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Database: UniProt
Entry: A0A0Q7FVI0_9FLAO
LinkDB: A0A0Q7FVI0_9FLAO
Original site: A0A0Q7FVI0_9FLAO 
ID   A0A0Q7FVI0_9FLAO        Unreviewed;      1364 AA.
AC   A0A0Q7FVI0;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 44.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=ASC72_10855 {ECO:0000313|EMBL:KQW99550.1};
OS   Flavobacterium sp. Root420.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Flavobacterium.
OX   NCBI_TaxID=1736533 {ECO:0000313|EMBL:KQW99550.1, ECO:0000313|Proteomes:UP000051729};
RN   [1] {ECO:0000313|EMBL:KQW99550.1, ECO:0000313|Proteomes:UP000051729}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root420 {ECO:0000313|EMBL:KQW99550.1,
RC   ECO:0000313|Proteomes:UP000051729};
RX   PubMed=26633631; DOI=10.1038/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:KQW99550.1}.
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DR   EMBL; LMEF01000029; KQW99550.1; -; Genomic_DNA.
DR   RefSeq; WP_056193133.1; NZ_LMEF01000029.1.
DR   STRING; 1736533.ASC72_10855; -.
DR   OrthoDB; 1522078at2; -.
DR   Proteomes; UP000051729; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR   CDD; cd00082; HisKA; 1.
DR   CDD; cd17574; REC_OmpR; 1.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 3.40.50.2300; -; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   Gene3D; 1.10.10.60; Homeodomain-like; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR   Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 2.
DR   InterPro; IPR011006; CheY-like_superfamily.
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; IPR009057; Homeobox-like_sf.
DR   InterPro; IPR018060; HTH_AraC.
DR   InterPro; IPR018062; HTH_AraC-typ_CS.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR011110; Reg_prop.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   InterPro; IPR011123; Y_Y_Y.
DR   PANTHER; PTHR43547:SF2; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE C; 1.
DR   PANTHER; PTHR43547; TWO-COMPONENT HISTIDINE KINASE; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF12833; HTH_18; 1.
DR   Pfam; PF07494; Reg_prop; 7.
DR   Pfam; PF00072; Response_reg; 1.
DR   Pfam; PF07495; Y_Y_Y; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SMART; SM00342; HTH_ARAC; 1.
DR   SMART; SM00448; REC; 1.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF63829; Calcium-dependent phosphotriesterase; 3.
DR   SUPFAM; SSF52172; CheY-like; 1.
DR   SUPFAM; SSF46689; Homeodomain-like; 1.
DR   SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS00041; HTH_ARAC_FAMILY_1; 1.
DR   PROSITE; PS01124; HTH_ARAC_FAMILY_2; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   4: Predicted;
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   Kinase {ECO:0000313|EMBL:KQW99550.1}; Membrane {ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW   ProRule:PRU00169}; Transferase {ECO:0000313|EMBL:KQW99550.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        789..809
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          843..1063
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          1110..1225
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   DOMAIN          1257..1356
FT                   /note="HTH araC/xylS-type"
FT                   /evidence="ECO:0000259|PROSITE:PS01124"
FT   MOD_RES         1158
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   1364 AA;  155069 MW;  D83CC8C8F1CCE32C CRC64;
     MKYKIAFLVL VFISGNIFSQ NKYRLKNIST TDGLSQSSVI AIHQDRFGQM WFGTRDGLNK
     YDGSHFTIFR NDVANKLSIS NNDILAIEED NSGKIWVGTY NGLNCYNPVT NTFTRYLHTK
     NNHTISGNAI WSIREIGDEM WFGTSKGLTI YNKKTGQFTS TFHSDTDNTT LPSNNILSIL
     KTKKGQIWIG TTKGLCVLTS RKNRKFSFKN YPLNASDLLT VQALAEDRDN NIWVGTKNKG
     LLKFSPATNK YVSFLSAEKL RELNTDIRAL TIDNEGSLWI GAYDGIYILG QDKSIEKINN
     SNNNNGIDKV KSVFLDKKGS VWIGCYYKGV NIWDVSNVNF SNYNQNSKKI PMSFDVVSSI
     ISDKNKNIYF GTEGGGITIY NSNTGSTNYI NSKSGQTTKN DIKSMCLAED NILWMGTFSK
     GISAYNTISK RIEDNRISSE LNGLLKDTGV YSIKTEANGI LWIGTFSKGL IRYNTISKTF
     QIIGNDNTKP NYLTNNIVRT ILVDRQKRLW VGTQNGLNLM ALSNFQPNKY AIKHFFFDAA
     ALAGDDILTL FQDSQNKIWV GTKAKGLHYF DGKKFNRINL KIGNTVITSI HSILEDNDKN
     LWISTNQGII KYSTTRKTVV IYDQKDGLAS NEFNDNSALK LGDNKFYFGS PSGVTYFDAR
     KISLNQFVPQ VLITDLKIKN ETINPQDSTQ ILEKSIGYTK NITLDYDKAN FSINFAIPNY
     IRSKNNQYSY RLTGLENTWT ITKNTEAIYA IQNPGTYVFE VRGANNDGVW NKVPTTLTVV
     VNPAPWRSIW AFLLYGIIIG SALYGLIWIM KSKARLKQKL ELEYLETKRI EENNRAKLDF
     FTNISHEFRT PLTLILGPLQ QILSNYNGTN EMYKKLLVIE GSANHLLSLI NRLMDFRKLE
     NDQVKLESAN GNIVKFTKEI FLSFIEYAKD GGYYYTFEAA EEEILVYYDR YKLERVFYNL
     ISNAFRYTPK GGTINIKIDH DHENLFIAVE DSGAGIAEEH IDKIFDLFFE VPLHNNVQKN
     YNKGTGIGLS IVKNIVKLHK GNIDVTNKET GGVVFKVTLP LGRAHLSDDE IIQDFKISDD
     IVQYTNQLET AEVTEPEDIE DFVVSAEKQT ILLVEDHKVL RTFMKNLLKK EYNIIEAENG
     KIAFEKAVQF VPNLIISDVI MPEMVGTELC SKIKSNLKTS HIPVILLTSR SSLVYKFEGL
     ESGADDYISK PFNLMEFKLR VKNLLNSTER LKNKFASEDN FVPSEITVSS LDEELLKKAF
     KIVEENISNE QFDIPFFCSE LGVSRTMLFL KIKAWTNYTP NEFIHEIRLK RAAQLLEQNK
     LNVSEVSYKV GFNNPKYFSK CFQKKYGETP SQFADKFSKP MSVI
//
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