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Database: UniProt
Entry: A0A0Q9U2I0_9BACL
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ID   A0A0Q9U2I0_9BACL        Unreviewed;       605 AA.
AC   A0A0Q9U2I0;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 41.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=ASG93_20970 {ECO:0000313|EMBL:KRF42179.1};
OS   Paenibacillus sp. Soil787.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=1736411 {ECO:0000313|EMBL:KRF42179.1, ECO:0000313|Proteomes:UP000051948};
RN   [1] {ECO:0000313|EMBL:KRF42179.1, ECO:0000313|Proteomes:UP000051948}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Soil787 {ECO:0000313|EMBL:KRF42179.1,
RC   ECO:0000313|Proteomes:UP000051948};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KRF42179.1, ECO:0000313|Proteomes:UP000051948}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Soil787 {ECO:0000313|EMBL:KRF42179.1,
RC   ECO:0000313|Proteomes:UP000051948};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) 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}.
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:KRF42179.1}.
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DR   EMBL; LMSP01000003; KRF42179.1; -; Genomic_DNA.
DR   RefSeq; WP_056830019.1; NZ_LMSP01000003.1.
DR   AlphaFoldDB; A0A0Q9U2I0; -.
DR   STRING; 1736411.ASG93_20970; -.
DR   OrthoDB; 9776552at2; -.
DR   Proteomes; UP000051948; 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; cd06225; HAMP; 1.
DR   CDD; cd12912; PDC2_MCP_like; 1.
DR   Gene3D; 6.10.340.10; -; 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; IPR003660; HAMP_dom.
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; IPR010559; Sig_transdc_His_kin_internal.
DR   PANTHER; PTHR42713; HISTIDINE KINASE-RELATED; 1.
DR   PANTHER; PTHR42713:SF2; TWO-COMPONENT SENSOR KINASE YESM; 1.
DR   Pfam; PF02743; dCache_1; 1.
DR   Pfam; PF00672; HAMP; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF06580; His_kinase; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00304; HAMP; 1.
DR   SMART; SM00387; HATPase_c; 1.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF158472; HAMP domain-like; 1.
DR   PROSITE; PS50885; HAMP; 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:KRF42179.1};
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        15..35
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        302..326
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          323..375
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          482..595
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
SQ   SEQUENCE   605 AA;  68403 MW;  63A9911E8DBDB4FC CRC64;
     MKLNRWVTSS LRTKMLIMFV MLTAIPLIAV GIISYTKSYN TVSQHSIATT ELVAEHLKNE
     MDVLFSDNRK FLDISKNSSV LRFLLIQNET YEEAKDILKT FSLYRDTYRF SNGITNIMLF
     NQYGKGISEK KGVFQMDGDP FQYGTFKNLL NYPDEILILP PSETDGFNNL DHAVQDSPFI
     ISIVATVKQE ITDEVIGFMV INLDATVIEN FCNNTKMGDN GFFYVTDSYG QPIIVPDKLK
     SAGRAAGLTK QQLFAPSGND IRHFNNRDQL VVYATSDLTG WKIVGEVPLS EVVKDAKQIE
     TLIFVSVVFT IVFTITLYAF ISSRLIRPIR FLKNKMRQAA SGYLEAKVGN VGHDEIADLG
     ISFNTMLDKI KILIENSIKE QEQIKMAELR TLQAQINPHF LYNTLDSIIW LAESKKSEEV
     IGIVNALATF FRISLSKGKD CITIREEIDH ISNYLTIQQM RYRDILDYEI HIQEEILACD
     ILKMTLQPLV ENALYHGIKN KRGKGRIRID GGYGKSGNIE FHVTDNGAGI PKDKQEQLIA
     MLQQDSHQAQ PQSGGFGIMN VHERIRLYYG EPYGLKLESD QGVGTTVIVS IPVRREYDEK
     SVVGG
//
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