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Database: UniProt
Entry: A0A1X7EFI3_9PROT
LinkDB: A0A1X7EFI3_9PROT
Original site: A0A1X7EFI3_9PROT 
ID   A0A1X7EFI3_9PROT        Unreviewed;       592 AA.
AC   A0A1X7EFI3;
DT   05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2017, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=SAMN02982917_1630 {ECO:0000313|EMBL:SMF33041.1};
OS   Azospirillum oryzae.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Azospirillaceae; Azospirillum.
OX   NCBI_TaxID=286727 {ECO:0000313|EMBL:SMF33041.1, ECO:0000313|Proteomes:UP000192936};
RN   [1] {ECO:0000313|EMBL:SMF33041.1, ECO:0000313|Proteomes:UP000192936}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A2P {ECO:0000313|EMBL:SMF33041.1,
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; FXAK01000002; SMF33041.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1X7EFI3; -.
DR   STRING; 286727.SAMN02982917_1630; -.
DR   OrthoDB; 7325042at2; -.
DR   Proteomes; UP000192936; 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   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   Gene3D; 3.30.450.20; PAS domain; 2.
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; IPR013767; PAS_fold.
DR   InterPro; IPR013655; PAS_fold_3.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
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   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00086; PAC; 2.
DR   SMART; SM00091; PAS; 2.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR   SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 2.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50113; PAC; 2.
DR   PROSITE; PS50112; PAS; 2.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553}.
FT   DOMAIN          57..128
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          132..184
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          185..245
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          256..306
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          340..578
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   COILED          297..331
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   592 AA;  64564 MW;  61964D7F88D577E0 CRC64;
     MAAEPVMMAL AAGAAGGLLG VLLGRYAGRR TAARPPGIGS GTGSGKVAAP LLHEPEIGER
     LEMALEATGA AVWDADLVAG TCWWSDTFPR MLGFRSRPAM PPDFWERRLH PEDRDRVLAH
     IASHLAGETS AYAYSYRLRH EAGGWVWIAA KGRAFRDKSG RAVRYAGIMT DITEARRQEE
     RLRASEERLL KIMEAAPIAV NVTTRDGRWL FCNAQSARLM GRGRSELMRS PVADLYADPA
     DREALIARFD REGAFRNAEI RFRRPDGSIV WVLSSWNSIE LDGESALLTW LYDITDRKVA
     ESAMNQAREE AEQALADLRE AQESLIQAET MASLGQLVAG VAHEINTPIG IGLTAASHIG
     EQAQALRERF AGNTLRRSDF LEFLDGLSES SRLLMANMDR AASLVQSFKQ VAVDQSSGDR
     RVFELGSYIR ELLFSLRPRL KRTNLKVAVE CDDELTMDSF PGALGQVLTN LVINAVVHAY
     GDGERLSETP SGTIRITAQP DGSDKVRIDF IDDGAGIAPE HLSKVFDPFF TTKRGQGGSG
     LGLHIVFNTV TGPLGGTVSV QSWPGQGTRF TILLPREAPA MQPALAEEPA LG
//
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