ID Q89VL4_BRADU Unreviewed; 662 AA.
AC Q89VL4;
DT 01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT 01-JUN-2003, sequence version 1.
DT 27-MAR-2024, entry version 133.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=bll1031 {ECO:0000313|EMBL:BAC46296.1};
OS Bradyrhizobium diazoefficiens (strain JCM 10833 / BCRC 13528 / IAM 13628 /
OS NBRC 14792 / USDA 110).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Bradyrhizobium.
OX NCBI_TaxID=224911 {ECO:0000313|EMBL:BAC46296.1, ECO:0000313|Proteomes:UP000002526};
RN [1] {ECO:0000313|Proteomes:UP000002526}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 10833 / BCRC 13528 / IAM 13628 / NBRC 14792 / USDA 110
RC {ECO:0000313|Proteomes:UP000002526};
RX PubMed=12597275; DOI=10.1093/dnares/9.6.189;
RA Kaneko T., Nakamura Y., Sato S., Minamisawa K., Uchiumi T., Sasamoto S.,
RA Watanabe A., Idesawa K., Iriguchi M., Kawashima K., Kohara M.,
RA Matsumoto M., Shimpo S., Tsuruoka H., Wada T., Yamada M., Tabata S.;
RT "Complete genomic sequence of nitrogen-fixing symbiotic bacterium
RT Bradyrhizobium japonicum USDA110.";
RL DNA Res. 9:189-197(2002).
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; BA000040; BAC46296.1; -; Genomic_DNA.
DR RefSeq; NP_767671.1; NC_004463.1.
DR AlphaFoldDB; Q89VL4; -.
DR STRING; 224911.AAV28_02000; -.
DR EnsemblBacteria; BAC46296; BAC46296; BAC46296.
DR KEGG; bja:bll1031; -.
DR PATRIC; fig|224911.5.peg.1058; -.
DR eggNOG; COG4191; Bacteria.
DR HOGENOM; CLU_000445_114_15_5; -.
DR InParanoid; Q89VL4; -.
DR OrthoDB; 7818322at2; -.
DR PhylomeDB; Q89VL4; -.
DR Proteomes; UP000002526; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004673; F:protein histidine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR CDD; cd06225; HAMP; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 6.10.340.10; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR InterPro; IPR003660; HAMP_dom.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR005467; His_kinase_dom.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR PANTHER; PTHR43065:SF10; PEROXIDE STRESS-ACTIVATED HISTIDINE KINASE MAK3; 1.
DR PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR Pfam; PF00672; HAMP; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00304; HAMP; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF158472; HAMP domain-like; 1.
DR PROSITE; PS50885; HAMP; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777}; Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000002526};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 7..26
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 292..316
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 312..365
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 406..639
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT REGION 642..662
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 363..397
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 645..662
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 662 AA; 72436 MW; 981229B0DA32D094 CRC64;
MPIRWRILSI AALNSAVVVV LVALIWNGSQ VLGSAWDDVR QVRESDRILA LLESETGRLH
NLIHRYINQP SPDLFAEILL LREAVLGTLA NRAAKDPMLS GSVEELERTT DRFLNGFGEL
RSVQATIAKT YEDQVQGPAR DMAGLYSIIE GATGHRDALI WPSLGKSREA FTAMLVAANS
YYLSQSSGAA DDARHNTETI EKTIPVMIDL ADNDLQRMAL QRLATRTVAL REGFAKLSEQ
LMSRTELLRN TIDASQAEAI GAIDDLSTKM RQREQKAQET FDRTLADISR RVLSIAVIFL
GIILTAGVLI ALSIRLPLQQ IMAAMRAITL GDLDREVQGT KARDEVGAMA RAVEVFRENA
IAKRETEDEL RASKEKAESA LLELNTAQQN LIDAERLAAL GGLVAGVAHE VNNPIGISLT
VASSFARRSD IFEAQLKGEG GLRRSQLEEF VQASRDASQQ LVANLQRAGE LIQSFKQVAV
DRSHAERRQF SLSEATDQII ASLRPVLKRS PITLQVDVPE GLLLDGYPGS YGQILTNLFL
NAANHAFADG RAGTITISAR PRGADDIEII FTDDGAGMTP DVQRQAFDPF FTTRRNEGGT
GLGLHIVYNL VTQQLGGRMM LESKLGQGTT FRIIMPRVAK GGAQSTEIDG TSQWPNRTMS
ST
//
