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Database: UniProt
Entry: A0A0Q7FJY7_9FLAO
LinkDB: A0A0Q7FJY7_9FLAO
Original site: A0A0Q7FJY7_9FLAO 
ID   A0A0Q7FJY7_9FLAO        Unreviewed;       490 AA.
AC   A0A0Q7FJY7;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=ASC72_17080 {ECO:0000313|EMBL:KQW96174.1};
OS   Flavobacterium sp. Root420.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Flavobacterium.
OX   NCBI_TaxID=1736533 {ECO:0000313|EMBL:KQW96174.1, ECO:0000313|Proteomes:UP000051729};
RN   [1] {ECO:0000313|EMBL:KQW96174.1, ECO:0000313|Proteomes:UP000051729}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root420 {ECO:0000313|EMBL:KQW96174.1,
RC   ECO:0000313|Proteomes:UP000051729};
RX   PubMed=26633631; DOI=.1038/nature16192;
RA   Bai Y., Muller D.B., Srinivas G., Garrido-Oter R., Potthoff E., Rott M.,
RA   Dombrowski N., Munch P.C., Spaepen S., Remus-Emsermann M., Huttel B.,
RA   McHardy A.C., Vorholt J.A., Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiota.";
RL   Nature 528:364-369(2015).
RN   [2] {ECO:0000313|Proteomes:UP000051729}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root420 {ECO:0000313|Proteomes:UP000051729};
RA   Garrido-Oter R., Bai Y.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|Proteomes:UP000051729}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root420 {ECO:0000313|Proteomes:UP000051729};
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   -!- 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:KQW96174.1}.
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DR   EMBL; LMEF01000034; KQW96174.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0Q7FJY7; -.
DR   STRING; 1736533.ASC72_17080; -.
DR   Proteomes; UP000051729; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   CDD; cd00075; HATPase; 1.
DR   CDD; cd00082; HisKA; 1.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 6.10.340.10; -; 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; IPR003661; HisK_dim/P.
DR   InterPro; IPR036097; HisK_dim/P_sf.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   PANTHER; PTHR43065:SF10; PEROXIDE STRESS-ACTIVATED HISTIDINE KINASE MAK3; 1.
DR   PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
PE   4: Predicted;
KW   Kinase {ECO:0000313|EMBL:KQW96174.1}; Membrane {ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Transferase {ECO:0000313|EMBL:KQW96174.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        193..212
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          280..489
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
SQ   SEQUENCE   490 AA;  55944 MW;  671B9C38A0A71208 CRC64;
     MFNNFKMSML SLRVRIFLSM IVLIVVASFL LASISIIQFK NEAKEYHQER LERKENAVKE
     HINYVLSTTT YPLKTANLDL IFKDKIHELA QIHKIEINIY SLDGKLLKSS KESFAVDKVA
     PPVPDYILKL VRSSIEKRFV DIKTIDGVKN RSSYSLIKDE KFKPLGILNL PYLEDDGYYD
     NELNTFLIRL SQVYSFMLIV AFALAYFLST YITKSLKTIS DKLEETNLDQ KNEKIVLEAN
     SKEVNFLIRA YNGMVDKLET SAIKLAQSER EEAWREMAKQ VAHEIKNPLT PMRLTVQSFQ
     RKFDPTAPDV KQKLNDYSET LIQQIDTMTA VASAFSNFAS MPAQQNETLN VVEVVELALD
     IFNEDYIVFE SEEEEIVSKM DRTQLIRVIT NLVKNATQAI PESQFHKSIL VTVKRRNNNV
     EIAVKDNGIG IQKQDADRIF EPKFTTKTSG MGLGLGIIKN IIENYKGTIT FESTFGKGTT
     FTVSLPITNS
//
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