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Database: UniProt
Entry: A0A3D9IS27_9BACL
LinkDB: A0A3D9IS27_9BACL
Original site: A0A3D9IS27_9BACL 
ID   A0A3D9IS27_9BACL        Unreviewed;       448 AA.
AC   A0A3D9IS27;
DT   16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT   16-JAN-2019, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=DFP95_103157 {ECO:0000313|EMBL:RED63916.1};
OS   Cohnella lupini.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Cohnella.
OX   NCBI_TaxID=1294267 {ECO:0000313|EMBL:RED63916.1, ECO:0000313|Proteomes:UP000256869};
RN   [1] {ECO:0000313|EMBL:RED63916.1, ECO:0000313|Proteomes:UP000256869}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CECT 8236 {ECO:0000313|EMBL:RED63916.1,
RC   ECO:0000313|Proteomes:UP000256869};
RA   Whitman W.;
RT   "Genomic Encyclopedia of Type Strains, Phase III (KMG-III): the genomes of
RT   soil and plant-associated and newly described type strains.";
RL   Submitted (JUL-2018) 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:RED63916.1}.
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DR   EMBL; QRDY01000003; RED63916.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3D9IS27; -.
DR   Proteomes; UP000256869; 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   Gene3D; 1.10.287.130; -; 1.
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   InterPro; IPR016120; Sig_transdc_His_kin_SpoOB.
DR   InterPro; IPR039506; SPOB_a.
DR   PANTHER; PTHR40448; TWO-COMPONENT SENSOR HISTIDINE KINASE; 1.
DR   PANTHER; PTHR40448:SF1; TWO-COMPONENT SENSOR HISTIDINE KINASE; 1.
DR   Pfam; PF02518; HATPase_c; 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; SSF55890; Sporulation response regulatory protein Spo0B; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:RED63916.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000256869};
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        63..80
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        89..115
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        127..149
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        170..192
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        204..225
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          238..447
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
SQ   SEQUENCE   448 AA;  51066 MW;  20BBDF0D91EF2C80 CRC64;
     MHEFFDFLKL NLLASQPQTF VFWVFCFSFL EIRPPKLIKR IAILTVIHSI YTDILILALP
     LPFHFINTIV SGLLLLFIIF KEIGTKQKLF LMLFSLVLGV FTDLISGSIL IYVMGVSSHA
     DMIRDHLYQL LTVLYPELLV LLVASWFIHK RNLFSAKRLF TIVLKNERST LTKVIIFIFI
     QFVLLGALQI LQYTPDNNQA RNSIFIYVII FVSLLALVSI IRLLIRTREQ AARMTQEVYV
     EEINDMFTSI RGQRHDFLNH VQVIHTMVQM NRTEQLKSYV SELVKETRDV SDIVHHSSPA
     LAAFVQAKLT VSLGKSISFT YELPDRWNAQ ETTVKVIDVV KILGNLVDNA FDETSNLPLG
     QRQVHASISI NKEDRIELQV SNKGRTIDSA ERERIFAPGY STKGEGHSGL GLAIVQERVK
     HYNGDLSLQS DDANGTTLFR VTLPQTAV
//
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