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Database: UniProt
Entry: A0A2T6DTQ6_9BACT
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ID   A0A2T6DTQ6_9BACT        Unreviewed;       895 AA.
AC   A0A2T6DTQ6;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=DB347_15840 {ECO:0000313|EMBL:PTY05822.1};
OS   Opitutaceae bacterium EW11.
OC   Bacteria; Verrucomicrobiota; Opitutae; Opitutales; Opitutaceae.
OX   NCBI_TaxID=2161865 {ECO:0000313|EMBL:PTY05822.1, ECO:0000313|Proteomes:UP000244239};
RN   [1] {ECO:0000313|EMBL:PTY05822.1, ECO:0000313|Proteomes:UP000244239}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EW11 {ECO:0000313|EMBL:PTY05822.1,
RC   ECO:0000313|Proteomes:UP000244239};
RA   Buenger W., Mueller J., Hurek T., Reinhold-Hurek B.;
RT   "Genomic and phenotypic characterization of four novel plant-associated
RT   Verrucomicrobia indicate a new subdivision with one cultivated member.";
RL   Submitted (MAR-2018) 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:PTY05822.1}.
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DR   EMBL; QAYY01000011; PTY05822.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2T6DTQ6; -.
DR   OrthoDB; 9784397at2; -.
DR   Proteomes; UP000244239; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR   CDD; cd00082; HisKA; 1.
DR   CDD; cd00130; PAS; 2.
DR   CDD; cd00156; REC; 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; 3.30.450.20; PAS domain; 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; IPR001610; PAC.
DR   InterPro; IPR000014; PAS.
DR   InterPro; IPR000700; PAS-assoc_C.
DR   InterPro; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR013767; PAS_fold.
DR   InterPro; IPR013655; PAS_fold_3.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR   NCBIfam; TIGR00229; sensory_box; 2.
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; PF00989; PAS; 1.
DR   Pfam; PF08447; PAS_3; 1.
DR   Pfam; PF00072; Response_reg; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00086; PAC; 2.
DR   SMART; SM00091; PAS; 3.
DR   SMART; SM00448; REC; 1.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF52172; CheY-like; 1.
DR   SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 3.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50113; PAC; 1.
DR   PROSITE; PS50112; PAS; 2.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   4: Predicted;
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW   ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000244239}.
FT   DOMAIN          164..196
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          215..267
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          397..470
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          541..754
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          774..894
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..20
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         828
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   895 AA;  97146 MW;  88F9ACEBDB946F8C CRC64;
     MMQYVKQTPS RSSASVPASG QPSGAPVLLT LDAEGHVVDV SRSAEVYWTP AKSLIGVPVV
     SLFSFGPESV HSGPSAAQWE LLRATAVGRP FSCSIRTNPP AIAPKVVVRL EESGLDDARY
     FAQIESAETP ASNVSPMVVD SGLALLSNEG PVGFFDLNFK AGQVYYSPAW KRMLGYNDTE
     LANTYDSWLR LLHPEDSAAA PDHTGKRAPR SARSFAVEVR MLHRHGNYIW VHCLGTQVYG
     SMGELERVTG LQIDITERKE LEEQTLANEE RMQRLVESGD VGLFDLNFAS QQYWFSPHWR
     KLIGSTALEG AQALKDFVEA LPSGRAMRGA ESFFVEPNVG HPSFITELRL IHADGSSVSV
     LFGAHRQLSR KGELVRAVGF ACALPDALPK SAALPFGPAL LQTTLDSLGE GIVVADAQGI
     VTHLNARAER LIGLERRDAR GRNLEQVFRL VYRDSRSVVE DPFETALSNS EEGRLFSDHA
     LVSVADASLR NIVWSARRVA DAGAELGGIV IIFRDPEEMS LSPDELLKIN RFENLGIVAG
     GISHDFNNLL TTILGGISQA KDSKDYSYLA DSERACLAAK ALTKQLLAVA RGGKSEVVQT
     IPVQEVVRDA VRLARAGTNA EFRIEIPDSI HPIQVDRAQI LQVFQNLIIN SLQALPPRGG
     SLWLSGVNVA LEEGNASGLS AGSYVRIEVR DNGCGIAPEN LELIFEPFFT TKKSGTGLGL
     SMVRSIVRKF GGDVSVTSTL GAGTTFQVLL PRAATAADAA NKRVAPSLRF GTGRVLLMDD
     DPDICHLAEG MLASLDYKYD IARNGEEAIT LYRRHLNIGR PYDAVILDLT IVGGAGGEET
     FHKLREMDKD VRAIVCSGYD SEDMIRHYTD MGFSGYLSKP FRAADLGKTL KSVIG
//
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