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Database: UniProt
Entry: A0A0C1F3V7_9FLAO
LinkDB: A0A0C1F3V7_9FLAO
Original site: A0A0C1F3V7_9FLAO 
ID   A0A0C1F3V7_9FLAO        Unreviewed;      1315 AA.
AC   A0A0C1F3V7;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   24-JAN-2024, entry version 46.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=OA85_06000 {ECO:0000313|EMBL:KIA87827.1};
OS   Flavobacterium sp. AED.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Flavobacterium.
OX   NCBI_TaxID=1423323 {ECO:0000313|EMBL:KIA87827.1, ECO:0000313|Proteomes:UP000031403};
RN   [1] {ECO:0000313|EMBL:KIA87827.1, ECO:0000313|Proteomes:UP000031403}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AED {ECO:0000313|EMBL:KIA87827.1,
RC   ECO:0000313|Proteomes:UP000031403};
RA   Gale A.N., Newman J.D.;
RT   "Flavobacterium sp. AED Genome.";
RL   Submitted (OCT-2014) 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:KIA87827.1}.
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DR   EMBL; JSYM01000001; KIA87827.1; -; Genomic_DNA.
DR   RefSeq; WP_039109405.1; NZ_JSYM01000001.1.
DR   STRING; 1423323.OA85_06000; -.
DR   OrthoDB; 1522078at2; -.
DR   Proteomes; UP000031403; 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; 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; 4.
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; 2.
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; PS01124; HTH_ARAC_FAMILY_2; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   4: Predicted;
KW   Kinase {ECO:0000313|EMBL:KIA87827.1}; Membrane {ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW   ProRule:PRU00169}; Signal {ECO:0000256|SAM:SignalP};
KW   Transferase {ECO:0000313|EMBL:KIA87827.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..1315
FT                   /note="histidine kinase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002132087"
FT   TRANSMEM        764..786
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          822..1035
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          1067..1182
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   DOMAIN          1214..1313
FT                   /note="HTH araC/xylS-type"
FT                   /evidence="ECO:0000259|PROSITE:PS01124"
FT   MOD_RES         1115
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   1315 AA;  152254 MW;  BCFBB32BF1C99DFC CRC64;
     MRKFLFFCIF LILTIDSLQA QEYYFKHYQV EEGLSNNTVL SSLQDEDGFM WFGTKDGLNR
     FDGYRFKTYR SNSDPIHSLG SNYIQSLHEY KGIIWVGTDK GLYKYDKKLD RFSILNEAIN
     DRIAAIEHDN HGNIWFISGN ILYKYSTVKN ETTTFNPNKY FIATSITRDA KGEIWVSSLN
     KLYHYSEESL SFETVPLNYN NPSYRITVIY ALDKNNILIG TQDHGVLSYN RINKSTSSLP
     FATKDPLFVR QFKKNGKNEI WIASESGVYI YNIQTKKYIN LKKDFNDPFS ISDNAAYSIT
     IDKENGVWIG TYFGGINYHQ KQYTQFKKYF PKNNQNSISG SAVREIHKDD NGDFWIGTED
     AGLNKFNPKT QVFTSYKPNG SPGSVSYYNI HALLPRKENI WIGTFEHGLD VLDRKSGKVI
     KHYNAGTEAG ALKSNFIFSF YKTRNKDLLV QTSVGIYKYN SINDNFDVLK NFPENMHYTS
     FMEDNDGNYW AGTYRDGLLF YNSKNKKKEI FRYNYKDAKG ISNNSINSIF EDSKKNLWIA
     TENGLNLFDK KTRTFTKFNT KKGFPSNVFY SILEDDKQNL WITTSKGLVQ FNPENNSIKI
     YTTANGLLSD QFNYNSAYKD TNGDMYFGNL NGMISFNPKH FSKNKFAPKI FITSLQINNQ
     EVQTNDKDSP IKKSISHVDE LELNHNQSSF NIEFAALNYT GAELTEYWYK LEDVNKDWVY
     LERNNKVFFT ELSPGSYIFK VKSRNSFGVW SKEIAVKIKI LPPFWASTYA YLLYFMLICY
     GLFMIIRYSN NLSQEKNDRK IKHLNDEKEK EIYQAKIEFF TNVAHEIKTP LTLIKSPLEK
     LLKFEYQTPE IPQNLSIMKK NTSRLLKLVN ELLDFRKTEI GGLKLTFVEV NISALVRNMH
     LRFSQLIEEK NIDFELELSD KDIYAFVDKE ALKKILSNLF NNAIKYSEKK VIVSLIRDEK
     KLELIVKNDG KLIPSNLKDK IFEPFFRVDN MDTNSGTGIG LSLAHSLTQL HHGSLQLIFS
     EPKMNVFEFI VPLHQEEEFM LYDEQTKETN NNENEIIEPE IKSEKTTILV VEDNEDLLNF
     ITNELLSSYA VLKANNGETA LKIIHNENIA LVISDIEMPI MDGITLCKKI KTNLETSHIP
     VILLTAKNSL KSQIDGLEVG ADSYVAKPFS MEYLKVQSSN LIENRKQIMN YYASSPLSHI
     KSMAHNKTDE NFLKKLDEEI IKNIADQNLS VESLSEIMNM SRSTLYRKIK DISNMSPNEL
     INLVRLKKAA ELLLNKDYKM YEIAEIVGYK SQTSFGRNFH KHFKMSPSDY ISMNK
//
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