ID A0A2T6CRA5_9BACT Unreviewed; 1056 AA.
AC A0A2T6CRA5;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=DB354_15450 {ECO:0000313|EMBL:PTX92714.1};
OS Opitutus sp. ER46.
OC Bacteria; Verrucomicrobiota; Opitutae; Opitutales; Opitutaceae; Opitutus.
OX NCBI_TaxID=2161864 {ECO:0000313|EMBL:PTX92714.1, ECO:0000313|Proteomes:UP000244023};
RN [1] {ECO:0000313|EMBL:PTX92714.1, ECO:0000313|Proteomes:UP000244023}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ER46 {ECO:0000313|EMBL:PTX92714.1,
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:PTX92714.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; QAYX01000023; PTX92714.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T6CRA5; -.
DR InParanoid; A0A2T6CRA5; -.
DR OrthoDB; 184236at2; -.
DR Proteomes; UP000244023; Unassembled WGS sequence.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 5.
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; 5.
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; IPR001610; PAC.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR NCBIfam; TIGR00229; sensory_box; 5.
DR PANTHER; PTHR43304:SF1; PAC DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR43304; PHYTOCHROME-LIKE PROTEIN CPH1; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF13188; PAS_8; 1.
DR Pfam; PF13426; PAS_9; 4.
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; 5.
DR SMART; SM00091; PAS; 5.
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; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 5.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 4.
DR PROSITE; PS50112; PAS; 5.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000244023}.
FT DOMAIN 30..146
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 164..237
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 239..291
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 292..362
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 426..470
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 504..554
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 555..626
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 633..683
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 684..740
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 759..811
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 840..1054
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT COILED 795..822
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 81
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1056 AA; 118395 MW; 7A822E661FE9C8B1 CRC64;
MSLIPPYTGP RRVNSTAKAA PLTYVKKELR ILVLEDVPAD VTLIDHELRQ AGIPFQVKRV
ETREEFTREL ETAPPDIILS DHGLPTFDGF AALSLARHRC PDVPFIFVTG SMGEELAIES
LRGGATDYVL KSHLTNLVPA VERALRLADE RGRRRAAEKD LRASEERFRL LVSGVKDYAI
CMLDPEGRVS SWNAGAEQVL GYHAGEVLGQ PLDRFYRPAE REAGKPAADL KTAAAEGAFR
EENWRLRKGD AAFWAHVDLR ALRDESGRLR GFTQVIRDVT ERRRADEALR RSEERYRRLV
ELSPDAIMVL REGQIAFANP AARRLLGAQE PEQLLGRDLL AFLPRESRPP LASRLQELGA
RESRAPWSEP TQPPTFDEHT LVRLDGTEIT VELGVSRMTF QDEPALQLIV HDLTLQRHAA
AALRESEARK AAILETSLEA IVGLDHRGVV REWNAAAERI FGYRREQALG TRLETLIVPV
PARQRPLPGL ADLLSGAAAN VLGRPLEALA RRASGEEFPI ELALTQITVT DPPFYTAFMR
DITDRKQAEE ALRRSEARKS AILESALDAI VTIDAQAKII EWNPAAGETF GYSRELALGR
SFSDLMAPSA NDELARKGLA RYLQTGRGRL LGQRMELMAL RANGAEFPVE LTLTHIVTGE
QRVFTSFIRD ITERRRTEEA LRKSEERFRL LVEGVEDYAI YMLDTHGRVT TWNAGAERIH
GYRAQEIIGR RFHRFYAEED VDRKKPDQAL AVATSEGRYQ DEHALLRQTG APFWASLVIT
ALRDEQGRLT GYSSIARDVT RRKEAEDEIR RLNAALQHQV QERTAELQAA YGEMEAFSYS
ISHDLRAPLI HIAGFVEMLK SDLGPQLDAR SRRHLETICS STEHMGHMIA ELIALSRIGR
AEMHKVRLQI SELVSDVQRE LAAQLQNRTV VWTVGSLPEV LGDPILLRQA IHHLMSNALK
FTRPRAEARI EIGSRPGEVE DIIFVRDNGV GFDLKYAAKL FGVFQRLHPQ AEFEGAGMGL
AKTRRIIQRH GGRIWAESAP TVGTTVFFAL PRAPGA
//