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Database: UniProt
Entry: X2FE45_9BRAD
LinkDB: X2FE45_9BRAD
Original site: X2FE45_9BRAD 
ID   X2FE45_9BRAD            Unreviewed;       214 AA.
AC   X2FE45;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
DE   Flags: Fragment;
GN   Name=nodV {ECO:0000313|EMBL:AHM97073.1};
OS   Bradyrhizobium sp. CCBAU 43257.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Nitrobacteraceae; Bradyrhizobium.
OX   NCBI_TaxID=1440359 {ECO:0000313|EMBL:AHM97073.1};
RN   [1] {ECO:0000313|EMBL:AHM97073.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CCBAU 43257 {ECO:0000313|EMBL:AHM97073.1};
RX   PubMed=24632260; DOI=10.1128/AEM.00044-14;
RA   Zhang X.X., Guo H.J., Wang R., Sui X.H., Zhang Y.M., Wang E.T., Tian C.F.,
RA   Chen W.X.;
RT   "Genetic divergence of bradyrhizobium strains nodulating soybeans as
RT   revealed by multilocus sequence analysis of genes inside and outside the
RT   symbiosis island.";
RL   Appl. Environ. Microbiol. 80:3181-3190(2014).
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; KF472990; AHM97073.1; -; Genomic_DNA.
DR   AlphaFoldDB; X2FE45; -.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR   CDD; cd00130; PAS; 1.
DR   Gene3D; 2.10.70.100; -; 1.
DR   Gene3D; 3.30.450.20; PAS domain; 2.
DR   InterPro; IPR001610; PAC.
DR   InterPro; IPR000014; PAS.
DR   InterPro; IPR000700; PAS-assoc_C.
DR   InterPro; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR013767; PAS_fold.
DR   NCBIfam; TIGR00229; sensory_box; 1.
DR   PANTHER; PTHR43304:SF1; PAC DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR43304; PHYTOCHROME-LIKE PROTEIN CPH1; 1.
DR   Pfam; PF00989; PAS; 2.
DR   SMART; SM00086; PAC; 1.
DR   SMART; SM00091; PAS; 2.
DR   SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 2.
DR   PROSITE; PS50113; PAC; 2.
DR   PROSITE; PS50112; PAS; 1.
PE   4: Predicted;
FT   DOMAIN          1..21
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          96..147
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          148..214
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:AHM97073.1"
FT   NON_TER         214
FT                   /evidence="ECO:0000313|EMBL:AHM97073.1"
SQ   SEQUENCE   214 AA;  24524 MW;  5F0998D3243145C9 CRC64;
     VILMACEDIT ERKQTELALQ RSEAHLAHAQ ELSHTGSFSW NASTGEAFWS KETFRIFQID
     LQTTPAPQLV IERTHPDDRA SVKEIIDEAM RDLRDFEHEY RLLLPDGSVK HIHAQARVTR
     TASGEIEFVG AATDITAARR AEQQLRRSEA YLAEAQHLTH TGSWSWDVHT RDFVYRSAEV
     DRLFGFNPQE PVSLETIRSR IHPEDLPGLQ EVQR
//
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