT KRKERQRKLE ASEQRYRTLA ENFPNGTVGL YDENLRYTAA
GGQLLDELGI DRDDVIGQTI ADRYPETILE TVEPHFRAAL EGEERSFDLR YHGRELLAHT
LPVQTDGTVR RGMLVVQDIT ERKAYERKLE ESNERLEQFA YAASHDLQEP LRMVTSYLQL
IESRYADELD DDAEEFIAFA VDGADRMREM IDGLLEYSRV ETRGDPFELV DLDDVLEDVR
RDLELQVDES GAVIETPDTL PAICGDRSQL RQVFQNLLAN AIEYSDDEPR VTVSAERDGQ
RWTVSVSDEG IGIDPDDADR VFDIFQRLHS HEEHDGTGIG LALCQRIVER HGGEIWVDSE
PGKGSTFSMT LPVAE
//
