ID A0A0Q5ZUM7_9BRAD Unreviewed; 506 AA.
AC A0A0Q5ZUM7;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=ASG57_31445 {ECO:0000313|EMBL:KQT16682.1};
OS Bradyrhizobium sp. Leaf396.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Bradyrhizobium.
OX NCBI_TaxID=1736363 {ECO:0000313|EMBL:KQT16682.1, ECO:0000313|Proteomes:UP000051536};
RN [1] {ECO:0000313|EMBL:KQT16682.1, ECO:0000313|Proteomes:UP000051536}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf396 {ECO:0000313|EMBL:KQT16682.1,
RC ECO:0000313|Proteomes:UP000051536};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQT16682.1, ECO:0000313|Proteomes:UP000051536}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf396 {ECO:0000313|EMBL:KQT16682.1,
RC ECO:0000313|Proteomes:UP000051536};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) 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};
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KQT16682.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LMQJ01000021; KQT16682.1; -; Genomic_DNA.
DR RefSeq; WP_024342867.1; NZ_LMQJ01000021.1.
DR AlphaFoldDB; A0A0Q5ZUM7; -.
DR OrthoDB; 9796100at2; -.
DR Proteomes; UP000051536; Unassembled WGS sequence.
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; 1.
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; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
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:SF49; HISTIDINE KINASE; 1.
DR PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
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; 1.
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); 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 1.
DR PROSITE; PS50112; PAS; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:KQT16682.1};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Transferase {ECO:0000313|EMBL:KQT16682.1}.
FT DOMAIN 14..60
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 89..140
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 160..376
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 394..505
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT MOD_RES 443
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 506 AA; 55137 MW; F3AE86542865A334 CRC64;
MVKKLNQQRD LFESERSFRL LVEGVADYAL YMLDPKGTIT SWNIGGERIK GYSPGEILGQ
HFSRFYTETD RANGKPARAL GIAREKGRYE EEGWRVRKDG TFFWASVVID PIYEDGELIG
FAKITRDITE RRNAQLKLEA MQKQLAESQK FDALGQLTGG VAHDFNNLLM IISGSLHILK
KSATSDPKLE RAMSAIETAT KRGAALTNQL LTFARRQSVN PQAIDFAERV GAIREVLDAG
VGSSVRLAFD IHSDTWPIKA DVSELETALL NLVINARDAM PDGGAVTIQA RNVVLNEPPL
AGDFVAIDVT DTGLGIPSDV LDKIFEPFFT TKPIGKGTGL GLSQVHGFAH QAGGTVKVAS
ELGKGTTFTI LLPRGMDAPV RDAAEAMSFR GSGTVLLVED NPDVALVSTG LLEQLGYEVR
RVADAEAALR EIENDAVDFV FSDIVMPGKM DGLSLAHHLR QIRPGLPILL ATGYSDVAAG
VRGDFPILRK PYEIHELSEA IAKLPR
//
