ID G8QHB7_AZOOP Unreviewed; 736 AA.
AC G8QHB7;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 65.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=Dsui_1887 {ECO:0000313|EMBL:AEV26262.1};
OS Azospira oryzae (strain ATCC BAA-33 / DSM 13638 / PS) (Dechlorosoma
OS suillum).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Rhodocyclales;
OC Rhodocyclaceae; Azospira.
OX NCBI_TaxID=640081 {ECO:0000313|EMBL:AEV26262.1, ECO:0000313|Proteomes:UP000005633};
RN [1] {ECO:0000313|EMBL:AEV26262.1, ECO:0000313|Proteomes:UP000005633}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-33 / DSM 13638 / PS
RC {ECO:0000313|Proteomes:UP000005633};
RX PubMed=22535943; DOI=10.1128/JB.00124-12;
RA Byrne-Bailey K.G., Coates J.D.;
RT "Complete genome sequence of the anaerobic perchlorate-reducing bacterium
RT Azospira suillum strain PS.";
RL J. Bacteriol. 194:2767-2768(2012).
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; CP003153; AEV26262.1; -; Genomic_DNA.
DR RefSeq; WP_014236960.1; NC_016616.1.
DR AlphaFoldDB; G8QHB7; -.
DR STRING; 640081.Dsui_1887; -.
DR KEGG; dsu:Dsui_1887; -.
DR eggNOG; COG2202; Bacteria.
DR eggNOG; COG4191; Bacteria.
DR HOGENOM; CLU_000445_114_39_4; -.
DR Proteomes; UP000005633; Chromosome.
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; cd16943; HATPase_AtoS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 3.
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; 3.
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; IPR013656; PAS_4.
DR InterPro; IPR013767; PAS_fold.
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; PF08448; PAS_4; 1.
DR Pfam; PF13426; PAS_9; 2.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00086; PAC; 3.
DR SMART; SM00091; PAS; 3.
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); 3.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 3.
DR PROSITE; PS50112; PAS; 3.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553}.
FT DOMAIN 29..70
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 87..139
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 140..209
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 213..263
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 264..336
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 355..407
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 480..729
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT COILED 398..471
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 736 AA; 81945 MW; 1E1E740F90361DC7 CRC64;
MPSLPDPGPI PPGLPELLHG EVLLRHLQVS VADDQGAILY VNERMCEACG YRPDELLQHN
YSVLATGRHP PEFFAELWQT VRAGFEWRGE MSNRRKDGSE YWIELTVVPL PAEGNLPRRY
VGLGSDITRI VEAEQQLRSS EARFRGLTET ISAAVILYKG GPMLYVNRAM ERLTGYSRAE
LLQMSFFDLA HPSVRDLLQE RAAARLRGEA MPATYEAPFV TKAGKTIWME ITAARIEYEG
GYAGLGTAID ITERKRAEAA QRSTQQMLQQ IIDGDPVPTF VIDAEHRVTH WNAACALVTG
MPGEKIIGST RAWSGFYAEE RPVLAELVVD GTADSRITGL YGDTFRRSPI IPGAYEVESF
FPNFGDRGRW LFFTAAPLKD AQGRIIGAIE TLVDVTERKE AEEALRNAHT KLEILVERRT
AQLSLAKQAL EEDVRRREAS ENELRQRNAE LLEVNKRLQE AQEQLVQSEK MASIGQLAAG
VAHEINNPIG YVQSNLSTLG RYLEDMQTVL DSLATAVAQL PSEHPAAQAV ARVKQDLDFD
FLLEDLPSLV TQSRDGIDRV RKIVADLKDF SRLDASQDWQ WADLHQGLDS TLNIVNNEIK
YRAEVVREYG QLPEVECLPS QLNQVFLNLL VNSAHAMPEG QMGRITLRSG HDEPAHQVWL
EVEDNGSGIS PENMHRLFDP FFTTKPVGKG TGLGLSLSYG IVQKHHGQIT VSSELGKGTT
FRIVLPVSQP KEGATP
//
