ID A0A1G3R3Y5_9SPIR Unreviewed; 534 AA.
AC A0A1G3R3Y5;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=A2V99_14755 {ECO:0000313|EMBL:OHD73656.1};
OS Spirochaetes bacterium RBG_16_67_19.
OC Bacteria; Spirochaetota.
OX NCBI_TaxID=1802196 {ECO:0000313|EMBL:OHD73656.1, ECO:0000313|Proteomes:UP000177018};
RN [1] {ECO:0000313|EMBL:OHD73656.1, ECO:0000313|Proteomes:UP000177018}
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:OHD73656.1}.
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DR EMBL; MIBK01000144; OHD73656.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G3R3Y5; -.
DR STRING; 1802196.A2V99_14755; -.
DR Proteomes; UP000177018; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd00082; HisKA; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.450.40; -; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR003018; GAF.
DR InterPro; IPR029016; GAF-like_dom_sf.
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; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR PANTHER; PTHR43065:SF10; PEROXIDE STRESS-ACTIVATED HISTIDINE KINASE MAK3; 1.
DR PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR Pfam; PF01590; GAF; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF52172; CheY-like; 1.
DR SUPFAM; SSF55781; GAF domain-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 169..392
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 415..532
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 391..413
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 133..160
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 394..408
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 466
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 534 AA; 57029 MW; 5E8B525D579D1B5D CRC64;
MVFLAEPDGT TVRLAYSSHG QESAQAVRAL LGRPAKEIAF DIESAEQIRK VIRERRVLLL
DAEEAVSQAL PGELKTQAAA IVRALNTRWA IEVPLTVEEK VIGLLVVHSG DLDQQDLPAI
TAFANQIAAS WQKARLMQDL ERSLRELQRT QGELIQAQKM EAIGRLAGGI AHDFNNLLTA
IGGYAQLLLE RFTGSDPARA DLEEIKKATG KAGALTRQLL AFSRKQVLQP RVLDLNEVIT
NMQTMLRPLI GEHIALEASL APELGRVKAD PLQLEQVIMN LAINAADAMP RGGRLILETD
NVEVEPGLEP AAPELRPGLY VLLAVSDDGV GMDSDTQGRL FEPFFTTKPP GKGTGLGLST
VYGIVAQSGG HVQAYSRPGY GSSFKVYLPR MPDPDIPAAE PPSPPPAQGS RGGETVLLVD
EDAAARDLLS KVLGARGYTV LEADQAETAL AQADGRGAQV QLVISDVILP GGMGGEALAA
LLASRHPGMR FLFVSGYTAG AVRHGGLLPP GARFLQRPFG PEALARAVRE VLDG
//
