ID H5S883_9BACT Unreviewed; 648 AA.
AC H5S883;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=HGMM_F01A04C16 {ECO:0000313|EMBL:BAL52369.1};
OS uncultured Planctomycetota bacterium.
OC Bacteria; Planctomycetota; environmental samples.
OX NCBI_TaxID=120965 {ECO:0000313|EMBL:BAL52369.1};
RN [1] {ECO:0000313|EMBL:BAL52369.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=16309394; DOI=10.1111/j.1462-2920.2005.00881.x;
RA Nunoura T., Hirayama H., Takami H., Oida H., Nishi S., Shimamura S.,
RA Suzuki Y., Inagaki F., Takai K., Nealson K.H., Horikoshi K.;
RT "Genetic and functional properties of uncultivated thermophilic
RT crenarchaeotes from a subsurface gold mine as revealed by analysis of
RT genome fragments.";
RL Environ. Microbiol. 7:1967-1984(2005).
RN [2] {ECO:0000313|EMBL:BAL52369.1}
RP NUCLEOTIDE SEQUENCE.
RA Takami H., Noguchi H., Takaki Y., Uchiyama I., Toyoda A., Nishi S.,
RA Chee G.-J., Arai W., Nunoura T., Itoh T., Hattori M., Takai K.;
RT "A Deeply Branching Thermophilic Bacterium with an Ancient Acetyl-CoA
RT Pathway Dominates a Subsurface Ecosystem.";
RL PLoS ONE 7:e30559-e30559(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; AP011626; BAL52369.1; -; Genomic_DNA.
DR AlphaFoldDB; H5S883; -.
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; 3.
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; IPR013655; PAS_fold_3.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR NCBIfam; TIGR00229; sensory_box; 3.
DR PANTHER; PTHR43065:SF10; PEROXIDE STRESS-ACTIVATED HISTIDINE KINASE MAK3; 1.
DR PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF08447; PAS_3; 1.
DR Pfam; PF08448; PAS_4; 1.
DR Pfam; PF13426; PAS_9; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00086; PAC; 3.
DR SMART; SM00091; PAS; 3.
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); 3.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 2.
DR PROSITE; PS50112; PAS; 3.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:BAL52369.1};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Transferase {ECO:0000313|EMBL:BAL52369.1}.
FT DOMAIN 14..50
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 133..209
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 213..264
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 265..318
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 336..389
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 402..625
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 648 AA; 73565 MW; DC26C768F2590156 CRC64;
MKTAFGYAEL ALTLFEESAD ALILFDPETE QILDVNPFAQ RLTGYTRREL RSVLITDLFR
SDKAGGLNHL RRAYQKTSVF HSQEGFWIRQ REQGWLPVNL SITRLHLDGQ VLGLVTARDV
SEMHAVRKQL EQREAELRHI LNSVSDFLWS AEIDTKGVWK MRYISSVVER LTGRSPEFFH
NSPEAWLSIL HPEDRPLMAQ RWAQVRSGEV EHVEDEYRVV RPDGQVRWLR DSVSVQRQKD
GRLMVHGVVS DVTERRKILE QLRYSEAKYR ALIENLEQCV FLKNRELRFA AVNPRFCEAV
GKPEHEILGK TDYDFYPPHL AEKYRADDMV VLTTGQTLEL EEENVSEGRT RLVRVVKRPM
RDEQGNIVGV LGIFWDITHQ RALEEQLRHA QKMEAVGQLA GGVAHDFNNL LTAILGNVSL
VLARLAPDDP NRELLQITEK AALRAAELTR QLLSFSRRTR LRPQPTEINP IVEETLSLLR
RTIDKRVEIQ SDLDPQCGKV HADAGQMQQV LMNLCLNARD AMPEGGKLLV RTRRVVLSAE
DARRHVSARP GIFVRLDVVD TGHGIPPEIR SRIFEPFFTT KGQGRGTGLG LAMVYGIIEE
HHGWIEVESE VGRGSTFSVF LPVHGLEELA TGQQPTVAAD GAASVSPP
//
