ID G7WQY1_METH6 Unreviewed; 1176 AA.
AC G7WQY1;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 67.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=Mhar_1766 {ECO:0000313|EMBL:AET65124.1};
OS Methanothrix harundinacea (strain 6Ac) (Methanosaeta harundinacea).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanotrichales; Methanotrichaceae; Methanothrix.
OX NCBI_TaxID=1110509 {ECO:0000313|EMBL:AET65124.1, ECO:0000313|Proteomes:UP000005877};
RN [1] {ECO:0000313|EMBL:AET65124.1, ECO:0000313|Proteomes:UP000005877}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=6Ac {ECO:0000313|EMBL:AET65124.1,
RC ECO:0000313|Proteomes:UP000005877};
RX PubMed=22590603; DOI=10.1371/journal.pone.0036756;
RA Zhu J., Zheng H., Ai G., Zhang G., Liu D., Liu X., Dong X.;
RT "The genome characteristics and predicted function of methyl-group
RT oxidation pathway in the obligate aceticlastic methanogens, Methanosaeta
RT spp.";
RL PLoS ONE 7:E36756-E36756(2012).
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; CP003117; AET65124.1; -; Genomic_DNA.
DR AlphaFoldDB; G7WQY1; -.
DR STRING; 1110509.Mhar_1766; -.
DR KEGG; mhi:Mhar_1766; -.
DR PATRIC; fig|1110509.7.peg.1963; -.
DR HOGENOM; CLU_273498_0_0_2; -.
DR Proteomes; UP000005877; Chromosome.
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; 6.
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; IPR013767; PAS_fold.
DR InterPro; IPR013655; PAS_fold_3.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR NCBIfam; TIGR00229; sensory_box; 6.
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; PF00989; PAS; 2.
DR Pfam; PF08447; PAS_3; 2.
DR Pfam; PF13426; PAS_9; 3.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00086; PAC; 7.
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; 6.
DR PROSITE; PS50112; PAS; 7.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:AET65124.1};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000005877};
KW Transferase {ECO:0000313|EMBL:AET65124.1}.
FT DOMAIN 69..139
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 141..191
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 192..263
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 359..397
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 401..453
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 454..525
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 528..579
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 585..635
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 656..708
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 709..780
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 783..835
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 832..877
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 899..951
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 962..1173
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT COILED 3..48
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1176 AA; 132288 MW; 91E8DF6CE7FFBA64 CRC64;
MTRYILKEEL EKARRQVRAL LQEECPSIEG LSRGLEELSA TLEELDGSAE EAWGEGEELA
KANEALRRSL ERYRCLVENV DGVIYVVETT GKIAYISPSV ERIFGYPAGE VQGRNVSQFL
IPEDSRYLEE RLKSALDGIF RVSELRFIAK DGSVHHVRTY GRPILEGHLR GIHGIMVDVT
EQKKAEEALR ESEERLKLAV EGADLAIWNR DLSTGEVVGN RRYAEIVGTA PAEESDVLAW
KRSIHPEDLP SVERALREIA AGRTDLFDLE YRTTSAPAEA WVHDRGLVVK RDESGRPIKM
AGVMQDVTWQ KKTDRAILEA SEKRKELERI VNRSPAIAFV QAVPFGGPVE FVSENVSQLG
YAPEDFYSRA ASFDRNLVHP EDLELVVSEL GRQIEEGSRS FFQEFRVLTS SGEVRWLASN
VWISRDEAGA VTHVEGIALD ITERKNMEMA LAESERRFRE MADTLPQPIF ECDLAGKVTF
ANQTAFELYG YDRQDLEVGV NIFQVFAYED REEMMKNFQR SLHDDKVFTY EYTGLRKEGT
TFHLIVYSRP IIRDGRPVGL RGTIVDITER KRVEENIKQL ADLSEKLVEI GSPMIFVIDR
DRRIFLWNRA SEKALGYSAE EVLGDEEVWT LLFPDGEERS EFLKTLDEIE MGLTAEGRRT
RILAKSGEEK VISWSGIKLE DGEGNGIGIV ITAQDTTEYA KMEEEIRSER EFSRGIIEGA
DLFIVGLDPR GRITLFNRGA EKVTGVSAKE AFGENFFMRF VAGADRRGFE MAVSSIFEGK
PAEQTEAAVV TRTGEPMAIQ WGWSAVRSRT GEIERVIAFG HDISYDRWLE EQMLLFMDAI
ESSNDGIAIF GKSNHLLFAN PALLDMFGFR LEEARGRLHQ DFILDFGEDV SSSGEGNGGR
RRVTCVRKDG STFPASISFA PVASSDGKPM ATIVVARDIS EMIEYQQRLE TLNRELESFA
YTISHDLRAP LRGIRGFALA LQEDYGDDLE EAGRKYLERI GAIAENMDRL ILDLLDYSRI
GRIKSPPEMV DLKRLVAEAY EDVKSAGKGK PATLSLVGEF PTISCERSRA KQVFSNLLEN
SLKYSKDAIE IEVGSLDRGD EYEFWVKDDG LGFDMKYAEK IFDPFTRLER SGEGSGIGLA
TVKKIVETCG GRIWAESAPG RGAAFRFTIP KPADPA
//
