ID A0A1Q3QQG4_9BACT Unreviewed; 598 AA.
AC A0A1Q3QQG4;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=BGO25_18995 {ECO:0000313|EMBL:OJV41744.1};
OS Acidobacteriales bacterium 59-55.
OC Bacteria; Acidobacteriota; Terriglobia; Terriglobales.
OX NCBI_TaxID=1895690 {ECO:0000313|EMBL:OJV41744.1, ECO:0000313|Proteomes:UP000186822};
RN [1] {ECO:0000313|EMBL:OJV41744.1, ECO:0000313|Proteomes:UP000186822}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=59-55 {ECO:0000313|EMBL:OJV41744.1};
RA Kantor R.S., Huddy R.J., Iyer R., Thomas B.C., Brown C.T., Anantharaman K.,
RA Tringe S., Hettich R.L., Harrison S.T., Banfield J.F.;
RT "Genome-resolved meta-omics ties microbial dynamics to process performance
RT in biotechnology for thiocyanate degradation.";
RL Submitted (SEP-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};
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:OJV41744.1}.
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DR EMBL; MKSV01000007; OJV41744.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q3QQG4; -.
DR STRING; 1895690.BGO25_18995; -.
DR Proteomes; UP000186822; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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; cd00075; HATPase; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd19410; HK9-like_sensor; 1.
DR CDD; cd00130; PAS; 1.
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; 1.
DR InterPro; IPR007891; CHASE3.
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; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013767; PAS_fold.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR NCBIfam; TIGR00229; sensory_box; 1.
DR PANTHER; PTHR43065:SF10; PEROXIDE STRESS-ACTIVATED HISTIDINE KINASE MAK3; 1.
DR PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR Pfam; PF05227; CHASE3; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00989; PAS; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
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; 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; PS50113; PAC; 1.
DR PROSITE; PS50112; PAS; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:OJV41744.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Transferase {ECO:0000313|EMBL:OJV41744.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..30
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 184..202
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 229..302
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 307..359
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 372..591
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 598 AA; 66027 MW; 43F0B30C249B44E8 CRC64;
MNLSQFNRIL RQVFLLPVIA LLLMAVALYL QIRGANSTVN LIQESNARIA QVSRIEKLIL
NEESGLRGYE NTSDNRFLQP YLAASSSLQA EFDRMQTLPG LDSVEKHYLD DLIEKHQLWQ
DAFALPVIAT IRAGGQVRDV DLNLRGKIMM DDIRQDIADT THNAEQRRSA RIELWRRQVR
QMEWFLLALA LCVGISIGLF TLNRLHAVSS AYKTSLDVLG RRAEEIFQSE QELRTTLASI
GDGVITCDAA GRVQMMNPVA VQLTGWTQAE AQGQPLEAIF HIVNEKTRDI VENPVAKVKR
LNRIVGLANH TVLIRKDKTE LNIADSGAPI RDRTDGIAGV VMVFRDITLE RKTQDALLAN
EKLAVAGRLA ATIAHEIHNP LDSVSNLLYL MRNGASKEES EQFMDMAEQE LARVTQISRA
MLGLYRESKA PVQVDLKEML QEILLLMEHR FSDERVTIHT DLPSSVSVDA FPAELRQVFT
NLIANAAEAA GPGGEVRVSI TPRGPDAYSN GIKQEPGATV LIADNGAGIP DDVRPRLFQP
FFTTKGERGT GLGLWVSRGI ITKHGGSIEL DSDTGHSTHG TVVSVFLATK PTINAGGD
//
