ID   Q89SW2_BRADU            Unreviewed;       527 AA.
AC   Q89SW2;
DT   01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT   01-JUN-2003, sequence version 1.
DT   27-MAR-2024, entry version 123.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   OrderedLocusNames=blr2288 {ECO:0000313|EMBL:BAC47553.1};
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:BAC47553.1, 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   -!- SIMILARITY: Belongs to the adenylyl cyclase class-4/guanylyl cyclase
CC       family. {ECO:0000256|RuleBase:RU000405}.
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DR   EMBL; BA000040; BAC47553.1; -; Genomic_DNA.
DR   RefSeq; NP_768928.1; NC_004463.1.
DR   RefSeq; WP_011085076.1; NZ_CP011360.1.
DR   AlphaFoldDB; Q89SW2; -.
DR   STRING; 224911.AAV28_08315; -.
DR   EnsemblBacteria; BAC47553; BAC47553; BAC47553.
DR   GeneID; 64022032; -.
DR   KEGG; bja:blr2288; -.
DR   PATRIC; fig|224911.44.peg.1832; -.
DR   eggNOG; COG2114; Bacteria.
DR   eggNOG; COG3706; Bacteria.
DR   HOGENOM; CLU_000445_110_0_5; -.
DR   InParanoid; Q89SW2; -.
DR   OrthoDB; 315417at2; -.
DR   Proteomes; UP000002526; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004016; F:adenylate cyclase activity; IEA:UniProt.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   GO; GO:0009190; P:cyclic nucleotide biosynthetic process; IEA:InterPro.
DR   CDD; cd07302; CHD; 1.
DR   CDD; cd00082; HisKA; 1.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 3.40.50.2300; -; 1.
DR   Gene3D; 3.30.70.1230; Nucleotide cyclase; 1.
DR   InterPro; IPR001054; A/G_cyclase.
DR   InterPro; IPR018297; A/G_cyclase_CS.
DR   InterPro; IPR011006; CheY-like_superfamily.
DR   InterPro; IPR003661; HisK_dim/P.
DR   InterPro; IPR036097; HisK_dim/P_sf.
DR   InterPro; IPR029787; Nucleotide_cyclase.
DR   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR   PANTHER; PTHR11920:SF335; GUANYLATE CYCLASE 32E; 1.
DR   PANTHER; PTHR11920; GUANYLYL CYCLASE; 1.
DR   Pfam; PF00211; Guanylate_cyc; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF00072; Response_reg; 1.
DR   SMART; SM00044; CYCc; 1.
DR   SMART; SM00388; HisKA; 2.
DR   SMART; SM00448; REC; 1.
DR   SUPFAM; SSF52172; CheY-like; 1.
DR   SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR   SUPFAM; SSF55073; Nucleotide cyclase; 1.
DR   PROSITE; PS00452; GUANYLATE_CYCLASE_1; 1.
DR   PROSITE; PS50125; GUANYLATE_CYCLASE_2; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   3: Inferred from homology;
KW   Lyase {ECO:0000256|RuleBase:RU000405};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002526};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT   DOMAIN          184..300
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   DOMAIN          354..481
FT                   /note="Guanylate cyclase"
FT                   /evidence="ECO:0000259|PROSITE:PS50125"
FT   REGION          70..90
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         233
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   527 AA;  58612 MW;  264BBBD4E06ACAF5 CRC64;
     MSIIDTDSAR AWRIQLAHLR QELQSPVNAL LGYAEILHEE ASRNGRLDIL PDMNRILGAA
     RDLAGKVDRL MDGDRAKSPP GSAATTQEQD LRHELRTPLN AIKGYGEMLR EDAASFSSDS
     LRADFDRLLA AATDLLLRLD RIVRFSVDVE ETSLAPDQTG AVMVSDLMRS LGPVRQYAAT
     ETGSILVVDD IEANRDLLSR RLTRDGHRVS SVAGGQQALQ ALANDEFDLV LLDLMMPDIN
     GLDVLVRMKA DERLRRIPVI MITALAETES AVRCIEAGAE DYLPKPFDPI LLRARINACL
     HKKRWRDREQ KYLRRIEEET AKFERLLLTI LPRQVIGRLN HGEAMIADRF EGVSVLFADL
     VGFTEHSSRV TPAAMVEYLN RLFSEFDALA RELGVEKIKT IGDAYMAVAG LPDPNPDAIA
     AIAKMALGMI DRLGRVNSHF GWPLQIRIGI HSGPVVAGII GAHRFIYDVW GDTVNVASRL
     EAYSLPNRIH VSRDIARHLV GRFALEPRGS IDVKGKGKLE TFFLSRI
//