ID A0A1X7FFF3_9PROT Unreviewed; 870 AA.
AC A0A1X7FFF3;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=SAMN02982917_2629 {ECO:0000313|EMBL:SMF50655.1};
OS Azospirillum oryzae.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Azospirillaceae; Azospirillum.
OX NCBI_TaxID=286727 {ECO:0000313|EMBL:SMF50655.1, ECO:0000313|Proteomes:UP000192936};
RN [1] {ECO:0000313|EMBL:SMF50655.1, ECO:0000313|Proteomes:UP000192936}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A2P {ECO:0000313|EMBL:SMF50655.1,
RC ECO:0000313|Proteomes:UP000192936};
RA Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL Submitted (APR-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; FXAK01000005; SMF50655.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1X7FFF3; -.
DR STRING; 286727.SAMN02982917_2629; -.
DR OrthoDB; 7267626at2; -.
DR Proteomes; UP000192936; Unassembled WGS sequence.
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; 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; IPR036097; HisK_dim/P_sf.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013767; PAS_fold.
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; PTHR43047:SF9; HISTIDINE KINASE; 1.
DR PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00989; PAS; 2.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
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; SSF47384; Homodimeric domain of signal transducing histidine kinase; 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; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}.
FT DOMAIN 196..241
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 442..497
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 508..721
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 748..868
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 244..272
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 802
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 870 AA; 93013 MW; 6A54CE3E745262E7 CRC64;
MTEESSGRLR RRAETILSRG NFEAADITAT SMKELLHELY VHQAELEIQN EELRGAQQAL
EASRLQYLQL FQSVPLACLA VNAAGIVGEA NSAAERQFGL PMLRLKGRPL TLLVDSLDHG
RLFTALGRLR DGGEWVRQEF RYLGPQGTII DGLTDARRVT LDDSDRGDVL LTITDLTERN
AWLREVQQAR DDAERARADY HHILQSVGDG ILGVDADGRI RFVNAAATAM TGHLDLDLIG
RPPSDLLAGP APETETGLPG SEGDTAFGGT GQAGGAARAL ALSLTDGRPR RVACERLRRE
DGGTLLVEIS ISPMLASGKR LAPMEERIQG AVVAFRDVTA RRTAEAALNL SERRHRVLVQ
SLHDALAMTA ADGHNLLANA MAERLLDGPA RALLDPTASA YDAADAQPVQ TTAGRRFIDA
NGNRLHGLPP AAEAVRSGKP VVERIIGMVE GGEATAPTRW LRVSSHPVAD QAGRVEAVVS
SVADITAVKA LERDLNVALD ARERFLAAAS HDLRQPVQAL LLLSDLLLKE SLPAGARRMA
EQIQSSLGGL GGMLDGMLDI SKLEAGLVAP NPEPVDIAAL LARLHGEFSA LAEKGGQSLR
LVAPSLSTRT DPGLLERVLR NLLTNALRYA PGGRVLLGAR RRGDRLQIEV WDNGIGIADQ
HIGRIFQDFF QVGNAARDRR EGLGLGLSIA RRLVTMLGGD IDVTSSLGRG SRFTVSLPLT
EQRANGGEHP AVGGSAGGSL TGDGTDRLVM LVEDDAVIRM ALVLMLEDWG YRVMEAGSGA
EAEQLLDSLI DAGEPPDLIL ADYRLPEGTT GLMVMDMVRR RLSRDVPGVL LTGDTSADRL
REAAGAQCAL LHKPIQPARL QDALASALGG
//
