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Database: UniProt
Entry: A0A2T6D2I3_9BACT
LinkDB: A0A2T6D2I3_9BACT
Original site: A0A2T6D2I3_9BACT 
ID   A0A2T6D2I3_9BACT        Unreviewed;      1496 AA.
AC   A0A2T6D2I3;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=DB354_08255 {ECO:0000313|EMBL:PTX96640.1};
OS   Opitutus sp. ER46.
OC   Bacteria; Verrucomicrobiota; Opitutae; Opitutales; Opitutaceae; Opitutus.
OX   NCBI_TaxID=2161864 {ECO:0000313|EMBL:PTX96640.1, ECO:0000313|Proteomes:UP000244023};
RN   [1] {ECO:0000313|EMBL:PTX96640.1, ECO:0000313|Proteomes:UP000244023}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ER46 {ECO:0000313|EMBL:PTX96640.1,
RC   ECO:0000313|Proteomes:UP000244023};
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:PTX96640.1}.
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DR   EMBL; QAYX01000020; PTX96640.1; -; Genomic_DNA.
DR   InParanoid; A0A2T6D2I3; -.
DR   Proteomes; UP000244023; 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; cd00082; HisKA; 1.
DR   CDD; cd00130; PAS; 2.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 2.10.70.100; -; 1.
DR   Gene3D; 3.40.50.2300; -; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR   Gene3D; 3.30.450.20; PAS domain; 2.
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; IPR013783; Ig-like_fold.
DR   InterPro; IPR001610; PAC.
DR   InterPro; IPR000014; PAS.
DR   InterPro; IPR000700; PAS-assoc_C.
DR   InterPro; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR013655; PAS_fold_3.
DR   InterPro; IPR011041; Quinoprot_gluc/sorb_DH.
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   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; PF00512; HisKA; 1.
DR   Pfam; PF08447; PAS_3; 2.
DR   Pfam; PF00072; Response_reg; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SMART; SM00086; PAC; 2.
DR   SMART; SM00091; PAS; 2.
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; 1.
DR   SUPFAM; SSF52172; CheY-like; 1.
DR   SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR   SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 2.
DR   SUPFAM; SSF50952; Soluble quinoprotein glucose dehydrogenase; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50113; PAC; 2.
DR   PROSITE; PS50112; PAS; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   4: Predicted;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW   ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000244023};
KW   Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..28
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           29..1496
FT                   /note="histidine kinase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5015775015"
FT   TRANSMEM        812..834
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          938..990
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          991..1058
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          1067..1119
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          1132..1355
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          1376..1493
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   MOD_RES         1427
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   1496 AA;  166494 MW;  C688C8020FF7A8AD CRC64;
     MWVKARWRNL MWILALFLRV LLTPSAIAAE PYQPLTVDPL SEPWRWRVFP QLAGMGVLCM
     TEAADGTLWF GTADGLWHFD GVRWQADDGS TQLPGGVLAL HTTGDGRIFA AGRWGISEYR
     DGTWSRRYEL AAERDTEVRR LVSLPDGTVW AASSYGAVEL RRTTCTLHTT AERAAQLRAA
     HFNPAPAFSI QEWPAAVQEP ILPGNPPALA RHDLFEACRD AMGRLWFGTS GGELLRLTPA
     ATPTSPPVWE LYNEKDGLVR GLRPYILGLK NGEVWVTYET RSAHLNQFDG TRWRATPLAT
     LGLPEVCVNP LQTRDGAVWL SARYVVSAFR EGRWRTYERP AVPIPRARNI LCATRDGALW
     IAGPNTEILR IDYSTHRWRT LDELMFQGED SAGREWFIHQ RGRIVCHDGD TWTSYGAEDG
     GISVPVALIV TRAGDVWVAG SHENEAATAR FDGRRWTRTV HANFSWGIDG QAIWEGFDGA
     LWFGAAVDTN GPARHRAGIL EYRDGRWIHH HQPGRVFPGE ADDDARTLLP ATQSPQPIGK
     FSRIAGSPDG RVWAGRTILA AYDGKRWQRV SPAVGVSIDS VDTLFTSEER DLWLGTRRYG
     AIRYDGRNWW RYQGSGSLEA NSVRDFAQTA DGTIWAATDR GYSRFDGQTW TSVLPGALTL
     PDAGGSLRAG RENRIWINHY PPEWLRRGWP RVKPGAHAQA EAFRAYSHVP TGTPPDTVLR
     PGPKVIGYPG HISVLWDGTA PWATGDDSRL EYSYRLDGGP WSAYTADRGT TLFSLGAGEH
     LFEVRARDRS FNVDPTPAKL RLKVQPPVWR QAWFVVLLAA LVATAAVLLI RVLLERARLR
     RTNRVLAEEI KSRERTEAAL RTSQAELKDA QHLSRLGTWH MSLATQQLEW SEEVVRTFEL
     DASARGAPYD RVLARVHPDD RERVHRAFRR AIYDRLMFDI EFRVGVPDGR TKYVRAIGRI
     LAGANGQSAS VSGSLQDITD RKESELQLRE SEERFRQLAE TITDAFWVAA TTPEPKVLYV
     SPAFESIWGR RCSELIQDPG MWLASVHADD RERVSRTMAA RAAGVGYDEE YRILRPDGAV
     SWVRDRAFPV QGAGGKVERM VGVARDVTSR RQMEAQLRQS QKMEAVGQLA GGVAHDFNNI
     LSVIVMQVEL AHSDPALPTE LQECLQEIRA AALRAANLTR QLLLFSRRQE LQSRPVDLNE
     VVGNLGKMLR RLIGEDIHLE IALHPSPLRT VADPGMLDQV VMNLVINSRD AMPAGGRLQI
     TTAPREIDAQ AAARLRTVEP GSYVALTVTD SGAGIPPDVL PHVFEPFFTT KEAGKGTGLG
     LATVFGIVKQ HRGGISVSSQ VGEGTRVEIF LPVITPTENA PDGNESSPAV SGGSETILLV
     EDEPSMRLAV RGFLERHGYH VIEAESGARG RAQWEQNRGK IRLLLTDIVM PGRISGRQLA
     RELRAEDPAL KVIYASGYAP EQKGEPLELE KADRFLPKPF APEQLLRLIR SLLDAR
//
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