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Database: UniProt
Entry: A0A1Y6ER59_9BACI
LinkDB: A0A1Y6ER59_9BACI
Original site: A0A1Y6ER59_9BACI 
ID   A0A1Y6ER59_9BACI        Unreviewed;       506 AA.
AC   A0A1Y6ER59;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=SAMN05444673_1104 {ECO:0000313|EMBL:SMQ64816.1};
OS   Bacillus sp. OV166.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=1882763 {ECO:0000313|EMBL:SMQ64816.1, ECO:0000313|Proteomes:UP000194454};
RN   [1] {ECO:0000313|EMBL:SMQ64816.1, ECO:0000313|Proteomes:UP000194454}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OV166 {ECO:0000313|EMBL:SMQ64816.1};
RA   Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA   Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL   Submitted (APR-2017) to the EMBL/GenBank/DDBJ databases.
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   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR   EMBL; FXWM01000001; SMQ64816.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y6ER59; -.
DR   OrthoDB; 9815750at2; -.
DR   Proteomes; UP000194454; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
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   CDD; cd12914; PDC1_DGC_like; 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; 2.
DR   InterPro; IPR033479; dCache_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; IPR029151; Sensor-like_sf.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   PANTHER; PTHR43065:SF10; PEROXIDE STRESS-ACTIVATED HISTIDINE KINASE MAK3; 1.
DR   PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR   Pfam; PF02743; dCache_1; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 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; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR   SUPFAM; SSF103190; Sensory domain-like; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:SMQ64816.1};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius};
KW   Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT   TRANSMEM        247..270
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          295..501
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
SQ   SEQUENCE   506 AA;  56671 MW;  9B78DE816D8200EC CRC64;
     MVVIRSFTSI LKNKFLLYLL LTLIPTVAIS TVLAQHQVKF LEDQNQYKAQ EYANLHTQNI
     ENLLGETVGR LEMLATSIKY QKNNLNDVEN LLRETMGKDL RLSGFFWTNA NGDLLISTNT
     NSKNINVSDQ PYFQQAIKTE KTSFSEVHIG RVTGRQIISI ATPIINHGQL QGVLVASLRI
     DEIKAAIKNH VKDEMVIVTD GSDHILLTAG SVPEESSIKS SMKIAKIPLT ISVLVRSEND
     LAFWKPFLKY LIIFLTISNI IFLSAQYFLL KRKIKKENEQ TELHKLELIG KLAASTAHEI
     RNPLTGIKGL VKLLSEEYQD KKTQSYFEVI QMEIDRINVI VSELLVLGKP TAHTLKTYNA
     NSIVAEIEPI IHSEANYMNV VLTVDYHSEE LLVSCVKDQL KQVILNLTKN SLQAMPYGGK
     FSITLHKQLD NCLITVTDNG VGMQKDQISQ AFNPFFTLKK DGSGLGLTVC KRIIDSYGGK
     ISIKSNPNEG TQVVITLPLV IDENSD
//
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