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Database: UniProt
Entry: A0A0Q9R449_9BACL
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ID   A0A0Q9R449_9BACL        Unreviewed;       586 AA.
AC   A0A0Q9R449;
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_18765 {ECO:0000313|EMBL:KRF09879.1};
OS   Paenibacillus sp. Soil787.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=1736411 {ECO:0000313|EMBL:KRF09879.1, ECO:0000313|Proteomes:UP000051948};
RN   [1] {ECO:0000313|EMBL:KRF09879.1, ECO:0000313|Proteomes:UP000051948}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Soil787 {ECO:0000313|EMBL:KRF09879.1,
RC   ECO:0000313|Proteomes:UP000051948};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KRF09879.1, ECO:0000313|Proteomes:UP000051948}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Soil787 {ECO:0000313|EMBL:KRF09879.1,
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:KRF09879.1}.
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DR   EMBL; LMSP01000048; KRF09879.1; -; Genomic_DNA.
DR   RefSeq; WP_056839351.1; NZ_LMSP01000048.1.
DR   AlphaFoldDB; A0A0Q9R449; -.
DR   STRING; 1736411.ASG93_18765; -.
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; cd18773; PDC1_HK_sensor; 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.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777};
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        20..41
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        300..320
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          320..372
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          482..586
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
SQ   SEQUENCE   586 AA;  67127 MW;  6CE6114850499796 CRC64;
     MKKKLPYSLF HFKSIQLTMA VAFSCLIMFT TLFISFTTYR LSTNAAEKSS REHTAQLIEQ
     VNTNIETYVN YMENISQMVL FNYDIREYLA KGTQDNENLE QRISYQLSSV LNTRKDISSI
     LIFDNDGNII PTKQIKLNKF VDPTQQSWYK KAIEASGKVV ISSSHVQNVI QDEYKWVVSL
     SRELSSEDAK QLGVLLVDLN YSVINDLCNK IKLGKKGYIF ILDQDGNIVY HPQQQLIYSS
     LKTEMIDQVM SSNTNNFTTS EGKNSRMYTI NQSKNTGWKI VGVTYVDELV PNKREIQTYI
     FMWGIGLTLI AVILSIILSL RISRPIKRLE TSMKEIEKGN FDIQVNIESS NEIGQLSKRF
     NRMTTVIKEL MFQNITEQEL KRKSELKALQ AQINPHFLYN TLDSIIWMAE GKKSEEVVQM
     VAALARLFRI SISKGQEMIS IANEIEHIKS YLTIQKIRYK DKLDFEIDVD KQILGYKVFK
     IILQPLVENS IYHGIKNNAG VGIVRITGRI VDERILLQVI DNGIGMSKES IRHMFEKTEK
     SVSGSGIGVS NVNQRIRLYF GDSYGITFES ELGQGTTANI WLPILE
//
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