ID   A0A0X8CDQ8_9BRAD        Unreviewed;       618 AA.
AC   A0A0X8CDQ8;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=BCCGELA001_04415 {ECO:0000313|EMBL:AMA55590.1};
OS   Bradyrhizobium sp. CCGE-LA001.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Nitrobacteraceae; Bradyrhizobium.
OX   NCBI_TaxID=1223566 {ECO:0000313|EMBL:AMA55590.1, ECO:0000313|Proteomes:UP000019052};
RN   [1] {ECO:0000313|EMBL:AMA55590.1, ECO:0000313|Proteomes:UP000019052}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCGE-LA001 {ECO:0000313|EMBL:AMA55590.1,
RC   ECO:0000313|Proteomes:UP000019052};
RX   PubMed=24952318; DOI=10.1016/j.ympev.2014.06.006;
RA   Servin-Garciduenas L.E., Zayas-Del Moral A., Ormeno-Orrillo E., Rogel M.A.,
RA   Delgado-Salinas A., Sanchez F., Martinez-Romero E.;
RT   "Symbiont shift towards Rhizobium nodulation in a group of phylogenetically
RT   related Phaseolus species.";
RL   Mol. Phylogenet. Evol. 79:1-11(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; CP013949; AMA55590.1; -; Genomic_DNA.
DR   RefSeq; WP_008543064.1; NZ_CP013949.1.
DR   AlphaFoldDB; A0A0X8CDQ8; -.
DR   STRING; 1223566.BCCGELA001_04415; -.
DR   KEGG; brc:BCCGELA001_04415; -.
DR   Proteomes; UP000019052; 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   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 3.40.50.2300; -; 2.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
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; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
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; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
PE   4: Predicted;
KW   Kinase {ECO:0000313|EMBL:AMA55590.1}; Membrane {ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Transferase {ECO:0000313|EMBL:AMA55590.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           26..618
FT                   /note="histidine kinase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5007793697"
FT   TRANSMEM        343..365
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          400..616
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
SQ   SEQUENCE   618 AA;  67820 MW;  7196E781F49446CE CRC64;
     MRILSGLTRI LIVCLFVNLS HQCIAADGPR QRSILVLEEA DFRSPFYLEI FTGISAAAKQ
     NGKFPTVIYG ESLDLARFPG PDYEESLVGH LKSKYAQRQI DVIVSIGVAS AKFLQTRKQE
     IWPTAPVVYG FVPDLPETRA LFLPDTTAIF ARVRPTHLLT AARAIVPDLT HVVLVGGAWK
     NPLVYGQWKQ DFAAAMPGLE VTDLSDAPLR EVRKQVASLP ARSAILTSAM YSDGEGTYYS
     PAAALARVAE SANRPIVITS DTFLGRSGVG GFLLLPDSIG REAGEVAMRV LGGEAPSSIP
     PFNGDNVKPI FDGRQLKRWN VDEANLPAGS QVRFRELSFW ERYYWHTTIA GSVMLVQALM
     IATLLRERRL RFLAQVEAGQ RMSELAHMNR RATAGQMSAS IAHELSQPLA AIMINAEAGA
     QALQHPSPDL GELRDILDHI RRDDQRASEV INWLRSFLKK EQTEPRELDF NVTVREVFQF
     LSVQAVARKV ELATEASSSD IRVKGDKVQL QQAILNLVVN GMDAVAHLPA DRRRVLGRTS
     LVEGNRAHLS IADAGDGILA EKTTEIFKPF FTTKAQGMGI GLSIARTIIE THGGRIWAEN
     VPSGGAVFHV SLPLAAQR
//