ID A0A1G3PRI2_9SPIR Unreviewed; 467 AA.
AC A0A1G3PRI2;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=A2Y33_08900 {ECO:0000313|EMBL:OHD57035.1};
OS Spirochaetes bacterium GWF1_51_8.
OC Bacteria; Spirochaetota.
OX NCBI_TaxID=1802190 {ECO:0000313|EMBL:OHD57035.1, ECO:0000313|Proteomes:UP000177109};
RN [1] {ECO:0000313|EMBL:OHD57035.1, ECO:0000313|Proteomes:UP000177109}
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:OHD57035.1}.
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DR EMBL; MIBE01000010; OHD57035.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G3PRI2; -.
DR STRING; 1802190.A2Y33_08900; -.
DR Proteomes; UP000177109; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
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; 1.
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; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013656; PAS_4.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR NCBIfam; TIGR00229; sensory_box; 1.
DR PANTHER; PTHR43711:SF1; HISTIDINE KINASE 1; 1.
DR PANTHER; PTHR43711; TWO-COMPONENT HISTIDINE KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF08448; PAS_4; 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.
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 30..49
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 231..459
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT COILED 197..231
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 467 AA; 52995 MW; B9FAB8B6A172D61C CRC64;
MGALIAGTIS TALAWWFFIP VINSFQFENP YSILSVFMFI SMSILYGFSQ ERTRVANKKA
AEALASERSA FLQLENEKRF RQTLDIMIEG CQIIDREFRY VYLNDTAAIH ARMKKEDLLG
HSMAEMFPGI DNSEMFAKLR LCLDNNESHR MENLFQYPDG TSKWYDLRIQ PAPEGAFILS
LDITDFKEAQ TILSRTNVEL ENMVQERTRS LEAALKEADE ANRAKSDFLA NMSHELRTPL
NSVIGFSEVL QDRLFGELND KQKEYLSYIE KSSRHLLTLI NDILDLSKVE SGNMRLEVSE
VPVRGVIDSS LLMVKEKALK HSVSLAVEIA PDADITLSAD ERKLKQVIVN LLTNAVKFTR
DHGKVSVAVY TNKSPGGNEK TVELIFRIED TGIGIKPDEL SQLFKRYGQL ETAYQRKYEG
TGLGLSLVKR LVELHGGRVW AESEFGKGSR FYFSLPIDLQ ASRPDVK
//
