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Database: UniProt
Entry: A0A286ITM3_9BACT
LinkDB: A0A286ITM3_9BACT
Original site: A0A286ITM3_9BACT 
ID   A0A286ITM3_9BACT        Unreviewed;      1418 AA.
AC   A0A286ITM3;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 18.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=SAMN06298216_3612 {ECO:0000313|EMBL:SOE23218.1};
OS   Spirosomataceae bacterium TFI 002.
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Spirosomataceae.
OX   NCBI_TaxID=1945892 {ECO:0000313|EMBL:SOE23218.1, ECO:0000313|Proteomes:UP000217493};
RN   [1] {ECO:0000313|EMBL:SOE23218.1, ECO:0000313|Proteomes:UP000217493}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TFI 002 {ECO:0000313|EMBL:SOE23218.1,
RC   ECO:0000313|Proteomes:UP000217493};
RA   Ehlers B., Leendertz F.H.;
RL   Submitted (SEP-2017) 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};
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DR   EMBL; LT907983; SOE23218.1; -; Genomic_DNA.
DR   OrthoDB; 9806995at2; -.
DR   Proteomes; UP000217493; Chromosome i.
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; 3.
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; 5.
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; PS01124; HTH_ARAC_FAMILY_2; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   4: Predicted;
KW   Kinase {ECO:0000313|EMBL:SOE23218.1}; Membrane {ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW   ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000217493};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Transferase {ECO:0000313|EMBL:SOE23218.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           24..1418
FT                   /note="histidine kinase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5012109073"
FT   TRANSMEM        837..858
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          895..1116
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          1166..1281
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   DOMAIN          1313..1412
FT                   /note="HTH araC/xylS-type"
FT                   /evidence="ECO:0000259|PROSITE:PS01124"
FT   MOD_RES         1214
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   1418 AA;  161564 MW;  1C0162CCC8219F1F CRC64;
     MASIVRKCFL VGILLLQSTS IFSQWRLNAI AGEEGLSHNT VTSIIQDEDG YLWFGTFNGI
     NKYDGYSMKQ YNYSLNAEGL SSNVIFKLFE DKKGYLWAGT TAGLNRINPN TGNIDVYFKG
     DDEPRYTGQN NIQQSKSGIF FINTIKGIKF FEIDGSGNLE YEFFLNKYKG LNLDIQNLTP
     SSNGKYWFLT PSAKVKLHQV EVLKNGKTPK LNIDATDYTE SLFSSGGAIL DILEYPKNTV
     WVINDQFELL KLKLNSDLKV VESEKILLVQ NIGKEQLKEQ GTVNMVADKE GRIWIAGNGL
     LLNYNTELRE SNNLSRNNQL KGLLTNLDIQ EIFVDNSNIL WMGTLNNGLY KMDLDNHTFY
     NSTEYLNSQE SQDLFKSPIH SMCEDERGNL WFGTQDGNIV ALRKNALKNN FSKSPIAYTY
     QVTGKKLDKV FQKPQIKRLM SDREGAIWAG SLNGLFKFKY DETSQSFEVK KIDSIKDNFG
     NIIDKPVFAI EEDRKGNIWF GAWEKGLVKM TFNKQRNSHQ SVIYSASNRD STSLSNNNIR
     DILEDTQGNI WVGTIKGLNK LKRSESGKVT FEKIFSKSEG SNTLSSAHVL DIHQAQNGAI
     YVGTYGGGLN RLNYSSKGNL EFTNYTVKNG LPSDVVYQIR EDFEGNIWLM HTRKISKLNP
     STGEVIYFEK NNGFNVDEFK ENAMEFTSSG TMLCGGVNGF TFFQPNKIIV NNLEPQMTIT
     DFKLLNESVR VNEVFDGRVI LSDGINKTNR IELPYHLNSF EFVFSSMHFS NPESNRYKFI
     LEGFEENART TIGNERRFAS YTNVPPGKYI FKVYGSNSSG IWNNDPKEVL IVITPPWYLT
     PLAILFFIAI CIAILYIINK VRWNQIKLKN DLKLESALHE KAEEINQMKL LFFTNISHEL
     RTPLTLIIGP LQQIMEGHTD PKYLKRLNGI MYKNSTRLLR LINQLLDFRK AESGNVNLIV
     EHGDLVVFLE EIYNAFEEIA IERNVGFTFK TKEKDLGAWF DNDKMEKILY NLLSNSFKFT
     PPNRNIELLL KKETVDGKES AVIQVVDEGI GIASEDLINV FERFYQVKKE SDMIQMGSGL
     GLAFTKRLIE VHRGNISINS STERGTTCTV SIPISKSEYE SDATLEMQTK QHNFSFVKNE
     IKDFKDLLAA PSKRVKEVKH SKETPTLLVV EDNTGLREYI SDYFEDHYKV LSAKDGEEGL
     KVAFEKSPDL IITDLMMPKM GGIEMCKIIK SDINTSHIPV IILTAKSGLE NEKEGLETGA
     DEFVLKPFNM EVLRLRVNNI LQTKQQWTEK FKTEPTSSTW KELSSNLDKE FLKKSLKIIR
     ENIDNSDYSG EDFAIDIGMS RSGLFKKIKS ITGQSTTEFI RTIRIKRAAN LITTCKYSIT
     EVVFMVGFTD PKYFRTCFKK QFGKTPSDYL KAFKESVL
//
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