ID M0AN68_9EURY Unreviewed; 782 AA.
AC M0AN68;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 24-JAN-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=C482_11158 {ECO:0000313|EMBL:ELY98833.1};
OS Natrialba chahannaoensis JCM 10990.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC Natrialbaceae; Natrialba.
OX NCBI_TaxID=1227492 {ECO:0000313|EMBL:ELY98833.1, ECO:0000313|Proteomes:UP000011693};
RN [1] {ECO:0000313|EMBL:ELY98833.1, ECO:0000313|Proteomes:UP000011693}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 10990 {ECO:0000313|EMBL:ELY98833.1,
RC ECO:0000313|Proteomes:UP000011693};
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:ELY98833.1}.
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DR EMBL; AOIN01000060; ELY98833.1; -; Genomic_DNA.
DR RefSeq; WP_006167674.1; NZ_AOIN01000060.1.
DR AlphaFoldDB; M0AN68; -.
DR STRING; 1227492.C482_11158; -.
DR PATRIC; fig|1227492.4.peg.2200; -.
DR OrthoDB; 8127at2157; -.
DR Proteomes; UP000011693; 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; 1.
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; 1.
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; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013767; PAS_fold.
DR NCBIfam; TIGR00229; sensory_box; 1.
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 SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00091; PAS; 1.
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); 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50112; PAS; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:ELY98833.1};
KW Transferase {ECO:0000313|EMBL:ELY98833.1}.
FT DOMAIN 390..460
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 560..781
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT REGION 49..73
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 134..211
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 488..521
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 142..160
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 196..211
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 490..521
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 782 AA; 84502 MW; D7D21179340FF363 CRC64;
MSRARVLCIS RDSSTRAALT LAFTDAPVSV SIVPDPDLAV DQLEFSRNQD FPEEGDWSDS
KTAAGRRHER TDHEHHERVD VIIVDVKTVD SVSAFVAQLE KDVSSPPSVF AYWDGSETAG
EGTALAPSQP VLAELSVPGT PSGTADGPQD RSSTRPMREA NATAGSGGLA ATVLSSIDAG
APNGRSGFPE LERTGVESSG RSDDGEAVDV SHPELVATVR RELADATSPQ TVERVLRTVF
TERDAFVFAW VGEYDRGERS VVPWATDPDA TEWPIHRTFR VGNGANPLLE RALYSQRLQT
QNLTSQPDLA ISGGAFTPAP FHDRARDHGA RSIAVAPLAT ESDRYGVLVV YAPTTFTAST
RRTIRAVAGV ASHVLETIAI RGQLEQQERT LHRYERLVKT AGDGIFVLDG SGHVMTVNDA
FVEMTGYSRE WLLGEHISLL FDDQTIEHAT ETVQSLVEAD RRSATIEVPL ETKTGSYVTC
EAQIAVLDRP SGDGTNNDSG SASGSGTDSG GDIDTATDTG TDTTITIGGT VGVLRDITER
KQNERRLRKQ NERLDAFARI VSHDLRNPLG IAQGYLDLID ETGSLEHLPT AQRSLDRMEA
IIHDVLAIAR DGTWASDTER VDLETVAREA WEHVSTGEAT LTLTETTTFM ADRSRLLRVF
ENLFRNAIEH GCPNGETDEL AMRVGVLEFE SSDQRRLSIA GGDEQTGDPC GFFVADNGSG
LPDDLAANDD LFDPSISSAT DSLGIGLWIV REVATGHDWQ VTARESEAGG ARFEFVTGNA
EQ
//
