ID L9YKJ7_9EURY Unreviewed; 1147 AA.
AC L9YKJ7;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-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 ORFNames=C487_15940 {ECO:0000313|EMBL:ELY74196.1};
OS Natrinema pallidum DSM 3751.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC Natrialbaceae; Natrinema.
OX NCBI_TaxID=1227495 {ECO:0000313|EMBL:ELY74196.1, ECO:0000313|Proteomes:UP000011618};
RN [1] {ECO:0000313|EMBL:ELY74196.1, ECO:0000313|Proteomes:UP000011618}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 3751 {ECO:0000313|EMBL:ELY74196.1,
RC ECO:0000313|Proteomes:UP000011618};
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:ELY74196.1}.
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DR EMBL; AOII01000089; ELY74196.1; -; Genomic_DNA.
DR RefSeq; WP_006186732.1; NZ_AOII01000089.1.
DR AlphaFoldDB; L9YKJ7; -.
DR PATRIC; fig|1227495.3.peg.3196; -.
DR eggNOG; arCOG02334; Archaea.
DR eggNOG; arCOG02348; Archaea.
DR eggNOG; arCOG02352; Archaea.
DR eggNOG; arCOG06712; Archaea.
DR eggNOG; arCOG06796; Archaea.
DR eggNOG; arCOG07605; Archaea.
DR OrthoDB; 106630at2157; -.
DR Proteomes; UP000011618; 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; 4.
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; 3.
DR Pfam; PF08448; PAS_4; 3.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00086; PAC; 5.
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};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553}.
FT DOMAIN 21..66
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 145..190
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 509..561
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 566..636
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 679..723
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 748..799
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 930..1143
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT REGION 107..145
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 549..576
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1147 AA; 126255 MW; DB5CB7E24B66D0B4 CRC64;
MTERAGPAVS APWDDSDKSA AQQWYRTVVE TVAGGVFQLD ADGRIVGVDD TLLELTGYTR
DALSGEHVTT LLGDSGSGAL EAGSATGVTE REGTIRTADG TAIPCELRLG SVPGSDGRQG
SIGVVTERGH GPRAASDAES TRPQPFESVT TVLEEADVGV FVLDEAFDVA WINQATERYF
GLDAADVVGR DKATVIDDTI RDRVGDPDAF ADVLESTYDG NGDAERFECR ITPGDGREER
WLEHRSKPIT AGPYAGGRVE LYYDVTEQHR RAAQLRQLHE AVREWLGTGT REAVAEQACQ
YLSEVLDLDL NGVFLSDAAG TGLEPVAWSE PEAAPFDEHP AFAAGAEIAR RVFDSGEPVI
DDVPVDSDDP AVPIRSAIGL PIGDHGVVVI GSETADAFDE GDRSLVKVAA SSLEATVDRI
SHEQSLERER SQTETLLRTT PVAISVEDAD GQTVLANRHA QAALGLADRR PLGETELLAE
GAVVDADGDP VGPDRGPSAR VRETGEPVFD EELMIEGPTG DPSWFSVTAV PVFGTDGDLE
RVVSAGEDIT ALKKHERRLE RRKHELETEL SEILGRVSDA FYALDDDWRF THVNDRAGEL
LGYDPAALVG ENIWETFPSG ARSDLRERYR TAMETQQPVA WERYSNSLDI WMEIRAYPSE
TGLSVYFQDI TDRKRRERHL EQYERIIETI EDGIYVLDED DRFTMVNEAY VSLTGYDRDE
LLGSHASLVA DEQVMSLARQ IAAESDDSTI EASVETKSGI QVPVEATVTS IATADTGPER
IGVVRDITER QERQQRLEAS EQRYRTLAEN FPNGIVALFD DELRYTAIGG QLLGEVGIDR
EAAIGKTIHE RYSDELLAEV EPHFRAALDG DERTFEVTYQ SRDLRATTLP VRTGDEVTAG
MLVIQDITER TAYRRKLEES NERLEQFAYA ASHDLQEPLR MVTSYLQLIE GRYADDLDAD
GREFIDYAVD GAERMREMIN GLLQYSRVET KGEPLEPVAL DAVLADVRED LQFCIDERDA
EITADPLPRV AGDASQLRQV LQNLLSNAIE YSGDEPPRVH VSAERTGWKW EISVRDEGIG
IDAENQDRIF QVFQRLHSHE EHAGTGIGLA LCHRIIERHG GEMWVDSTPG EGSTFSFTLP
AAETATN
//