ID L9W3D7_9EURY Unreviewed; 965 AA.
AC L9W3D7;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=C496_05952 {ECO:0000313|EMBL:ELY42853.1};
OS Natronorubrum tibetense GA33.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC Natrialbaceae; Natronorubrum.
OX NCBI_TaxID=1114856 {ECO:0000313|EMBL:ELY42853.1, ECO:0000313|Proteomes:UP000011599};
RN [1] {ECO:0000313|EMBL:ELY42853.1, ECO:0000313|Proteomes:UP000011599}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GA33 {ECO:0000313|EMBL:ELY42853.1,
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:ELY42853.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AOHW01000022; ELY42853.1; -; Genomic_DNA.
DR RefSeq; WP_006089010.1; NZ_KB913017.1.
DR AlphaFoldDB; L9W3D7; -.
DR STRING; 1114856.GCA_000383975_01097; -.
DR PATRIC; fig|1114856.3.peg.1240; -.
DR eggNOG; arCOG02358; Archaea.
DR eggNOG; arCOG02360; Archaea.
DR eggNOG; arCOG02369; 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 CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 2.
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; 3.
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; IPR000700; PAS-assoc_C.
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; 2.
DR PANTHER; PTHR43304:SF1; PAC DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR43304; PHYTOCHROME-LIKE PROTEIN CPH1; 1.
DR Pfam; PF01590; GAF; 2.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF08448; PAS_4; 3.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00065; GAF; 2.
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; 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); 3.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 2.
DR PROSITE; PS50112; PAS; 2.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:ELY42853.1};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Transferase {ECO:0000313|EMBL:ELY42853.1}.
FT DOMAIN 183..227
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 525..587
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 595..665
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 667..718
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 736..949
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT REGION 945..965
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 706..736
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 947..965
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 965 AA; 108546 MW; 4621BC776EF722E2 CRC64;
MATSDPPTGQ LRSRIRQQEV IAELGKRALE SSDFDELLVD AGAAVRDALE VDYCGMFEVV
RDRDAVVLRQ GVGWRDGAVG SETVSTGANV PAGRTLETDD VVVAADVEAS DRLSTSTLLA
SHDVTSAVSV GIDADADGDE PWGILAVYTT ERREFADHEL SFVRNVAAVL ASAIENLRVR
RGLETELETT IGRFTDAFIG LDADWRVTYV NDRARELTER EGDELIGVTL WEAFPATVDS
TFERECRRAM VTQEPTTFEE YYPPLETWLE VNASPSETGL SISFRDVSDR DATQRELQAN
NRTLQRLYAI TADRELSFDE KTRELLDLGR ERLGLEVGFM ADIDERNDRF EVVHSSGDDE
RLQPGSVTQL SDTYCRRTIE EDELLVLTNA PVEGWGEDHA YEKWEFDSYL GGQLRVDGEP
YGTLCFADDA PRSTSFTPAE RSFVELLTQW LSYELERQHH QRELEESERR YRTLVEQFPN
GIVALFDEEL RYTLGGGRIL EEIDISIDDV VGQTIYDRYD GETLETFESN FQAALSGERT
SFEYGIHGRE WLAHTVPVED DRGEVFAGMI MVQDVTERNE QERQLREREA RLERFKAYTD
DILDAVDDVF YVVGEDGSFQ RWNETLCAVT GYSDAEVDSM TPLDFFDGED QQRIGNAIQE
VFETGQTRVE ADVVTKDGQT IPYEFIASAL ENPDGSPVLT GIGRDISDRR ADQRRLEELV
DELEESNERL EQFAYAASHD LQEPLRMVAS YLTLVDQRYA DELDDDGQEF VAYAVDGARR
MQEMIDGLLA YSRVDTQGDP FEVVDCEAVV DDVLTDLEVR IEETDADITV ESLPEVYGDP
GQLRQVFQNL LDNAITYSGE EAPRISVFAE KDGQEWRLSV RDRGIGIDPV NTERIFQVFD
RLHSVGEYAG TGIGLALCQR IVERHDGDIR VTSTPGEGAT FTVTLPEPPD SEATTEPTGT
FTTNE
//
