ID Q89I31_BRADU Unreviewed; 861 AA.
AC Q89I31;
DT 01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT 01-JUN-2003, sequence version 1.
DT 27-MAR-2024, entry version 140.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=bll5808 {ECO:0000313|EMBL:BAC51073.1};
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:BAC51073.1, 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; BAC51073.1; -; Genomic_DNA.
DR RefSeq; NP_772448.1; NC_004463.1.
DR RefSeq; WP_011088552.1; NZ_CP011360.1.
DR AlphaFoldDB; Q89I31; -.
DR STRING; 224911.AAV28_26575; -.
DR EnsemblBacteria; BAC51073; BAC51073; BAC51073.
DR GeneID; 64025577; -.
DR KEGG; bja:bll5808; -.
DR PATRIC; fig|224911.44.peg.5755; -.
DR eggNOG; COG0784; Bacteria.
DR eggNOG; COG4191; Bacteria.
DR HOGENOM; CLU_000445_114_51_5; -.
DR InParanoid; Q89I31; -.
DR OrthoDB; 9796100at2; -.
DR PhylomeDB; Q89I31; -.
DR Proteomes; UP000002526; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 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; 2.
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; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013656; PAS_4.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR NCBIfam; TIGR00229; sensory_box; 1.
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; PF00512; HisKA; 1.
DR Pfam; PF08448; PAS_4; 2.
DR Pfam; PF13426; PAS_9; 1.
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; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000002526};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 26..47
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 54..78
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 476..699
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 741..857
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 792
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 861 AA; 93472 MW; 5F602903E63D0590 CRC64;
MTAETDHDLT REPVAAHEPS PRSGSIALVL LVAAGLVAVA VGLMTLGRAQ AQPYILGILA
VLAMVGLFNL FAFAAGIIRF ADRSLDDPVV GRIADHGFDG LAVTDPRGHV VYSNAAYLTL
TGATSPQDVR PVERVFIGNP DVSEAVFRLL KAAREGKRQQ EEVRISGHDG SQGRWLRMRV
RPLGTGKREA KYAVWSIADI TRDRERQEDV FQELQHAIEY LDHAPCGFFS VNPAGELAYV
NATLANWLDY DLAEIGSGGL KLADIVSGDG ASLLSSIVAV PGEVKTEVFD IDLRMRTGKT
MPVRLYHKLA FGADGAPGPS RTLVISRARD ERSDPDRAAE VRFMRFFDHT PMAIATVDRG
GNVVRANARY AKLAQGLGLD SASKSIFRAI NSRDRHLVIT AINQAAEGKA DIAPVEVALE
GTKERWGQFF VTPVDAAEND AEAAIVHMLE TTERRALENQ INQSQKMETV GQLAGGIAHD
FNNVLSAIMM ANDFLLNAHK PTDPSFQDIM QIKQNATRAA TLVRQLLAFS RRQTLRPQVL
DLGDALSDLT MLLRRLIGEK VKLDLIHGRD LWPVKVDVSQ FEQVIVNLAV NARDAMPDGG
KLIIRTANVA TEDAGKLAYK GMPAADYVRI EVADTGTGIP ADIRDKIFEP FFSTKEVGKG
TGLGLSTVYG IVKQTGGFIY VDSEPGQGTS FHIFLPRHHA EPEVQVEQPA AVVSTANGAA
KEAVPATAEA KPRTDLTGQG TILLVEDEEG LRALNARGLR SRGYTVVEAE NGVEAMEMLE
EQSGAIDLVV SDVVMPEMDG PTLLKAMREK NPDIKFIFVS GYAEDAFEKS LPEGQQFDFL
PKPFTLSQLV AAVKETMTKQ G
//
