ID A0A1I6KIG9_9EURY Unreviewed; 1217 AA.
AC A0A1I6KIG9;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=SAMN05216559_0821 {ECO:0000313|EMBL:SFR90670.1};
OS Halomicrobium zhouii.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Haloarculaceae; Halomicrobium.
OX NCBI_TaxID=767519 {ECO:0000313|EMBL:SFR90670.1, ECO:0000313|Proteomes:UP000199062};
RN [1] {ECO:0000313|EMBL:SFR90670.1, ECO:0000313|Proteomes:UP000199062}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.10457 {ECO:0000313|EMBL:SFR90670.1,
RC ECO:0000313|Proteomes:UP000199062};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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};
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DR EMBL; FOZK01000001; SFR90670.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I6KIG9; -.
DR STRING; 767519.SAMN05216559_0821; -.
DR OrthoDB; 106630at2157; -.
DR Proteomes; UP000199062; Unassembled WGS sequence.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 3.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 7.
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; IPR004358; Sig_transdc_His_kin-like_C.
DR NCBIfam; TIGR00229; sensory_box; 7.
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; 5.
DR Pfam; PF13426; PAS_9; 2.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00086; PAC; 4.
DR SMART; SM00091; PAS; 7.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 7.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 4.
DR PROSITE; PS50112; PAS; 4.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000199062}.
FT DOMAIN 101..158
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 160..212
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 213..269
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 428..480
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 485..530
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 666..722
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 719..788
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 901..963
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 981..1213
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT REGION 1115..1137
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 468..495
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 951..981
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1217 AA; 135991 MW; 11C49981DADB90F1 CRC64;
MGPSGSAPDV TREDALGVFS GLAEPHTPLT TGDVASTLEC SEQAAERRLR ALADDGAVRT
RQVGDGLRVW WRPADADLAT SRRSTLAEFG AFVRAVEDYA IFTLEADGTV ASWNDGAERI
KGYAADEIVG EHFSTFYTDE DVAAGVPEAN LETAAERGRV EDEGWRVRAD GTRFWADVVV
TAIRDDDGDL VGFTKVTRDR TEQREYEQQL RRERDLTEQI LETVPLSISL VEADGQFVRA
NEQTLDRLGL DEDELMDANV DAWDLYDADG DPIPVAERPW KRALEAGEPV TGFECQIDLP
SLGRRWLSVN AAPLGDGGDG EVAGDDRVVV TVEDVTDQKE RERQLRRERD QTEQLLRTVP
VGIAVQNADR ETLRTNEHVQ AEMGLTEQEF REQPVDEGEW QIYDVDGDPL GPEETPSARA
IEQEAAVFDE EIVMESPDGD RTHYRINAAP LFDDDGVVER VVLAGEDITE LKTQQRQLER
QKSELETELG EIFERISDAF YALDDEWRFT HVNERAAEIV GHSPDELLGQ VAWDQIPGGR
DGALGERFRT AMDTQEPITF EEYVPVSDVW LEFNVYPSES GLSTYFRDVT ERKERERELE
ESERRYRALV ENFPNGVVAL VDEDLRYQTV GGSPTDVVDR TIDQVEGEYV GDALPDELAD
ELVPYYEAAI RGERGEFEAD VGERVFQFQV VPVRDAAGDI FAALGMSQDV TDQKRREREL
TKYETIVETV NDGIYVKDDD GYFTMVNDAY AELTGYDREE LVGAHSSLVV DEAAIEQSRE
LEAAMERGDN PTMEATIQTA GDEAVPAEAT FTTFETSDGE RNHVGVVRDI SERLAQRRRL
EESERRHRTL VENFPDGAVG LFDEDLEYTA VGGQLLDAAG VGKEDRVGST VSDVYPDHLV
ETVEPYFESA LDGESNSFEA EFHDRHLLAH TLPVTNADDE VFAGMLVVQD VTEQVEREQR
LEELVDRLEA SNERLEQFAY AASHDLQEPL RMVSSYLRLI EQRYADELDD DGREFIEYAV
DGADRMRDMI EGLLQYSRVD TRGDPFGPVD LNAVLADVRD DLQVRIDETD ADVDAEDLPV
VEGDGGQLRQ VFQNLLDNAI EYSGDAPPEI RLSAQRRGVR ASDPSEGSSD EWPESDGDWW
EISVTDQGIG IDPADADRVF EVFQRLHAPD DHSGTGIGLA LCERIVERHG GDIWVDSEPG
EGATFTFTLP AAGERDA
//
