ID Q89RB0_BRADU Unreviewed; 860 AA.
AC Q89RB0;
DT 01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT 01-JUN-2003, sequence version 1.
DT 27-MAR-2024, entry version 138.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=blr2862 {ECO:0000313|EMBL:BAC48127.1};
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:BAC48127.1, 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};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; BA000040; BAC48127.1; -; Genomic_DNA.
DR RefSeq; NP_769502.1; NC_004463.1.
DR RefSeq; WP_011085646.1; NZ_CP011360.1.
DR AlphaFoldDB; Q89RB0; -.
DR STRING; 224911.AAV28_11325; -.
DR EnsemblBacteria; BAC48127; BAC48127; BAC48127.
DR GeneID; 64022614; -.
DR KEGG; bja:blr2862; -.
DR PATRIC; fig|224911.44.peg.2486; -.
DR eggNOG; COG2203; Bacteria.
DR eggNOG; COG4191; Bacteria.
DR eggNOG; COG5002; Bacteria.
DR HOGENOM; CLU_017430_0_0_5; -.
DR InParanoid; Q89RB0; -.
DR OrthoDB; 1931120at2; -.
DR PhylomeDB; Q89RB0; -.
DR Proteomes; UP000002526; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd06225; HAMP; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd12912; PDC2_MCP_like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.450.40; -; 1.
DR Gene3D; 6.10.340.10; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 1.
DR InterPro; IPR033479; dCache_1.
DR InterPro; IPR003018; GAF.
DR InterPro; IPR029016; GAF-like_dom_sf.
DR InterPro; IPR003660; HAMP_dom.
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; 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; PF02743; dCache_1; 1.
DR Pfam; PF01590; GAF; 1.
DR Pfam; PF00672; HAMP; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00065; GAF; 1.
DR SMART; SM00304; HAMP; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF55781; GAF domain-like; 1.
DR SUPFAM; SSF158472; HAMP domain-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50885; HAMP; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 4: Predicted;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, 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|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 41..65
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 314..333
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 334..386
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 606..850
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT COILED 371..405
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 860 AA; 93592 MW; D037D9CA31AC69AB CRC64;
MSLSLHPDAP QARTLPSAAP DGAVAGEAVG RGIRTRLFTK YVALFVAVVA VALLANGLFE
VFFYYREHKA SLIRVQHEQA EAAAAKIGQF VKEIESQLGW TTQLPWSAGS IEQRRFDALR
LLRQVPGITE LAQVDSSGKE RLRVSRLAMD AIDSGIDLSG DPKFTEAVAH KVYYGPVYFR
RDSEPYMTLA LAGARKEAGV SIAEVNLKLI WDVVSQIKVG EHGNAYVVGP EGRLIAHPDI
SLVLRNTDMS GLAQVRAAQS GGGTMSDPLP EARNIQGRKV LTASAPIEPL HWTMFVELPV
EEAYAALYAS LQRLAIVLLA ASIFAVLAGI FLARRMVGPI QALRSGAERI GGGDFSQRIA
IRTGDELEGL ADQFNEMGAR LQESYADLEN KVEQRTAELS ESLQQQTATA DVLKVISRSA
FDLQTVLNTL VGSAARLCDA DEGTIFRPSD GVFYLAASCG LDAEQENKLR TFASVPERGS
VVGRTLLDAK TVHVPDVQAD PEYAPSSARR RSNVRTMLGV PLLREGTPIG VFVLTRHMVR
PFSDKQIELA TTFADQALIA IENVRLFEEV QERTRELSRS LDDLRAAQDR LIQTEKLASL
GQLTAGIAHE IKNPLNFVNN FSSVSTELID ELNEVLEAAK LDGKTKAEVD ELTAMLRGNL
EKVVQHGKRA DSIVRNMLVH SRQGSGEHRP VDINAVMEES LNLAYHGARA ERPAFNVTLQ
RAFDPAAGLV DIYPQEITRV FLNLISNGFY AAAKRKESVA DSFEPILSAA TRSLGDTVEI
RIRDNGTGIP PEVKEKLFNP FFTTKPAGEG TGLGLSMSHD IVVKQHGGTI DVKTEPGIFT
EFIITLPRTM AAGDTAGGKT
//
