ID A0A0B0IA22_9BACI Unreviewed; 681 AA.
AC A0A0B0IA22;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 24-JAN-2024, entry version 36.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=LQ50_15805 {ECO:0000313|EMBL:KHF39353.1};
OS Halalkalibacter okhensis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Halalkalibacter.
OX NCBI_TaxID=333138 {ECO:0000313|EMBL:KHF39353.1, ECO:0000313|Proteomes:UP000030832};
RN [1] {ECO:0000313|EMBL:KHF39353.1, ECO:0000313|Proteomes:UP000030832}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Kh10-101T {ECO:0000313|Proteomes:UP000030832};
RA Prakash J.S.;
RT "Genome sequencing and annotation of Bacillus Okhensis strain Kh10-101T.";
RL Submitted (SEP-2014) 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 -!- 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:KHF39353.1}.
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DR EMBL; JRJU01000020; KHF39353.1; -; Genomic_DNA.
DR RefSeq; WP_034630717.1; NZ_JRJU01000020.1.
DR AlphaFoldDB; A0A0B0IA22; -.
DR STRING; 333138.LQ50_15805; -.
DR eggNOG; COG5002; Bacteria.
DR OrthoDB; 9759607at2; -.
DR Proteomes; UP000030832; Unassembled WGS sequence.
DR GO; GO:0016020; C: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; cd00075; HATPase; 1.
DR CDD; cd00082; HisKA; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR InterPro; IPR011623; 7TMR_DISM_rcpt_extracell_dom1.
DR InterPro; IPR008979; Galactose-bd-like_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; 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; PF07695; 7TMR-DISM_7TM; 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; SSF49785; Galactose-binding domain-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000256|ARBA:ARBA00022777}; Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000030832};
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 209..228
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 235..260
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 272..289
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 301..323
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 329..347
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 359..378
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 459..679
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 681 AA; 78337 MW; A8B67AC37109B5C1 CRC64;
MKSKVRLMVL LLLTFFLLFL ALIFKHNEAI EDVVVRQGVA QLDAIQKDQI YNVTGDWEFH
WKELLEPDDF LMTALNPIYL KTPRSWVDTI KEHENNSIGY GTYRLQLVYP EDLMGEKQAF
YLGYIGVAYK VWVDGVLLDE VGEVSSNKEG EIPLLKSNFI YFEPDQEQVE VIIQVSNHEF
REGGIFGDVL TGSRTAITNY IVKNLAIDLL LIGGFLFIGI YHLVMFGVSK NDITFFYIGM
IGLLAALRNM LLCEYLFYLL FPTVPWTLMT RVEYLCEVVG LFFLVSLMYK MYPKEVNKHV
LNLAYAMIGI LVLYYLFAPM YIYTSTLTVS MIPLGLILFY FIFVVGLKAL AEGREGAKLN
VFGIILLTFA SINDILSYTQ SLQTIPMLGY STLFFLMLQG IIKSDRYTKL YEENRELTQT
LVKSNATLES KVIERTEKLG QTNKRLEELN NSRAEMLAFI AHDLGSPIIA IKTQLSLMKE
GYVAPNEQLY EQMIQKSDYM KRLVQDLFEL SKLESKEYVM LKKNVNVKKF MEDVWKVFSH
ELNNQQFMLS FTNMVGAQYD SIYIEADQQR LMQVLSNFIF NAVKYSKNVN KVELRVMTKY
KGSKGYVQVE VEDYGVGIEA ENIPFVFNRF YREQPHQKDG TGLGLTIAKE IIHKHGGVVG
VTSIKGKGST FYFTLPMKEE K
//
