ID M0A3Z0_9EURY Unreviewed; 933 AA.
AC M0A3Z0;
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=C483_05858 {ECO:0000313|EMBL:ELY93465.1};
OS Natrialba hulunbeirensis JCM 10989.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC Natrialbaceae; Natrialba.
OX NCBI_TaxID=1227493 {ECO:0000313|EMBL:ELY93465.1, ECO:0000313|Proteomes:UP000011519};
RN [1] {ECO:0000313|EMBL:ELY93465.1, ECO:0000313|Proteomes:UP000011519}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 10989 {ECO:0000313|EMBL:ELY93465.1,
RC ECO:0000313|Proteomes:UP000011519};
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:ELY93465.1}.
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DR EMBL; AOIM01000014; ELY93465.1; -; Genomic_DNA.
DR RefSeq; WP_006652412.1; NZ_AOIM01000014.1.
DR AlphaFoldDB; M0A3Z0; -.
DR STRING; 1227493.C483_05858; -.
DR PATRIC; fig|1227493.4.peg.1144; -.
DR Proteomes; UP000011519; 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; 2.
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; IPR013656; PAS_4.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR NCBIfam; TIGR00229; sensory_box; 1.
DR PANTHER; PTHR43304:SF1; PAC DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR43304; PHYTOCHROME-LIKE PROTEIN CPH1; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF08448; PAS_4; 2.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00065; GAF; 2.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00091; PAS; 2.
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); 2.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50112; PAS; 2.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:ELY93465.1};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Transferase {ECO:0000313|EMBL:ELY93465.1}.
FT DOMAIN 306..359
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 420..494
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 718..933
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 66..90
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 140..195
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 207..247
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 66..82
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 169..185
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 214..233
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 933 AA; 103479 MW; 8847EDD0C029B75B CRC64;
MPAPPRTDSG ESSVSDVRRH REHVVREIRQ RALEYTRLDR FLDDVSDRIV TAVDVPALSV
LEFDDVPTEK PADAETESSA DAERATRIAP TATVRAVATS EETVSAESSG ETAIGCSHSV
AHGLVGRALE SAEPVVGEVS GDDLGFVSVG SMSGGGTEDR DEGGDEDRDS GGDENRDRAR
DGVEGSGDND NASSVRGCVV RLGGAGESEY NGGCDRGHGY DRAPEERAKS QSGDEDQPVS
VSDSEHDQPW GLLTLTLPTD TTHQFNEADI AFLQRVATVL ESAIRNVQAK QRPEPECTAT
EAGFSTHDRV VQALETASEG ISLLDEEGTF IYVNSAYAAL YGYEPESMIG MHWERLYPEG
MTDDLYEDMI STLQEGESWS GETVGLRRDG SQFIEDHYLA PTDDGGMVCV VRDVTKRRQL
EEELDEVHTR ITDAFIGIDT DWTFTYVNDS AVDLLDASDE ALVGRSFWSV FPDTDDVESI
LRDAAATQES VSFEANVPAL DAWLEINAYP SETGLSIYLR DVSDREETKR ELRKSNRTLQ
RLYEITADRE RSFEEKVDDL LELGRERLDL PVGFVSAVDA DRNRFEVAQS IGGREIEPGA
TAPLSETYCR ETIDTDDLLV LIDSPPAETV SDAAYERWDF DAYVGGKVMV DDTLYGTLCF
AGDDERPAPF SPAEQRFVEL ATQWLSYEYE RQRRQTELET LVSNLESSNE RLEQFAHAAS
HDLQEPLRMV SSYLQLLDSR YREELDDEGA EFLEFAVNGA DRMRAMIDGL LEYARVETRG
EPLEPVELDT IVEEVRKDLQ VQVTERDAEI TVESLPRVQG DESQLRQVVQ NLLSNALVYN
DEESPTVHVS AERRTWDDEC VISIADDGIG IDADDQERIF SVFDRLHSRE EFEGTGIGLA
LCQRIVERHG GTIWVESEPG EGTTISFTLP LAE
//
