ID A0A1G2QS42_9BACT Unreviewed; 331 AA.
AC A0A1G2QS42;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=A2117_02455 {ECO:0000313|EMBL:OHA62812.1};
OS Candidatus Wildermuthbacteria bacterium GWA2_46_15.
OC Bacteria; Candidatus Wildermuthbacteria.
OX NCBI_TaxID=1802443 {ECO:0000313|EMBL:OHA62812.1, ECO:0000313|Proteomes:UP000179245};
RN [1] {ECO:0000313|EMBL:OHA62812.1, ECO:0000313|Proteomes:UP000179245}
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:OHA62812.1}.
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DR EMBL; MHTO01000003; OHA62812.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G2QS42; -.
DR STRING; 1802443.A2117_02455; -.
DR Proteomes; UP000179245; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR CDD; cd06225; HAMP; 1.
DR Gene3D; 6.10.340.10; -; 1.
DR InterPro; IPR003660; HAMP_dom.
DR PANTHER; PTHR45436:SF5; SENSOR HISTIDINE KINASE TRCS; 1.
DR PANTHER; PTHR45436; SENSOR HISTIDINE KINASE YKOH; 1.
DR Pfam; PF00672; HAMP; 1.
DR SMART; SM00304; HAMP; 1.
DR SUPFAM; SSF158472; HAMP domain-like; 1.
DR PROSITE; PS50885; HAMP; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777}; Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT TRANSMEM 6..31
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 167..189
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 190..242
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT COILED 294..328
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 331 AA; 37903 MW; C1FA605878D5D0E8 CRC64;
MRTKHLSIYN IVLAVFAWTL LVGAILVYFS LSQQRQDLYR SAVEEKVKLA ETIKETVASP
SWLYQISLLR DLERGLIAGL SKFKDVRFIR VVKISGEIYQ SSLAGEIGKK IKEPGVVEVA
QSGKPLIRDD VFQNEEIKLL IYPGYEDRTI WIGFSLKDTE VLIQKLLLRY FFMALAALLL
LGLALFVILR SVVDPIRKIT ASCEDVRRGN LDIQAEVGWQ TEIGELAETF NKMIGDLKAS
RKSLEESKEV LEIRVVARTK ELEDLAQSLE GQVKVRTRDL REKMEQLERF NKLAVDRELK
MIELKKDINE LRAQLNESTS KRDRSKKTNT A
//
