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Database: UniProt
Entry: A0A1Y6FR05_9BACI
LinkDB: A0A1Y6FR05_9BACI
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ID   A0A1Y6FR05_9BACI        Unreviewed;       536 AA.
AC   A0A1Y6FR05;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=SAMN05444673_2711 {ECO:0000313|EMBL:SMQ77107.1};
OS   Bacillus sp. OV166.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=1882763 {ECO:0000313|EMBL:SMQ77107.1, ECO:0000313|Proteomes:UP000194454};
RN   [1] {ECO:0000313|EMBL:SMQ77107.1, ECO:0000313|Proteomes:UP000194454}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OV166 {ECO:0000313|EMBL:SMQ77107.1};
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};
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DR   EMBL; FXWM01000001; SMQ77107.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y6FR05; -.
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   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; IPR003594; HATPase_C.
DR   InterPro; IPR036890; HATPase_C_sf.
DR   InterPro; IPR005467; His_kinase_dom.
DR   InterPro; IPR033463; sCache_3.
DR   InterPro; IPR029151; Sensor-like_sf.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   InterPro; IPR016120; Sig_transdc_His_kin_SpoOB.
DR   InterPro; IPR039506; SPOB_a.
DR   PANTHER; PTHR43065:SF10; PEROXIDE STRESS-ACTIVATED HISTIDINE KINASE MAK3; 1.
DR   PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF17203; sCache_3_2; 1.
DR   Pfam; PF14689; SPOB_a; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF103190; Sensory domain-like; 1.
DR   SUPFAM; SSF55890; Sporulation response regulatory protein Spo0B; 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:SMQ77107.1};
KW   Membrane {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        12..32
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        179..199
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          434..534
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
SQ   SEQUENCE   536 AA;  59401 MW;  F0F09519D26B5FED CRC64;
     MGWKIRLSKP KLRLQSTITL LVCIVVVMAL LVTEILITNR ISQETEKSQA EKATDIARIV
     ARSPIVMNGL KNKTAEKDIQ TFANDIKQST HVEFIVVMDM YGTRKSHPNR NLLGLHFVGG
     DEGPVLKGKE HISIAKGTLG LSLRSFVPVY DQENNQIGAV AVGISLEKVN QAIEQSRKII
     LIGVGVGILV GILGALFLAR KIKAILFGLE PSEMAKLLEE RSAMLQSTKE GILAVDQDAF
     TTLVNNEGIR LLQKAGIHGS FLGRKVDDYM PNSMLSSVLE TGESQLDQEQ EINHITILTN
     RVPVVVKGKI VGAIATFREK TEIKQLAEQL TGVKLYAEAL RTQSHEFMNK LHVISGLIHM
     KDYQMVSSYI TKIVDHQQTE VEFVISRFKD PVLAGFIVGK LSFARENGCE LIIDGEGSLP
     EPQQQEITHE VVTILGNLID NALDAVTDRP QKKVTLRFDY YDDVLALEVH DTGKGIDEAV
     KNRLFIKGYS TKGENRGIGL SLVQRSLEKL NGQIEIHSQK DKGTTFIVTF LYKGKQ
//
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