ID A0A1G1Q7S6_9BACT Unreviewed; 741 AA.
AC A0A1G1Q7S6;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=A2243_04460 {ECO:0000313|EMBL:OGX50044.1};
OS Omnitrophica WOR_2 bacterium RIFOXYA2_FULL_38_17.
OC Bacteria; Candidatus Omnitrophota.
OX NCBI_TaxID=1801873 {ECO:0000313|EMBL:OGX50044.1, ECO:0000313|Proteomes:UP000179162};
RN [1] {ECO:0000313|EMBL:OGX50044.1, ECO:0000313|Proteomes:UP000179162}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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:OGX50044.1}.
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DR EMBL; MHHG01000026; OGX50044.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G1Q7S6; -.
DR Proteomes; UP000179162; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; 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; cd00082; HisKA; 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; 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; IPR013767; PAS_fold.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR NCBIfam; TIGR00229; sensory_box; 2.
DR PANTHER; PTHR42878:SF7; BACTERIOPHYTOCHROME; 1.
DR PANTHER; PTHR42878; TWO-COMPONENT HISTIDINE KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00989; PAS; 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; 1.
DR SMART; SM00091; PAS; 2.
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); 2.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 1.
DR PROSITE; PS50112; PAS; 2.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils}; Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 35..55
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 207..231
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 247..317
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 321..373
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 374..440
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 528..741
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 490..521
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 741 AA; 84384 MW; B276D9DD9D2B54CF CRC64;
MKDSSYRDNK RPANNPTRQN TFKENFRKHF ELTKLAIILA AFSICAAIFI STFSYQRTIN
DTLNQHLIFY SKIAGMIAAD IGENLNMPDK EIVYSIERKW KKIKNRPSDE YLCIVNEDSK
LLLHTSIPSS VGNIVAKNLI LNKAEQKYCS LGDLVKEQKE YVGEYISSSG DAQIAAFEPV
TQKQWIVGVH RSKEDLLKEI NSALKSVFFS LIIICSTLIP ISFALLFWAF IACYRKGIHA
DQALTDFEIS YRAIVDGTDD LITQVDANGL FTFVNHASNK IWGLSPKDCI GLSAFDLIHP
DDRESTKKAF EGWISQKLKR ATYQNRQVNK DGQIFEMLWT INFDFNAAGE VVSVLNIAHD
ITEQKDAERR TFKSEENYRI LFNEMLSGFA QSEIICDSQG RPINSRYMVI NPAFERIVGV
KAEKVVGKTI LEVFPNLEPE WLEKFGRVAL TGKSEHFVAF ASDTGIWFDV LAFCPAPNQY
ACTFFDITAR KKAEQEITEL NKNLEKLVKE RTLKLEAVNA ELDAFNYSVS HDLRAPIRSM
EGFSKILLKN NENTLNEESK DHLNRIIKGA ARMKDLVDSL LKISRISRRD LVKNKINISD
LATNIFKTLR SDHPERLINV VIEKDLFLYG DKKLFNIALE NLIDNAWKFT SKVTDPRIEL
GSIKSESGVI FFIKDNGCGF DMEYADKIFI AFQRLHNKNE YPGIGIGLAT VKRIMNLHGS
KIWVKSELNK GTTFYFELPG A
//
