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Database: UniProt
Entry: A0A1V4HBF0_9BACL
LinkDB: A0A1V4HBF0_9BACL
Original site: A0A1V4HBF0_9BACL 
ID   A0A1V4HBF0_9BACL        Unreviewed;       345 AA.
AC   A0A1V4HBF0;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=BC351_37475 {ECO:0000313|EMBL:OPH49282.1};
OS   Paenibacillus ferrarius.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=1469647 {ECO:0000313|EMBL:OPH49282.1, ECO:0000313|Proteomes:UP000190626};
RN   [1] {ECO:0000313|Proteomes:UP000190626}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CY1 {ECO:0000313|Proteomes:UP000190626};
RA   Florea S., Webb J.S., Jaromczyk J., Schardl C.L.;
RL   Submitted (JUL-2016) 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:OPH49282.1}.
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DR   EMBL; MBTG01000040; OPH49282.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1V4HBF0; -.
DR   STRING; 1469647.BC351_37475; -.
DR   OrthoDB; 9780487at2; -.
DR   Proteomes; UP000190626; 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:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0000160; P:phosphorelay signal transduction system; IEA:UniProtKB-KW.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   InterPro; IPR003594; HATPase_C.
DR   InterPro; IPR036890; HATPase_C_sf.
DR   InterPro; IPR005467; His_kinase_dom.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   PANTHER; PTHR45453; PHOSPHATE REGULON SENSOR PROTEIN PHOR; 1.
DR   PANTHER; PTHR45453:SF2; TWO-COMPONENT SENSOR HISTIDINE KINASE; 1.
DR   Pfam; PF02518; HATPase_c; 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   PROSITE; PS50109; HIS_KIN; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Kinase {ECO:0000313|EMBL:OPH49282.1}; Membrane {ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000190626};
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        12..30
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        42..62
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          128..337
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
SQ   SEQUENCE   345 AA;  39296 MW;  67D88F527EDCF558 CRC64;
     MSFVHYLKDK RYFFLIYGVI MLFVSLIMFV SVKWQDAINN IAYANAGCLF FAAVYITVGY
     YYRKSFFNEL QDLVGNTQVE SAITSVPEPQ SAEQALYLKL LKQLYLEQTN GTRKLQNEMK
     DHQNFVLSWI HEVKVPIAAS RLIMENYSGK SAEHLVDKLE DELSKIDSYV EQALYYSRID
     SFSRDYFIIE VPLQTIAKES VKRAAKLFIN KRIRPNLEEL HHTVNSDSKW LSYMVNQIVM
     NSLTYTPSGG SIAFISEETE HDKRLIIQDS GLGISPADLG RVFDKGFTGS IGRTHYKSTG
     MGLYLAKQMA LKLGHDLTIA SVEGKGTAVT IHFPKIRNYD DLRGA
//
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