ID A0A1F5MGX6_9BACT Unreviewed; 740 AA.
AC A0A1F5MGX6;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=A3J13_01565 {ECO:0000313|EMBL:OGE64626.1};
OS Candidatus Daviesbacteria bacterium RIFCSPLOWO2_02_FULL_36_8.
OC Bacteria; Candidatus Daviesbacteria.
OX NCBI_TaxID=1797793 {ECO:0000313|EMBL:OGE64626.1, ECO:0000313|Proteomes:UP000183317};
RN [1] {ECO:0000313|EMBL:OGE64626.1, ECO:0000313|Proteomes:UP000183317}
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:OGE64626.1}.
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DR EMBL; MFDU01000004; OGE64626.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F5MGX6; -.
DR Proteomes; UP000183317; 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 Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.450.40; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
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; IPR031621; HisKA_7TM.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR PANTHER; PTHR43711:SF1; HISTIDINE KINASE 1; 1.
DR PANTHER; PTHR43711; TWO-COMPONENT HISTIDINE KINASE; 1.
DR Pfam; PF13185; GAF_2; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF16927; HisKA_7TM; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 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.
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 6..22
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 29..49
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 61..82
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 94..114
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 134..153
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 169..191
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 197..217
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 237..259
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 492..714
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT COILED 458..485
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 740 AA; 82502 MW; 382E1A142F677A3B CRC64;
MELPVTIFTV ASNVFLGLLT YFKNPRSATN ILFALLSTIL GAWAVSNYFS LHAADLPSTL
AWIRIVLSIV TPMWTVLFLL VLVFPGDELK VNKVLFGFLI LYTILTSGVA LSPYMFTSIT
GTLANPQPVP GPGIALHAVL AIGSLIACSF VLIRRFRKAQ GRLRSQLKFF LFGIVISFSL
LILTNFVLVN VFQNTSLVVF GPFFTLILVG SISYAIVRHR FLDIRLIVAR TVAYVSLLTI
LAVVYSLGFF VIGDFIIGVT GRGQLVVSTA LAMIIALSFQ PLRNFIERLT DKIFFRYHYD
SQEFLKNLSV FMSVTIDLKR LTGGILEKLL SEVRITRGAF ILLVSHDHDM IEATDFRGYD
RSPIITASEI AQFLSQKNMF VFDELPEGLP KEIMRKLNIS LVLPLIVNDE KVGVLFLGEK
QSGDIYSQKD IKVLEILVPE LSVAIKHSKE YEEIKKFNIT LREEVNKATG ELKEANVKLQ
ELDLLKDDFV SIASHELRTP MTAIRSYAWM ALHKADIPLS DKVEKYIIRV LLSTERLINL
VNDMLNISRI ESGRIEINPE SVDLVSLVKD IVDEVYYSKS TERNLHFMIL EKKIPKAFAD
PDKLRQVLLN LVGNSLKFTP IDGKITFDFF TDGKVVEVSV KDSGVGISKE DQSKLFHKFS
RLDSSYTAIS TSGGTGLGLF ISKSLIELMH GKIWASSEGI GKGTTMTISL PVASPDIIAH
PENYIVKAKG EVKGLEPVAI
//
