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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//